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Synthyra 5

A0A2N6JFX7

TRTA_HERS1

MIRIDATPYPYQFHPRSTALVVIDMQRDFIEEGGFGSALGNDVRPLAAIVPTVAALLQLAREAGMLVVHTRESHLPDLSDCPRSKRLRGNPTLGIGDVGPMGRILVQGEPGNQILPQLAPVEGELVIDKPGKGAFYATDLHAQLQERRITHLLVAGVTTEVCVQTSMREANDRGYECLVIEDACASYFPDFHRITLEMLTAQGGIVGWRTPLAQLQAGVAAYTGENP

3.5.1.-

amide catabolic process [GO:0043605]

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]

PF00857;

3.40.50.850;

Isochorismatase family

CATALYTIC ACTIVITY: Reaction=H2O + triuret = 1-carboxybiuret + NH4(+); Xref=Rhea:RHEA:75199, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:36955, ChEBI:CHEBI:142864; Evidence={ECO:0000269|PubMed:33172891};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for triuret (at pH 6.5 and 25 degrees Celsius) {ECO:0000269|PubMed:33172891}; Note=Catalytic efficiency, kcat/KM, is 5.3 X 10(5) M(-1)sec(-1). {ECO:0000269|PubMed:33172891};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:33172891};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The melting temperature (Tm) is 65 degrees Celsius. {ECO:0000269|PubMed:33172891};

FUNCTION: Involved in the degradation of triuret (carbonyldiurea), an impurity in agricultural urea fertilizer, and an intermediate of uric acid oxidation endogenously found in human urine and in prokaryotic metabolism. Catalyzes the hydrolysis of triuret to 1-carboxybiuret and ammonia. The product, carboxybiuret, channels into biuret metabolism and is spontaneously decarboxylated to biuret. Extremely specific for triuret with four, three and two orders of magnitude less activity with biuret, 1-nitrobiuret and formylurea, respectively. No activity with tetrauret, pentauret or nonplanar compounds methylene diurea or succinamide. {ECO:0000269|PubMed:33172891}.

Herbaspirillum sp. (strain BH-1)

A0A2P1GIW2

CS_CATRO

MNSSTDPTSDETIWDLSPYIKIFKDGRVERLHNSPYVPPSLNDPETGVSWKDVPISSQVSARVYIPKISDHEKLPIFVYVHGAGFCLESAFRSFFHTFVKHFVAETKVIGVSIEYRLAPEHLLPAAYEDCWEALQWVASHVGLDNSGLKTAIDKDPWIINYGDFDRLYLAGDSPGANIVHNTLIRAGKEKLKGGVKILGAILYYPYFIIPTSTKLSDDFEYNYTCYWKLAYPNAPGGMNNPMINPIAENAPDLAGYGCSRLLVTLVSMISTTPDETKDINAVYIEALEKSGWKGELEVADFDADYFELFTLETEMGKNMFRRLASFIKHE

4.-.-.-

alkaloid metabolic process [GO:0009820]

cytosol [GO:0005829]; nucleus [GO:0005634]

hydrolase activity [GO:0016787]; lyase activity [GO:0016829]

PF07859;

3.40.50.1820;

'GDXG' lipolytic enzyme family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. Nucleus {ECO:0000269|PubMed:29724909}.

CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate = acetate + catharanthine + H(+); Xref=Rhea:RHEA:58580, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:142675, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58581; Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};

PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102}.

FUNCTION: Component of iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis pathway from 19E-geissoschizine. Catalyzes the conversion of O-acetylstemmadenine (OAS) to catharanthine. {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}.

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

A0A2P1GIW3

TS_CATRO

MGSSDETIFDLPPYIKVFKDGRVERLHSSPYVPPSLNDPETGGVSWKDVPISSVVSARIYLPKINNHDEKLPIIVYFHGAGFCLESAFKSFFHTYVKHFVAEAKAIAVSVEFRLAPENHLPAAYEDCWEALQWVASHVGLDISSLKTCIDKDPWIINYADFDRLYLWGDSTGANIVHNTLIRSGKEKLNGGKVKILGAILYYPYFLIRTSSKQSDYMENEYRSYWKLAYPDAPGGNDNPMINPTAENAPDLAGYGCSRLLISMVADEARDITLLYIDALEKSGWKGELDVADFDKQYFELFEMETEVAKNMLRRLASFIK

4.-.-.-

alkaloid metabolic process [GO:0009820]

cytosol [GO:0005829]; nucleus [GO:0005634]

hydrolase activity [GO:0016787]; lyase activity [GO:0016829]

PF07859;

3.40.50.1820;

'GDXG' lipolytic enzyme family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. Nucleus {ECO:0000269|PubMed:29724909}.

CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate = (-)-tabersonine + acetate + H(+); Xref=Rhea:RHEA:58584, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57893, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58585; Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909};

PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}.

FUNCTION: Component of iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis pathway from 19E-geissoschizine. Catalyzes the conversion of O-acetylstemmadenine (OAS) to tabersonine, a precursor of vindoline. {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}.

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

A0A2R2JFI5

OPHMA_OMPOL

METSTQTKAGSLTIVGTGIESIGQMTLQALSYIEAAAKVFYCVIDPATEAFILTKNKNCVDLYQYYDNGKSRLNTYTQMSELMVREVRKGLDVVGVFYGHPGVFVNPSHRALAIAKSEGYRARMLPGVSAEDCLFADLCIDPSNPGCLTYEASDFLIRDRPVSIHSHLVLFQVGCVGIADFNFTGFDNNKFGVLVDRLEQEYGAEHPVVHYIAAMMPHQDPVTDKYTVAQLREPEIAKRVGGVSTFYIPPKARKASNLDIIRRLELLPAGQVPDKKARIYPANQWEPDVPEVEPYRPSDQAAIAQLADHAPPEQYQPLATSKAMSDVMTKLALDPKALADYKADHRAFAQSVPDLTPQERAALELGDSWAIRCAMKNMPSSLLDAARESGEEASQNGFPWVIVVGVIGVIGSVMSTE

2.1.1.-

methylation [GO:0032259]

methyltransferase activity [GO:0008168]

PF00590;

Precorrin methyltransferase family

PTM: OphMA automethylates at Val-401, Val-403, Val-404, Gly-405, Val-406, Ile-407, Gly-408, Ile-410, Gly-411 and Val-413 before being processed by the prolyloligopeptidase ophP which likely forms a peptidyl ester upon removal of the follower propeptide, which then undergoes macrocyclization with the N-terminus of the modified core peptide (PubMed:28715095, PubMed:30151425, PubMed:32491837, PubMed:33574430, PubMed:36220874). Peptide backbone alpha-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides (Probable). {ECO:0000269|PubMed:28715095, ECO:0000269|PubMed:30151425, ECO:0000269|PubMed:32491837, ECO:0000269|PubMed:33574430, ECO:0000269|PubMed:36220874, ECO:0000305}.

PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28715095, ECO:0000269|PubMed:30151425, ECO:0000269|PubMed:32491837}.

FUNCTION: Fusion protein of the methyltransferase ophM and the omphalotin core peptide; part of the gene cluster that mediates the biosynthesis of omphalotin A, a highly methylated cyclic dodecapeptide with nematodicidal activity (PubMed:28715095, PubMed:30151425, PubMed:32491837, PubMed:33574430). Omphalotin A derives from the C-terminus of the ophMA protein, and it is the ophMA protein that methylates its own C-terminus using S-adenosyl methionine (SAM) (PubMed:28715095, PubMed:30151425, PubMed:32491837, PubMed:33574430). The C-terminus is subsequently cleaved off and macrocyclized by the prolyloligopeptidase ophP to give the final product (PubMed:28715095, PubMed:30151425, PubMed:32491837). {ECO:0000269|PubMed:28715095, ECO:0000269|PubMed:30151425, ECO:0000269|PubMed:32491837, ECO:0000269|PubMed:33574430}.

Omphalotus olearius (Jack o'lantern)

A0A2R4QKX7

TPS3_PIPNI

MGFSFVTNAAIAAHMPPSKQEIIRRDAKFHPTIWGDHFIQYLDTPIDPPQKVVERMEELKKQVRAMLRDTNLDISLIDWIQRTGIAYHFEEQIAETLKHVYEASTLTTDSSKYLEHFDLRHIALRFRLSRQQGYHASTDVFKRFMDEGDKFKQSIANDIEGMLSLYEASFMSVKGEAILDEALAFTGKNLEATLPNLTGSLAQQVECALEIPLRRCTDLVKARRSISCYENKNGRNEVVLELAKLDFNLLQAVHQRELALLTSWWNELGASTNLPFTRNRVVELYFWVLEVLSKPEHARAREIMVKSIIMASILDDVYDVYGTLEELQLFTSALERWDLQALEQLPNTIKTAYSIVLRVFKEYEDLLKPHEVYRVGFARKALIPYMNAYFLEAKWFYSHHHPSFEEYMDNALVSCGYPFLFLVSLVGLDEIATKDVFEWAIKRPNIVVAASMICRNRDDIVGHKEEQERGDVPSGVECYTKDHGCTEEEACMALQAMVDDAWKDINCELLHDTSMPKAILMRAVGLARIISILYQYRDGYSDSTHETKAHVTQVLVQPIPL

4.2.3.-; 4.2.3.133

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7};

alpha-copaene biosynthetic process [GO:1901931]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762]

alpha-copaene synthase activity [GO:0102877]; germacrene-D synthase activity [GO:0052577]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

PF01397;PF03936;

1.10.600.10;1.50.10.130;

Terpene synthase family, Tpsa subfamily

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene D; Xref=Rhea:RHEA:68716, ChEBI:CHEBI:33019, ChEBI:CHEBI:49045, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68717; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate; Xref=Rhea:RHEA:33991, ChEBI:CHEBI:10221, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.133; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33992; Evidence={ECO:0000269|PubMed:29248443};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.152 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.185 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}.

FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into alpha-copaene and germacrene D (PubMed:29248443). {ECO:0000269|PubMed:29248443}.

Piper nigrum (Black pepper)

A0A2R6W0K6

PGMP1_MARPO

MAFSAAASASTNLVPAVASGRGGAAASASQHGETARLARFGVSSSACANALSLSSSRSCASMGEVLWANGGAVRLAARRTLRVRAAGAGTIVQPEGFQITSVPTTPIDGQKTGTSGLRKKVKEFQSPNYLANWIQALFDSLPAEDVKGSTLVLGGDGRYFNKEASQIIIKIAAGNGVGKILVGREGIASTPAVSAIIRARKANGGFVMSASHNPGGPKYDWGIKFNYSSGQPAPESITDKIYGNTLSIKEIKQADIPDVNLSELGVHKFGDFSVEVIDPVADYLNLLEEVFDFDLLKGLLTSKDFRFKFDAMHAVTGAYAKPIFVDRLGAPEDSIFNGVPLEDFGGGHPDPNLTYAEELVKIMYGTDAPDFGAASDGDGDRNMILGNHFFITPSDSVAMIAANADAIPYFKTGLKGLARSMPTSGALDRVAKELGLPFFETPTGWKFFGNLMDAGKCSVCGEESFGTGSDHVREKDGIWAVLAWISIVAYKNRDRKVGEKLVTVADIAKEHWAKYGRNFFSRYDYEECESAGANKMVEHLRDIIAKSKKGDKYGNYELELADDFAYTDPIDGSVATKQGIRFIFSDGSRIIFRLSGTGSAGATIRIYVEQYEQDTTKHDLDAQDALKPLIDIALSVSKLQEFTGRTKPTVIT

5.4.2.2

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00949}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949};

carbohydrate metabolic process [GO:0005975]; detection of gravity [GO:0009590]; glucose metabolic process [GO:0006006]; response to cold [GO:0009409]; starch biosynthetic process [GO:0019252]; sucrose biosynthetic process [GO:0005986]

chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; stromule [GO:0010319]

magnesium ion binding [GO:0000287]; phosphoglucomutase activity [GO:0004614]

PF02878;PF02879;PF02880;

3.40.120.10;3.30.310.50;

Phosphohexose mutase family

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:Q9SCY0}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]; Xref=Rhea:RHEA:68748, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58392, ChEBI:CHEBI:58601, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:Q9SCY0}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = alpha-D-glucose 6-phosphate + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:68752, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58225, ChEBI:CHEBI:58392, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:Q9SCY0};

FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (By similarity). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (By similarity). This enzyme participates in both the breakdown and synthesis of glucose (By similarity). Required for sucrose production and accumulation necessary during plant development (PubMed:31851335). Promotes gravitropic responses, negative in shoots but positive in roots, by facilitating starch granules (statoliths) formation (By similarity). {ECO:0000250|UniProtKB:P36871, ECO:0000250|UniProtKB:Q9SCY0, ECO:0000269|PubMed:31851335}.

Marchantia polymorpha (Common liverwort) (Marchantia aquatica)

A0A2R6XIK6

PRAF_MARPO

MVVREAMIVPQTVQGGGKGVNGCSLVSNYQNSRDLCLQSAAMEQKSKGVIENCNLGPHDVGVGWKRNSSEGSISSMDSLPCGETVFSPSDPHNSVFRKPRRLGVSESDDESVIDQSQEESLLRKSKRSVMGGTVQPHSAMAQSVDEAAPDHSSTPSDDGKDFPSSRVKFMCSFGGKILPRPSDQQLRYVGGQTRIIGINRDVNFSELRNKMRESFGQCYTFKYQLPDEDLDALVTVSSDEDLENMMEEYDKLEADGSSRLRVFLFPADQDATSFDIDSTGDLRNSEQRYVDAVNGIAESSTRRISDGVLGASPVSSDLLGLELSEPSWGLARGPDAVPMAMLATHHDPNLIHQVPVAHPVSALTGNLSNRSNAPSAPSSAPSSPPLLARNLHGKLPLVGELHQFQYLQDSQFKGVGPQYTGMPSEVAHQDSESYGGSGGSSAASQHEMHYRSTDSRRGPESPPKKFHDALHQDHPITVEQRRLSGTKMPRIGSHGKLTRLSEHSELAPSSRVDSQQMPDIHMAPGELQRLFPQQVPLQQTLWPHAMDTQQDSYRRPDMLQSSGAQPAVSGQQQQGYQPQQQLQHLFRSGLSQTGANHEGAYRQGDQQQQSQQFQEDLHVNPNYIPRSVSSHAIAAGIAAGQSTSYHGSAPSSPRPGFRELPSRHLPGGPQLQHQWTFNGAGYVDQGFGRRVMNYPDQATRSFRLSSSPPRYRDHHPHSEERLHRQAQQVSEPLHHEQVPVSGQLKFETNSVSQAQYDLVPRPQVPQYKGHNPFQEKITSFQDHQEVGDIRRHVLQQGKDNQLLAGQQHLHSILQPQRIDYQESLKQQGDQSIPIHPRFQDGQEKVAEWMVQERALEEEEARKRVLGRIRQAELEEEAAAEAVVSQHKDTHQGVYAGLHLPNDEDLLTSSLGDYPSGNRRNERLESSISNAFPFRHLPPSVLGGYTAPKSRVNPTETSHVAQYVSRPVDTDYLAVAGLRGGGNGQDMRSAALFEVNGLQQTSGYQMPSGPHRLMEERLMPSAFNPITQLQKLRINDNLALNNDMRWSGSEDVRNEPSIPARDRMGGIYEDHHQGLPGLTLGRSAGKLSRPSSNTSIPNLLDETIGEGSLLPSGPSYGTQAQGTNLIDITQSISAIDNPLYSTSYASRLSNTSLGLDSPLVTSGGMLNSSLEGTSFSDYYKIKMGDDLPNAKMPSSKIPSAEDNLSRSSSSSLSELSKSGSEDGLGGQLTMDQRTVDMVVAALDLDRSGSVVQSVLESSDAKEASLSESVHDHSLGKLGSVVGSVGTQSVWPLDSAPTLAAGLWEKKLDEAGMTEETFERHITSDGTTFEELTADDHEVLASTVDKENQEEVRTGLDEPADEDKANSTGLGSDPAAKAIARGLQTIKNADLEELRELGSGTFGTVYHGKWRGTDVAIKRIKASCFAGRPSEQERLIEDFWREACNLGHLHHPNVVAFYGVVADGPGGTLATVTEYMVNGSLKQVLQKKDRTIDRRKRLLIAMDAAFGMEYLHGKNIVHFDLKCENLLVNMRDPHRPICKVGDLGLSKVKHQTMVSGGVRGTLPWMAPELLNGNSSLVTEKVDVFSFGIVMWELLTGEEPYDKMHYGAIIGGIVNNTLRPLIPSWCDPAWRSLMERCWANEPAVRPSFSDIAKELRTMAAALQPKTQAQTQGQSHPHPQMQIV

2.7.11.1

cellular response to auxin stimulus [GO:0071365]; phosphorylation [GO:0016310]; regulation of auxin mediated signaling pathway [GO:0010928]; regulation of photosynthesis [GO:0010109]; response to absence of light [GO:0009646]; response to auxin [GO:0009733]; response to blue light [GO:0009637]; response to red light [GO:0010114]; signal transduction [GO:0007165]; sucrose metabolic process [GO:0005985]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]

PF00564;PF07714;

1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family

PTM: Hyperphosphorylated in response to auxin (PubMed:38128538). Its phosphorylation state is also rapidly stimulated by photosynthetic activity (e.g. in response to blue light and red light irradiation); dephosphorylated in the darkness (PubMed:31851335). {ECO:0000269|PubMed:31851335, ECO:0000269|PubMed:38128538}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:38128538}. Note=Broadly distributed to both membrane-associated and intracellular punctate structures. {ECO:0000269|PubMed:38128538}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};

FUNCTION: RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming (PubMed:38128538). Required for general growth and developmental process (PubMed:31851335, PubMed:38128538). Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1 (PubMed:31851335). Necessary for optimal chloroplast electron transport rate (ETR) (PubMed:31851335). {ECO:0000269|PubMed:31851335, ECO:0000269|PubMed:38128538}.

Marchantia polymorpha (Common liverwort) (Marchantia aquatica)

A0A2R8Q1W5

KEP1B_DANRE

MTECKAEVTPSASNGHRVFSYTLESHTAAAFAIMNELRRERQLCDVTLRVRYCPLDTHVDFVAHKVVLASSSPVFRAMFTNGLKECGMEVVPIEGIHPKVMGRLIEFAYTASISVGEKCVIHVMNGAVMYQIDSVVQACCDFLVEQLDPSNAIGIASFAEQIGCTELHQKAREYIYMNFSQVATQEEFFTLSHCQLVTLISRDELNVRCESEVFHACVAWVQYDREERRPYVQALLQAVRCHSLTPHFLQRQLEHFEWDAQSKDYLSQIFRDLTLHKPTKVIPLRTPKVPQLIYTVGGYFRQSLSFLEAFNPCSGAWLRLADLQVPRSGLAACVISGLLYAVGGRNNGPDGNMDSHTLDCYNPMNNCWRPCAHMSVPRNRIGVGVIDGMIYAVGGSHGCTHHNSVERYDPERDSWQLVSPMLTRRIGVGVAVINRLLYAVGGFDGTHRLSSAECYNPERDEWRSIAAMNTVRSGAGVCALGNYIYVMGGYDGTNQLNTVERYDVEKDSWSFSASMRHRRSALGVTTHHGRIYVLGGYDGNTFLDSVECFDPETDSWTEVTHMKSGRSGVGVAVTMEPCHKELIPCQC

cellular response to oxidative stress [GO:0034599]; cellular response to prostaglandin stimulus [GO:0071379]; cellular response to xenobiotic stimulus [GO:0071466]; protein ubiquitination [GO:0016567]; regulation of autophagy [GO:0010506]; ubiquitin-dependent protein catabolic process [GO:0006511]

cytoplasm [GO:0005737]; inclusion body [GO:0016234]; nucleus [GO:0005634]

PF07707;PF00651;PF01344;

1.25.40.420;2.120.10.80;

KEAP1 family

PTM: Non-enzymatic covalent modifications of reactive cysteines by electrophile metabolites inactivate the BCR(KEAP1) complex. {ECO:0000250|UniProtKB:Q9Z2X8}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2X8}. Nucleus {ECO:0000250|UniProtKB:Q9Z2X8}. Note=Mainly cytoplasmic. {ECO:0000250|UniProtKB:Q9Z2X8}.

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9Z2X8}.

FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting nfe2l2/nrf2 for ubiquitination (PubMed:18057000). Keap1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of nfe2l2/nrf2, a transcription factor regulating expression of many cytoprotective genes (PubMed:18057000). In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting nfe2l2/nrf2 nuclear accumulation and expression of phase II detoxifying enzymes (By similarity). {ECO:0000250|UniProtKB:Q9Z2X8, ECO:0000269|PubMed:18057000}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A2R8QCI3

DAPLE_DANRE

MDITVSELMSNFMDSPLVVWVKTFGPLGFSSEDKLSMFMDLVDGVFLHKIMTHIDPSPMNQRVNKQVNNDVNLRIQNLNTVIRHIKNYYQEHLQQLIVMNLPNVLAIAKDPLSGKSMEEMKRMLLLILGCAVQCDRKEEIIEKIKLLDIETQAAIVTHIQEVTHNQENVLDLQWMEVAEIPAEQLDPLSRTMAFHLRKLIDERDESAELVIELTQERDYLQSQQPSGLLGFPSPERTSLSPITLLSKEDRQHLAVELADTKAKLRRSRQELEEKTEQLIDAKNEIERLDSDIQKLKQENTQLLAEARSVRAYRDEVDSLRERAGKVDRLETELSRFKEKLNDVHFYKTRIEELREDNLTLLETKSMLEEQLTGARGRCDKLHELEKENLQLRSKLHDIEIDRDSDKKRLEELLEENMLLEISQKQSMNESAHLGWELEQLAKNNEVNEARKSFVFELNESASSRLLKLEKENQCLQSTIQELREASINMEEGQLHSLELEKENQSLSKKLERLQSQLDQEKQTTQDMENLGEELIKEKQRMEKTLETIQAEKDRQISELEQEKEHLTQAVSSLRKRAQANSEARVREVETENRILHQTISETGGKLARLEAEKRQVTKELESLRERGERCEELEREVPRLERVREQLQREAAALKIGSERAEALERENATLEQDNRRLKKLADTAQNATLRLAVLEKDHQQLEEENLEQRRALETLRPAAARLAQLQQEHAELEREHEEMCRTMEELRSQAKRSERLEKSCGSLSLENQRLQQTLENSSTKMQGLESELRQNEAEMKDLQRELEGLRQKVTWAETLEKENRGMEQELSQLEKEKKQLEKEARRFRQQLEVKEAALEENCLRLASMEKEGTALSKELGRVKEAAGRLKELERENKDLQKQATMDKKTLATLREELVNEKLRVQQQCNELEKLSHELEKIGLNREKLLQEEHSCEDNKYKILETKIESALKKTLELREEKIQSLESRLEESSSLNQQLRTELTTVKKNLEALKQRHEEEAAHSEISQQTLGQTRSLPDKEKWEMEQREATAELLKLKDRLIDVEKNVRQRHVSIDIHRVIFSIVICFCDSLQNAALQTEKYLLKDQLKQIDSQNAQLNAQTLALQKQAASLQEHNTSLHKETAKLQVENSTLSSQSSSLMAQYGALQAQLQTLESEAESLQKQREEASAARDRVTQDHERLLGVHERQASEYEQLIAQHAALKASQRALEQENRTLENKYMVLLKQKDAMEALEESLQRDRESLGEEIRKNTLILGENRSLREEVDRVSHMHTQLRQEYDSLQLQTKELKTSLNESQLELNRWQARYDQLKEQHQGLDISMTKLDNHCELLTRLKGNLEEENHHLLSQIQMLSQQNQTLLERTMESKELYHEEQKQYIDKLNSLRRQKEKLEEKIMDQYKFYDPTPKKSRQWVGAKAIAKFIKPKKESSRERPDAPRERIRSAPDIPLPEIPTCIDCPESAPPPPPPPLPPRQSRPSLDSMNSQSVEENHVQSPTLSSPALNGRVLNESGGSRSRDGYRSIGGGSESMNGYEELLRWRSREPGGATCSTPLSRNSHNAPGFTSSSSLRPGRRPKGLVSEEDLRHHSPDAGFGSGVHGNTGHRPSSAEFSRNTSSSNSPVSSKGSLDCLQGRSASLSSDDVVGLAHEGSRLSQSSLLPRSSTLPCDSPSASRPSQRPASRRPSSPGSEMVTLEEFLQESNALSPPTVQTGSREDLMTDYFTRSTRPVPLRDGAKTPTNYVTPTVKTTPPELDARTPKPGHSVKPSVRLTDTSTPPSHSQTLPNRGAGLRPSALQQSSPRGSVGGSASLSRTFSLASADLLRSNGPDSYRTEAASPNQNDVVMRRPGAVARERPMSARVTGSSPLPGDPGHISVDPRRLSLAQPRDEFSLVSPPPLHSSSMSLQAEREYVGSGSSRAGAARSGSAQPRGAPHRGEVAMVTPVRAVPALRLNDLEEEPQEQREAESPLLKKADTTNLSYASKEQPTSKPASPDPNNDPQTVWYEYGCV

apical constriction [GO:0003383]; cytoplasmic microtubule organization [GO:0031122]; cytoskeleton-dependent intracellular transport [GO:0030705]; neural tube formation [GO:0001841]; small GTPase-mediated signal transduction [GO:0007264]; Wnt signaling pathway [GO:0016055]

anchoring junction [GO:0070161]; cell junction [GO:0030054]; centrosome [GO:0005813]; cytoplasm [GO:0005737]

dynein light intermediate chain binding [GO:0051959]; G-protein alpha-subunit binding [GO:0001965]; guanyl-nucleotide exchange factor activity [GO:0005085]; microtubule binding [GO:0008017]

PF19047;

1.10.287.1490;6.10.250.3110;1.10.418.10;

CCDC88 family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. Cell junction {ECO:0000250|UniProtKB:Q9P219}. Note=Enriched at apical cell junctions. {ECO:0000250|UniProtKB:Q9P219}.

FUNCTION: Positive regulator of Wnt signaling, acting synergistically with dvl2 (By similarity). Functions upstream of ctnnb1/beta-catenin in the canonical Wnt pathway, and also activates jnk in the Wnt/planar cell polarity (PCP) pathway (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha (Gi-alpha) subunits (PubMed:30948426). This promotes apical cell constriction and subsequent bending of the neural plate during neurulation via arhgef18 (By similarity). {ECO:0000250|UniProtKB:P85120, ECO:0000269|PubMed:30948426}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A2R8VHR8

DT3UO_MOUSE

MLKMSGWQRQSQNNSRNLRRECSRRKCIFIHHHT

artery development [GO:0060840]; cell redox homeostasis [GO:0045454]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER overload response [GO:0006983]; gene expression [GO:0010467]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy in response to ER overload [GO:0034263]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of autophagy [GO:0010506]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to endoplasmic reticulum stress [GO:0034976]; response to platelet-derived growth factor [GO:0036119]; response to wounding [GO:0009611]; sensory perception of sound [GO:0007605]; vascular associated smooth muscle cell migration [GO:1904738]; vascular associated smooth muscle cell proliferation [GO:1990874]

CHOP-ATF3 complex [GO:1990622]; CHOP-ATF4 complex [GO:1990617]; CHOP-C/EBP complex [GO:0036488]; cytoplasm [GO:0005737]; late endosome [GO:0005770]; nucleus [GO:0005634]

DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6Z9}. Cytoplasm {ECO:0000250|UniProtKB:Q9H6Z9}. Note=Colocalizes with WDR83 in the cytoplasm. {ECO:0000250|UniProtKB:Q62630}.

FUNCTION: [Isoform AltDDIT3]: Product of the upstream open reading frame (uORF) of DDIT3/CHOP that is specifically produced in absence of stress, thereby preventing translation of downstream stress effector DDIT3/CHOP. {ECO:0000269|PubMed:21285359}.

Mus musculus (Mouse)

A0A2R9YJI3

GPR22_DANRE

MESMPSSLTHQRFGLLNKHLTRTGNTREGRMHTPPVLGFQAIMSNVTVLDNIEPLDFEMDLKTPYPVSFQVSLTGFLMLEIVLGLSSNLTVLALYCMKSNLVSSVSNIVTMNLHVLDVLVCVGCIPLTIVVVLLPLEGNNALICCFHEACVSFASVATAANVLAITLDRYDISVRPANRVLTMGRAVALLGSIWALSFFSFLVPFIEEGFFSQAGNERNQTEAEEPSNEYYTELGLYYHLLAQIPIFFFTAVVMLVTYYKILQALNIRIGTRFHSVPKKKPRKKKTISMTSTQPESTDASQSSAGRNAPLGMRTSVSVIIALRRAVKRHRERRERQKRVFRMSLLIISTFLLCWTPITVLNTVILSVGPSNFTVRLRLGFLVMAYGTTIFHPLLYAFTRQKFQKVLKSKMKKRVVSVVEADPMPNNVVIHNSWIDPKRNKKVTFEETEVRQKCLSSEDVE

cell projection organization [GO:0030030]; cellular response to hormone stimulus [GO:0032870]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; determination of left/right symmetry [GO:0007368]; determination of liver left/right asymmetry [GO:0071910]; G protein-coupled receptor signaling pathway [GO:0007186]; heart looping [GO:0001947]; Kupffer's vesicle development [GO:0070121]

plasma membrane [GO:0005886]

G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277]

PF00001;

1.20.1070.10;

G-protein coupled receptor 1 family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D4A3U0}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Orphan G-protein coupled receptor that regulates cilia length and structure in the Kupffer's vesicle leading to the left-right asymmetry development by establishing a directional fluid flow. {ECO:0000269|PubMed:25335082}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A2S1XB67

ASO_CATRO

MIKKVPIVLSIFCFLLLLSSSHGSIPEAFLNCISNKFSLDVSILNILHVPSNSSYDSVLKSTIQNPRFLKSPKPLAIITPVLHSHVQSAVICTKQAGLQIRIRSGGADYEGLSYRSEVPFILLDLQNLRSISVDIEDNSAWVESGATIGEFYHEIAQNSPVHAFPAGVSSSVGIGGHLSSGGFGTLLRKYGLAADNIIDAKIVDARGRILDRESMGEDLFWAIRGGGGASFGVIVSWKVKLVKVPPMVTVFILSKTYEEGGLDLLHKWQYIEHKLPEDLFLAVSIMDDSSSGNKTLMAGFMSLFLGKTEDLLKVMAENFPQLGLKKEDCLEMNWIDAAMYFSGHPIGESRSVLKNRESHLPKTCVSIKSDFIQEPQSMDALEKLWKFCREEENSPIILMLPLGGMMSKISESEIPFPYRKDVIYSMIYEIVWNCEDDESSEEYIDGLGRLEELMTPYVKQPRGSWFSTRNLYTGKNKGPGTTYSKAKEWGFRYFNNNFKKLALIKGQVDPENFFYYEQSIPPLHLQVEL

1.21.3.-

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O64743};

alkaloid metabolic process [GO:0009820]

endoplasmic reticulum [GO:0005783]; vacuole [GO:0005773]; vesicle [GO:0031982]

FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]

PF08031;PF01565;

3.30.465.10;3.40.462.20;3.30.43.10;

Oxygen-dependent FAD-linked oxidoreductase family

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:29724909}. Vacuole {ECO:0000269|PubMed:29724909}. Vesicle {ECO:0000269|PubMed:29724909}. Note=First targeted to endoplasmic reticulum (ER) and progressively secreted to vacuole by ER-derived vesicles. {ECO:0000269|PubMed:29724909}.

CATALYTIC ACTIVITY: Reaction=O-acetyl-15alpha-stemmadenine + O2 = H2O2 + precondylocarpine acetate; Xref=Rhea:RHEA:58572, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:142673, ChEBI:CHEBI:142769; Evidence={ECO:0000269|PubMed:29724909, ECO:0000269|PubMed:30256480}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58573; Evidence={ECO:0000269|PubMed:29724909, ECO:0000269|PubMed:30256480};

PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29724909, ECO:0000269|PubMed:30256480}.

FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts O-acetylstemmadenine (OAS) to reactive acetylated intermediates, likely dihydroprecondylocarpine acetate. {ECO:0000269|PubMed:29724909, ECO:0000269|PubMed:30256480}.

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

A0A2S3R7M0

MARTX_VIBVL

MGKPFWRSVEYFFTGNYSADDGNNSIVAIGFGGEIHAYGGDDHVTVGSIGATVYTGSGNDTVVGGSAYLRVEDTTGHLSVKGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNNGDVSYGGAAAYNGITRKGLSGNVTFKGAGGYNALWHETNQGNLSFAGAGAGNKLDRTWFNRYQGSRGDVTFDGAGAANSISSRVETGNITFRGAGADNHLVRKGKVGDITLQGAGASNRIERTRQAEDVYAQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTITRKGSGSSFDAQGMEYAKAEDIVLTAAQMHGLSIDNGNKFHAVTAVKSEREPNTYLFAIADGTYTKINKVRLYNDPETGKLKYYSEAWFKRGNHLAELARSDVSSAGGFEVNPINGGYTLANIAVEHQQSVTVHAVEKNLTEYEWVTYANGTLIDAKDVALSEAKMGGHAISTDGTTVDVQAVKSNRKPNTYVYAKVLGPYTKIVVVELANDPKTGALKYQARSWYKEGDHTANLANEDISSANGYHSMGKGGYSLSDLHYSVNAVRSTSETVADIDEYTDQTLFKPATDSGESSGDVRFNGAGGGNVIKSNVTRGNVYFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSKQGKMDVYAGGAVNVLVRIGDGQYLAHLLAYGNISVHKGNGNSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVASVLAGGANVLTKVGDGDLTAGMLGGANVITHISGDNETSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGIMLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNANIFTHVGSGSTFAAMIGQANIMTKVGNDLTAALMVGKANIYTHVGDGTSLGIFAGEVNVMTKIGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKVGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDIGNVMTHVGDGTTIGIAKGKANIITKVGDGLGVNVAWGQANVFTQVGDGDRYNFAKGEANIITKVGDGKEVSVVQGKANIITHVGNGDDYTGAWGKANVITKVGNGRNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGKANITTTVGDGLSVTAAYGDANINTKVGDGVSVNVAWGKYNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNKLSALFDNIKQTLLGVGGSQAINYLVQGDEASSSGTQKGRGAIATPEITKLDGFQMEAIEEVGSDLGDSLTGSVTKVDTPDLNKMQNALDVDGSSDQTQAPNLIVNGDFEQGDRGWKSTHGVEASYSGNVYGVNGEGHGARVTELDTYTNTSLYQDLTDLTEGEVIAVSFDFAKRAGLSNNEGIEVLWNGEVVFSSSGDASAWQQKTLKLTAHAGSNRIEFKGTGHNDGLGYILDNVVAKSESSQQANAVSEHATQNQASQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALGNNGQAQRDAVKEESEAVTAELTKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTQSDNNSKVKESVAKSEAGVAQGEQNRAGAEQDIAEAKADAETRKADAVAKSNDAKQAESDAHSAANDAQSRGDRDAMNAENKANQAQNDAKGTKQNEGDRPDREGVAGSGLSGNAHSVEGAGETGSHITTDSQTNADGRFSEGLSEQEQEALEGATNAVNRLQINAGIRGKNSGSTITSMFTETNSDSIVVPTTASQDVVRKEIRISGVNLEGLGEASHDSAESLVAARAEKVANLYRWLDTDNDVATDKYVPVPGFERVDVDVSDEVKQRMIQSMSGYIEHTDNQVPKDQAEALATLFVESTLDYDWDKRVEFLTKLESYGYSFEAPHAEKSIVSFWSGKNFKQYRDILDNAQTDGKKVVYDIDVKGNAFAIDLNKHLMRWGGLFLDPDNAEQNQLKSSIDAATFSNTGFWSSVYATGAQNDVYVIAEGGVRLGNYFWNVELPALRQLQREGLVGEIRLLDKPVSEYKDLPADQIGRRLTDAGVAVKVRFDALSHERQAELLADNPDGYKADTLVELDVKLSAIDSMLRESLPFYSLRTERNLLVQEGEEGFEVRSWPGIDGKSKTILLDNPEDAAQQKSIERFILANFDNFEQMPDELFLVDNKVLSHHDGRTRIIAQKEDGAWTYNTNVELMSVTELLDAAHVNGKVRGDSYQQVIDALTEYHASTVEHADYELESVEKLLNLRKQIEGYVLGHPDSGRVEAMNSLLNQVNSRLEEVSVLAVSEQSIKAHDSFSRLYDQLDNANLKESKHLYLDGNGDFVTKGKGNLATIDQLGGSDAVLEKVKAAVTHEYGQVVADTIFARLSANDLAKDGKGIDIAGLNKVHQAIEQHMSPVSATMYIWKPSDHSTLGHAALQIGQGRTQLEGQAAADFNKQNYVSWWPLGSKSSNIRNIFNVATEDQPDLKLRWSDFSQPAHQNDTLEHDMASEENDGFGLKDGETKLKRFIEKLNAAKGIDASYKDASEGYASVLLGNPDMLASTGIPAHVFQPFVDQWNDTSYDMMDVANRFAEELQKQAQASGDPALVEKRIDNVVRLFAERALEEIEAFKASQADEGRVFRINLEGLDVAAMQAEWNRLSNDPDARYQLLTKNCSSTVAKVLKAGGADKLIGHTWRPKFGVWTPTELFNFGQALQEAQLEIAAKKQSHQVTDVLDALSGNEKHKENVTIENDGTPPRDKESLSPLTRFLNNELYGEKDARRKIGEITQTLLDHAVENGESQKVTLKGEAGRLTGYYHQGAASSEGETSATSGKVVLFLHGSGSSAEEQASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKGLYQDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADLARYAAQNGQAVSGLLLDRPMPSMTKAITAHEMANPAGIVGAIAKAVNGQFSVEKNLKGLPKETPILLLTDNEGLGEEGEKLRAKLAIAGYNVTGEQTFYGHEASNRLMGQYADQIVSGLFNAEQAAVEAGEVLKGLEKDFKRYGDALKPDTSVPGKSKDIRTTKDFLNGYKNDHAKEIVDGFRSDMSIKQLVDLFVKGNWSAEQKGALAWEIESRALKVTFQNKSEKYNRLFREIASAGVVDAKATEQLAPQLMLLNLSNDGFGGRCDPLSKLVLVAKQLENDGQVGVARQLLEKMYSAAAVLSNPTLYSDSEKANASKLLSSLAAIHAKNPMHDTSMKVWQEKLEGKQALTVNGVVEKITDASANGKPVLLELDAPGHAMAAWAKDSGDDRVYGFYDPNAGIVEFSSAEKFGDYLTRFFGKSDLDMAQSYKLGKNDAGEAIFNRVVVMDGNTLASYKPTFGDKTTMQGILDLPVFDATPIKKPTGGVASDLEALGDKTKVVVDLAQIFTVQELKERAKVFAKPIGASYQGILDQLDLVHQAKGRDQIAASFELNKKINDYIAEHPTSGRNQALTQLKEQVTSALFIGKMQVAQAGIDAIAQTRPELAARIFMVAIEEANGKHVGLTDMMVRWANEDPYLAPKHGYKGETPSDLGFDAKYHVDLGEHYADFKQWLETSQSNGLLSKATLDESTKTVHLGYSYQELQDLTGAESVQMAFYFLKEAAKKADPISGDSAEMILLKKFADQSYLSQLDSDRMDQIEGIYRSSHETDIDAWDRRYSGTGYDELTNKLASATGVDEQLAVLLDDRKGLLIGEVHGSDVNGLRFVNEQMDALKKQGVTVIGLEHLRSDLAQPLIDRYLATGVMSSELSAMLKTKHLDVTLFENARANGIRIVALDANSSARPNVQGTEHGLMYRAGAANNIAVEVLQNLPDGEKFVAIYGKAHLQSHKGIEGFVPGITHRLDLPALKVSDSNQFTVEQDDVSLRVVYDDVANKPKITFKDSLSGANTALHNQNVNDWERVVVTPTADGGESRFDGQIIVQMENDDVVAKAAANLAGKHPESSVVVQIDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDDSESNNTRLSGYSADELAVKLAKFQQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRSSELAVDEAGRKHTKDANGDWVQKAENNKVSLSWDEQGEVVAKDERIRNGIAEGDIDLSRIGVSDVDEPARGAIGDNNDVFDAPEKRKAETETSSSSANNKLSYSGNIQVNVGDGEFTAVNWGTSNVGIKVGTGGFKSLAFGDNNVMVHIGNGESKHSFDIGGYQALEGAQMFIGNRNVSFNLGRSNDLIVMMDKSIPTPPLVNPFDGAARISGVLQSIATSGEGQDWLAAQEQQWTLSGAKKFVKDMSGLDQSSSVDYTSLVELDSQNERSSRGLKHDAEAALNKQYNQWLSGNSDSDTSKLSRADKLRQANEKLAFNFAVGGQGADIQVTTGNWNFMFGDNIQSILDTNLGSLFGLMTQQFSATGQAKTTFTYTPEDLPRQLKNKLLGQLAGVGAETTLADIFGVDYTASGQIVSRNGEAVDGVAILKEMLEVIGEFSGDQLQAFVDPAKLLDSLKSGINMGADGIKSFAETHGLKEKAPEEEEDNSSVSVNGASVNSAQGATVADGSTETAETPDRAFGFNSLNLPNLFATIFSQDKQKEMKSLVENLKENLTADLLNMKEKTFDFLRNSGHLQGDGDINISLGNYNFNWGGDGKDLGAYLGDNNNFWGGRGDDVFYATGTSNIFTGGEGNDMGVLMGRENMMFGGDGNDTAVVAGRINHVFLGAGDDQSFVFGEGGEIDTGSGRDYVVTSGNFNRVDTGDDQDYSVTIGNNNQVELGAGNDFANVFGNYNRINASAGNDVVKLMGYHAVLNGGEGEDHLIAAAISKFSQFNGGEGRDLMVLGGYQNTFKGGTDVDSFVVSGDVIDNLVEDIRSEDNIVFNGIDWQKLWFERSGYDLKLSILRDPASDSDQAKFEHIGSVTFSDYFNGNRAQVIIAMGEKDATGEREYTTLSESAIDALVQAMSGFDPQAGDNGFMDNLDSKSRVAITTAWADVVHKKGITV

2.3.1.-; 3.4.22.-; 6.3.2.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9KS12}; Note=Binds 2 Mg(2+) ions per subunit. Mg(2+) is required for actin cross-linking activity. Can also use Mn(2+) ions instead of Mg(2+). {ECO:0000250|UniProtKB:A0A0H3AIG7};

proteolysis [GO:0006508]

extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]

acyltransferase activity [GO:0016746]; cysteine-type peptidase activity [GO:0008234]; ligase activity [GO:0016874]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; toxin activity [GO:0090729]

PF00561;PF11647;PF11713;PF20899;PF07634;PF21735;

1.20.140.180;3.40.50.11050;3.40.50.11550;3.40.50.1820;2.60.120.260;

SUBCELLULAR LOCATION: [Multifunctional-autoprocessing repeats-in-toxin]: Secreted {ECO:0000250|UniProtKB:Q9KS12}. Host cytoplasm, host cytosol {ECO:0000250|UniProtKB:Q9KS12}. Note=Secreted via the type I secretion system. {ECO:0000250|UniProtKB:Q9KS12}.; SUBCELLULAR LOCATION: [N-epsilon-fatty acyltransferase F2]: Host cell membrane {ECO:0000250|UniProtKB:Q9KS12}. Note=Targeted to the host cell membrane via the membrane localization region (MLD). {ECO:0000250|UniProtKB:Q9KS12}.; SUBCELLULAR LOCATION: [Actin cross-linking toxin F1]: Host cytoplasm, host cytosol {ECO:0000250|UniProtKB:Q9KS12}.

CATALYTIC ACTIVITY: [N-epsilon-fatty acyltransferase F2]: Reaction=hexadecanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] = CoA + H(+) + N(6)-hexadecanoyl-L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59768, Rhea:RHEA-COMP:17936, Rhea:RHEA-COMP:17953, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:86021, ChEBI:CHEBI:138936; Evidence={ECO:0000250|UniProtKB:Q9KS12}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59769; Evidence={ECO:0000250|UniProtKB:Q9KS12}; CATALYTIC ACTIVITY: [N-epsilon-fatty acyltransferase F2]: Reaction=dodecanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] = CoA + H(+) + N(6)-dodecanoyl-L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59796, Rhea:RHEA-COMP:17936, Rhea:RHEA-COMP:17954, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:86021, ChEBI:CHEBI:143221; Evidence={ECO:0000250|UniProtKB:Q9KS12}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59797; Evidence={ECO:0000250|UniProtKB:Q9KS12}; CATALYTIC ACTIVITY: [N-epsilon-fatty acyltransferase F2]: Reaction=decanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] = CoA + H(+) + N(6)-decanoyl-L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59800, Rhea:RHEA-COMP:17936, Rhea:RHEA-COMP:17955, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430, ChEBI:CHEBI:86021, ChEBI:CHEBI:143222; Evidence={ECO:0000250|UniProtKB:Q9KS12}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59801; Evidence={ECO:0000250|UniProtKB:Q9KS12};

FUNCTION: [Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain-containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells. {ECO:0000250|UniProtKB:Q9KS12}.; FUNCTION: [Cysteine protease domain-containing toxin F3]: Following autocatalytic cleavage in cis, this chain mediates processing in trans to release other individual toxin chains to the host cytosol. Released effector toxin chains cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells. {ECO:0000250|UniProtKB:Q9KS12}.; FUNCTION: [Actin cross-linking toxin F1]: Actin-directed toxin that catalyzes the covalent cross-linking of host cytoplasmic monomeric actin. Mediates the cross-link between 'Lys-50' of one monomer and 'Glu-270' of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding. The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners. Acts as an acid--amino-acid ligase that transfers the gamma-phosphoryl group of ATP to the 'Glu-270' actin residue, resulting in the formation of an activated acyl phosphate intermediate. This intermediate is further hydrolyzed and the energy of hydrolysis is utilized for the formation of the amide bond between actin subunits. {ECO:0000250|UniProtKB:Q9KS12}.; FUNCTION: [N-epsilon-fatty acyltransferase F2]: N-epsilon-fatty acyltransferase that mediates lysine-palmitoylation of host Rho GTPase proteins, with a strong preference for host Rac1. After delivery to the host cytosol, localizes to the host cell membrane where it palmitoylates host Rho GTPase proteins, resulting in loss of all active GTP-bound Rho and subsequent actin depolymerization. Prenylation of host Rac1 at the C-terminus is required for lysine-palmitoylation. {ECO:0000250|UniProtKB:Q9KS12}.; FUNCTION: [ABH effector region toxin F5]: Indirectly activates the small GTPase CDC42. {ECO:0000250|UniProtKB:Q9KS12}.

Vibrio vulnificus

A0A2S4N3N0

OMPA_SHIFL

MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFIPNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGDNINGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKANVPGGASFKDHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDANTIGTRPDNGLLSLGVSYRFGQGEAAPVVAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA

monoatomic ion transmembrane transport [GO:0034220]

cell outer membrane [GO:0009279]; pore complex [GO:0046930]

porin activity [GO:0015288]

PF00691;PF01389;

2.40.160.20;3.30.1330.60;

Outer membrane OOP (TC 1.B.6) superfamily, OmpA family

SUBCELLULAR LOCATION: Extracellular vesicle. Note=(Microbial infection) Upon infection with phage Sf6 is found in extracellular vesicles that associate with the tails of mature phage particles. {ECO:0000269|PubMed:22386055}.; SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250|UniProtKB:P0A910, ECO:0000255|HAMAP-Rule:MF_00842}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00842, ECO:0000305|PubMed:21071053}.

FUNCTION: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. {ECO:0000255|HAMAP-Rule:MF_00842}.; FUNCTION: Required for conjugation with F-type plasmids; probably serves as the mating receptor on recipient cells. {ECO:0000255|HAMAP-Rule:MF_00842}.; FUNCTION: (Microbial infection) Serves as a secondary receptor during phage Sf6 infection; infection requires both lipopolysaccharide (LPS) and the OmpA beta-barrel. {ECO:0000269|PubMed:24673644}.

Shigella flexneri

A0A2T4VDM4

GSDM_VITXG

MGLCSDPAITYLKRLGYNVVRLPREGIQPLHLLGQQRGTVEYLGSLEKLITQPPSEPPAITRDQAAAGINGQKTENLSFSIGINILKSVLAQFGAGAGIEAQYNQARKVRFEFSNVLADSVEPLAVGQFLKMAEVDADNPVLKQYVLGNGRLYVITQVIKSNEFTVAAEKSGGGSIQLDVPEIQKVVGGKLKVEASVSSQSTVTYKGEKQLVFGFKCFEIGVKNGEITLFASQPGAIAMALDAAGGVMPSDSALLDEGGLLDLEGF

defense response to virus [GO:0051607]

cytoplasm [GO:0005737]; plasma membrane [GO:0005886]

Bacterial gasdermin family

PTM: Palmitoylation helps stabilize the inactive state; may self palmitoylate. {ECO:0000269|PubMed:35025633}.

SUBCELLULAR LOCATION: [Gasdermin bGSDM]: Cytoplasm {ECO:0000305|PubMed:35025633}.; SUBCELLULAR LOCATION: [Gasdermin bGSDM, N-terminus]: Cell inner membrane {ECO:0000250|UniProtKB:P0DV48}; Multi-pass membrane protein {ECO:0000305}.

FUNCTION: [Gasdermin bGSDM]: Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Expression of bGSDM and the neighboring protease gene (Ga0334635_1659) is toxic in E.coli (PubMed:35025633). Cleavage of this precursor by its dedicated protease releases the active moiety (gasdermin bGSDM, N-terminus) which inserts into membranes, forming pores and triggering cell death (By similarity). {ECO:0000250|UniProtKB:A0A0S2DNG5, ECO:0000250|UniProtKB:P0DV48, ECO:0000269|PubMed:35025633}.; FUNCTION: [Gasdermin bGSDM, N-terminus]: Pore-forming protein that causes membrane permeabilization via a pyroptosis-like activity. Makes ring-like pores when released. {ECO:0000250|UniProtKB:P0DV48}.

Vitiosangium sp. (strain GDMCC 1.1324)

A0A2T5Y4G4

CAP12_SPHFK

MKKRIFIGSSSEQLTILNEIVDLLGDDVECIPWTDAFALNKSGLDSLIKQTRLADYSILIATKDDLTKQRGESLTKPRDNVVFEFGLFLGAAGPEKCYLIAEEDTDLPTDLDGITVAKFTRNSGQYNSLDKIVESIRTHLVKIAEMSQLGLLPSTALAIGYYNSFIKRVCEEIHGSECVELEGKKIKVKSFRVDVVIPETLDDNGVGNFTTLYNKRYGLSKATTCTNPALLGTRGFPFHFKVDPPDANQESPVDIHLLDIPSTLSTIVESLKLYLPSNQVGQDFDMDYLEMRELENFAKVLKYLIGRNAATKGYVNVLTNVKL

3.2.2.5

defense response to virus [GO:0051607]

NAD+ nucleosidase activity [GO:0003953]; nucleotide binding [GO:0000166]

PF10137;PF20300;

Bacterial STING family

CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5; Evidence={ECO:0000269|PubMed:32877915, ECO:0000269|PubMed:35859168};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27 uM for NAD(+) {ECO:0000269|PubMed:32877915}; Note=kcat is 2.3 sec(-1). {ECO:0000269|PubMed:32877915};

FUNCTION: Effector protein of a CBASS antiviral system with NAD(+) hydrolase activity (PubMed:32877915). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system (PubMed:32839535). {ECO:0000269|PubMed:32877915, ECO:0000303|PubMed:32839535, ECO:0000305|PubMed:32877915}.; FUNCTION: Upon activation by 3'3'-c-di-GMP forms filaments which hydrolyze NAD(+); filament formation is required for enzyme activation (PubMed:32877915, PubMed:35859168). Induction in an E.coli strain that synthesizes c-di-GMP leads to significant growth inhibition (PubMed:32877915, PubMed:35859168). Binds c-di-GMP and 3'3'-cGAMP (3'3'-cyclic GMP-AMP), but not c-di-AMP, 2'3'-cGAMP or cUMP-AMP (PubMed:32877915). {ECO:0000269|PubMed:32877915, ECO:0000269|PubMed:35859168}.

Sphingobacterium faecium (strain DSM 11690 / JCM 21820 / NBRC 15299 / NCIMB 13408 / KS 0470)

A0A2U1LIM9

NCPR1_ARTAN

MQSTTSVKLSPFDLMTALLNGKVSFDTSNTSDTNIPLAVFMENRELLMILTTSVAVLIGCVVVLVWRRSSSAAKKAAESPVIVVPKKVTEDEVDDGRKKVTVFFGTQTGTAEGFAKALVEEAKARYEKAVFKVIDLDDYAAEDDEYEEKLKKESLAFFFLATYGDGEPTDNAARFYKWFTEGEEKGEWLEKLQYAVFGLGNRQYEHFNKIAKVVDEKLVEQGAKRLVPVGMGDDDQCIEDDFTAWKELVWPELDQLLRDEDDTSVATPYTAAVAEYRVVFHDKPETYDQDQLTNGHAVHDAQHPCRSNVAVKKELHSPLSDRSCTHLEFDISNTGLSYETGDHVGVYVENLSEVVDEAEKLIGLPPHTYFSVHTDNEDGTPLGGASLPPPFPPCTLRKALASYADVLSSPKKSALLALAAHATDSTEADRLKFLASPAGKDEYAQWIVASHRSLLEVMEAFPSAKPPLGVFFASVAPRLQPRYYSISSSPKFAPNRIHVTCALVYEQTPSGRVHKGVCSTWMKNAVPMTESQDCSWAPIYVRTSNFRLPSDPKVPVIMIGPGTGLAPFRGFLQERLAQKEAGTELGTAILFFGCRNRKVDFIYEDELNNFVETGALSELVTAFSREGATKEYVQHKMTQKASDIWNLLSEGAYLYVCGDAKGMAKDVHRTLHTIVQEQGSLDSSKAELYVKNLQMAGRYLRDVW

1.6.2.4

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};

sesquiterpene biosynthetic process [GO:0051762]

cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]

flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; NADP binding [GO:0050661]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity [GO:0016491]

PF00667;PF00258;PF00175;

3.40.50.360;3.40.50.80;2.40.30.10;

NADPH--cytochrome P450 reductase family; Flavodoxin family; Flavoprotein pyridine nucleotide cytochrome reductase family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.

CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16612385};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 uM for cytochrome P450 {ECO:0000269|PubMed:16612385}; KM=23 uM for NADPH {ECO:0000269|PubMed:16612385};

FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes (By similarity). It can also provide electron transfer to heme oxygenase and cytochrome B5 (By similarity). Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:16612385). Acts as a redox partner for CYP71AV1 which catalyzes the conversion of amorphadiene to more oxygenated products (PubMed:16612385). {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16612385}.

Artemisia annua (Sweet wormwood)

A0A2U8QPE6

OXLA_MICMP

MNVFFMFSLVFLAAFGSCADDTRPLGECFREADYEEFLEIARNGLKKTSNPKHVVVVGAGMSGLSAAYVLAKAGHKVTLLEASEGVGGRVKTYRNKQEGWYINLGPMRLPERHRIVREYIRKFHLPLSEFVQENENTWYYIKNIRKRVSEVKKNPDLFEYPVNPSEKGKSASQLYQESLEKVIDELKRTNCNHILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSSFYLSFIESLKSDDIFSYEKRFDEIVGGFDQLPISMYQAIAEMVHLNAQVIKIQHNAKKVIVTYQTPAKTLPSVTADYVIVCSTSRAARHIRFQPPLPTNKARALRSIHYRSAIKIFLTCTKRFWEADGIHGGKSTTDLPSRFIYYFNQNFTNGIGVIMAYVLADDAKFFQPHDLKTNADIVINDLSLIHQLPKEEIQALCRPSWIQKWSLDKYAMGSITSFTPYQFLDYFEIAAAPVGRIHFAGEYTAKHHGWIDSTIKSGLRAARDVNRA

1.4.3.2

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382};

amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]

extracellular region [GO:0005576]

L-amino-acid oxidase activity [GO:0001716]; toxin activity [GO:0090729]

PF01593;

3.90.660.10;3.50.50.60;1.10.405.10;

Flavin monoamine oxidase family, FIG1 subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29900074}.

CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:29900074, ECO:0000269|PubMed:31129208}; CATALYTIC ACTIVITY: Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:29900074, ECO:0000269|PubMed:31129208}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:29900074}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:29900074};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:29900074};

FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:29900074, PubMed:31129208). Shows activity on L-Leu, L-Trp, and L-Tyr (PubMed:29900074, PubMed:31129208). Is not active on L-His, L-Ser, L-Arg, L-Ala, L-Glu, L-Cys,L-Lys, L-Val, L-Ile, and L-Thr (PubMed:29900074). Induces apoptosis in Jurkat cells through a hydrogen peroxide-mediated signaling pathway dependent mostly on CASPASE-3 pathway (PubMed:31129208). Remarkably, does no induce toxic effect on peripheral blood lymphocytes (PubMed:31129208). Also exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, and antiparasitic activities, as well as regulation of platelet aggregation (By similarity). Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity). Shows antibacterial activity against S.aureus, but not against E.coli (PubMed:29900074). {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:29900074}.

Micrurus mipartitus (Red-tailed coral snake)

A0A2U9GGW3

THS2_PAPSO

MAPLGVSGLVGKLSTELEVDCDAEKYYNMYKHGEDVKKAVPHLCVDVKIISGDPTSSGCIKEWNVNIDGKTIRSVEETTHDDETKTLRHRVFEGDVMKDFKKFDTIMVVNPKPDGNGCVVTRSIEYEKTNENSPTPFDYLQFGHQAIEDMNKYLRDSESN

4.2.99.24

alkaloid metabolic process [GO:0009820]; defense response [GO:0006952]

carbon-oxygen lyase activity [GO:0016835]; protein homodimerization activity [GO:0042803]

PF00407;

3.30.530.20;

MLP family

CATALYTIC ACTIVITY: Reaction=(7S)-O-acetylsalutaridinol = acetate + H(+) + thebaine; Xref=Rhea:RHEA:56908, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57672, ChEBI:CHEBI:59953; EC=4.2.99.24; Evidence={ECO:0000269|PubMed:29807982}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56909; Evidence={ECO:0000269|PubMed:29807982};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=3.2 nmol/min/ug enzyme {ECO:0000269|PubMed:29807982};

PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000269|PubMed:29807982}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:29807982};

FUNCTION: Catalyzes the formation of thebaine from (7S)-salutaridinol 7-O-acetate at the expense of labile hydroxylated by-products, which are preferentially produced by spontaneous allylic elimination. No visible activity toward (7S)-salutaridinol (at pH 7). {ECO:0000269|PubMed:29807982}.

Papaver somniferum (Opium poppy)

A0A2V5GX43

PYVA_ASPV1

MDPQQRLLLEVVFEAFEDAGISLEEMNGSRTSVLCGAFTNDYNAMLTKDLEYYPKYTVTGTGNAILANRISYAFNLKGMSLTIDTACSSSLVGFHLGAQAILNGDCEMAIIVGSALHFDPNIFITMTDLGMLSQEGRCRAFDAGGKGYARGEGICAVILRGQMQAEMHGDHIRALVRATGSNHDGMTQGITLPSSEAQEALIRRTYQSCGLDPADTQYVEAHGTGTARGDPLEMRAIGACFSSPRRSDPLYVGSVKSNIGHAEGASGLAGLIKASMALEKGQIPPNMHFKHPNPEIAFADWQIEVPTRVIDFPSNAQGTRRVSINSFGYGGSNAHVILESYDQLPHVQPTDPGAHRPYLVPLTSHTEKAGKLMVEKLGAYLDDRPSTLVVDLAHSLATRRTLHDERSFAVGASAADIRTQLSEGLPAWTKVRREPVRLGFVFTGQGAQWHAMGRQLLEQCPFFRHTLERADRILATLPDKPEWSIVTELTQPKETSRLGETRLSQPICTALQLAILDLLKSWGIVPQATVGHSSGEVAGAYAAGILTFENAMYAAYYRGLHMSSPRSSTSPGRDAIPGAMLAVGLGEAEAMAETESYRGRAVVAAVNSPSSVTLSGDADAIAEIKERLDAQKVFARRLQVQQAFHSHHMDPLAPAYEEALRNCPGFAATAPACRFFSSVTARVANPDTMGPQYWSANMTGTVRFSDALIGVLLDDLEDPNVDALVEIGPHPALKGPARQVMKSVNMDLPYFASLSRGVPDYEGILALAGQLFQLGYPVDLTAVNSDTYLADSDPPRQTHRAQRIPDLPLYAWDHSDRYWAETRLIKEHRLRPHHHPILGAKMPGSIEGHVRWRNYLRTRELPWLVDHMVDNKVTFPAAGYVTLAIEAALRMKDTVMAAQGVSLRNLSIKSALVLDESEMGSEVVVDIRPQTTSAKSRSDTWLEFTIFSYNGSLTCAEHCTGLISISTATTADGAPSRKPYRQHPQPQPGRMSTASFPAQSFYTHLRQLGLQYGEHFQLLTGTIESGAGFSSSMLTFEPAQYAAQPADRTVVHPTMLDAAFHTIFAALEGLSGRTLQTAFVPTFVHSLDIFPAMLSGMDAPRPLEARVASSAHFSGPRAAVSDVDMYRQGDGEALLSLAGLRLTSLSNGRAAHNRSLFFRTRWQPAFDQLAEDSPALQDQTLAGVLDLFLHQHPDTKILHFTPDINQTRQLVGCLVDQGSERRRFRSITPVATGGAFAEELERVQREQPGCLVTGEPEPEAYDLVIVSEAQEAHPLPFLRDGGYVISHGSAIDETNLTKRFQCADVEVWQRTRETRRDVRPLLLAMAPTPSRRTLDLASHIRAANPDRPVSCLGLQELLARMTGVEDVVVLASLDRDLLSGLDPQGELFFEATRALLIRPDVNVLWLLQDTTAPRHVDSLGSSMIVGLARTARSENPSSRIVTLDLPVDWSPAAVVPWLPQLLDPEVHEDEFHLRDQVLSIPRIENDDGLNSKVPGGVSSGPRPESFSAQRPMRLAIGQAGLLETLVWEDDVEILNEPLPDDEIEIEVKASALNFRDVAAAMGIIDDHRLGDECAGLVRRVGQQVDPAAFQPGDRVVALRPGRGAHRSVVRNPACHCFRLGPMPFEQATALPLILTTAYYSLVETARLQPGETVLIHCAAGGVGQMAIQIAQQIGARIIATVGSPAKRDLLQSRYGLTEAHILSSRDASFVDGVMQLTGGRGVDVVLNSLSGKLLHASWNSLATFGRFIEIGKRDIHENTLIEMDPFRRNVLFASVDMVTIYAQNRALGARIFDHCCNMVHEGRIQLPATILALPYSEAVQGFRLLQMGRHTGKVVLVAEDQGDQVPVSPPTWNAVANRLSPDKTYLLVGGLGGLGRTLTEWLVQRQAKRIAFLSRSGADRPEAQATVAWLRARGIAVSVHAADVADPGHVQACIKAIPDLGGVFHAAMVLADAPLERMSYAQWHRCVQPKVRGAYNLHCATVHCPLDFFVCFSSISAFFGSKAQANYAAANVYLDSLVRYRRQLGLPASSMNCGRITGVGVAAADASLERFMVEEGFDGVNRQELLYQIEEAIFSADHPAPLSGRGTDMSQTLTGVTLERDDVYWAQRSIFRNLYRNHDVEGQSRPGADEVNLSVQLARTIDLSDRVALLMERFVDKVSVVLGLSPESLKPADPVYGLDSLVAVELRNWFTKSVGVDIALFDVLGSPSIQALVEKAIGLFDAQVQQQQQQQQSVQSSSAPSNDDQSPTFNKNLDSQDPSTSLQIPKADCSRPLPMSTFQNRLWVSHRFAADKSRINLAITMHLRGQADHGILEQALSELIARNPILRTAYGEGEAQDEQRVMAPRPFHLGFHDLSKSGPSEGPTASLETLVGSLKRKEMRIEEGEVLEATLVQRSSTECALVLIMHHICTDRSNSQSFVRQLAALYDALRQGRSLSTIPAPKVTYADFTLWHNQLLTSPSMGKGVEYWKQTLAGMPASCQLLPFAKGERPSWDEYGRETVVAALSARQLQRMKRICSQARTSPFHFLLAAFRAFLHRYTADEDLTILMVDGNRPHADLGEVLGFFVNMAPIRCRDACAGSFETLLKTIGGRVLEAMAHSHVPFDVIVAQTQGARTPAHFPVSQVLVNYQQPDEQARYQTTDFTFQGTEVQNMPTGCELSLQAREDAEHGLQLELEYATALYEDGDMRCFFDNFQTFVTSLIQDHRQSIPEVRLAGTLELERLALHCWNSHPPDHGWQPLNLPRRIVEVAETQPRAIAITTSAGEAVTYQDLVASARRVAFSLQNLGIGPGQVVGILASPGIELVTAMLGALFNRCGYVPLDPTMAVGRLAYIVGDSGMQLLLVDEESDPLASSLGRESPSLPNVMSIKNATRAAWPADLPRSLPTDPFYMMYTSGSTGTPKGVPLTQENVGEMLAAMQARFNFTREDRFLHQISPSFDLSVVELFSPLCVGAKLCIATKTTRSDPRLLGDYLRQASVTVTYFTPTQFALVLEHSGASLVACPDYRIALLCGERLPTRLAEAFHQLACAATLYNAWGPTEAAVQTTIHRVQWPADQTLNIPIGHAVGSCRHYIVDAAMNPLPVGFVGEICIGGPQVARGYWNRAESNRQQFLRNPFASPDDHRRGWTRLFRTGDLGRFLPDGQLEFLGRIAGDKQIKLRGFRIDLGEIEHVLHRHSGTPDGQGIVDLAVIAQSAPEDADALTDDRWLVAFIVPKQAIPTEAAKRAYATLLHTRAKPYLNRYMLPAAYQFVDQLPTTASGKTDRRALGASQAPGTPPQHGAGPAAASTLDPAQAQAQDRADEEVGDRTMATVTRVWQEVLRLDHDIPVEPTSNFFDMGGSSTLLLRLQGKLQTTLSIPISLQEMVRRPTLVQLVELVHSKVPREGQPPPTPGSRPEEDVVDWAQETTLPAETRYHPPSAPMSPGGRDILMTGAESFTGIHLLAQLLTSHPSGTIHLLGTHHPWDHAQVFQRLQEYNLLNATLTPEQILTRLRTIPGSLAEGSHFGLSPRAFEALGRSIATIYHLASEVSLLKTYHDLKPINTAAILPLIELARWGGPSPIHYLSTWSVPHLQLWTAPPTTPAVVHEASAGHFTPPPTADQGYFKSRWAAEMLLTHAAARGFPVTIYRASAVTGNPTTGLPAPAGDFVRSLILDMLRHRLVPRFARESPAPVVVDLVPVNYLTALLAHLAQRPRAAAAEGPRPAGVEIFHLTNPTPLPLDQLPGLTGSIRGDATAGRVVSVDDWLAAVSGSDPAAAAADEDEQLRVQVAGGYFRRGHQMFALDRRRTDAALGGVTEGWVDCPPVDANYLRALWLQKV

2.3.1.-; 6.3.2.-

fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolite biosynthetic process [GO:0044550]

cytoplasm [GO:0005737]; plasma membrane [GO:0005886]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]

PF00698;PF00107;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF07993;PF21089;PF00550;PF14765;

3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.90.180.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;

NRP synthetase family

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:33117309}.

FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranoviolin A, a pyranonigrin analog with a C-3 methoxy group (PubMed:33117309). Initially, the PKS portion of pyvA synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA, which is then condensed with the thiolation (T) domain-bound glycine activated by the adenylation (A) domain (PubMed:33117309). The subsequent chain release by Dieckmann condensation (DKC) could be catalyzed by the TE domain present at the C-terminus of pyvA and/or the alpha/beta hydrolase pyvD, installing the tetramic acid moiety (Probable). The FAD-dependent monooxygenase pyvC next epoxidizes one of the olefins of the polyketide part, and the epoxide ring-opening induces the dihydro-gamma-pyrone ring formation (Probable). The cytochrome P450 monooxygeanse pyvB would be responsible for the 2 consecutive reactions, in which the dihydro-gamma-pyrone is oxidized to gamma-pyrone and C-7 is hydroxylated to yield pyranonigrin F (Probable). Finally, the O-methyltransferase pyvH methylates the C-3 hydroxy group to complete the biosynthesis (Probable). {ECO:0000269|PubMed:33117309, ECO:0000305|PubMed:33117309}.

Aspergillus violaceofuscus (strain CBS 115571)

A0A2Y9GHM3

APOE_NEOSC

MKVLWAALVVALLAGCWADVEPESPLQGKPEPELEPELEPKRELEQEVEAEAGWQAGQPWELALARFWDYLRWVQTLSDQVQEDMLSNQVTQELTTLMEETMKEIKAYRAELEEQLGPMASETQARVAKELQAAQARLRSDMEDVRTRLTQYRGEVQAMLGQSTEELRARFASHMRKLRKRVLRDAEDLQKRLAVYRAGVREGAERSVSSIRERLWPLLEQARTRHANLATQPLRERVDALGQQLRGRLEEVGSRARSHLDEVREQMEEVQAKMEEQANQMRQQVEAFQARLKSWFEPLVEDMQRQWAGLVEKVQVAVGTSPTTPPLETK

cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221]

chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361]

amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326]

PF01442;

1.20.120.20;

Apolipoprotein A1/A4/E family

PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02649}.

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000250|UniProtKB:P02649}.

FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. {ECO:0000250|UniProtKB:P02649}.

Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi)

A0A2Z4HPY4

EFUA_HORCR

MPSYHNTDKTLLGDARQSLQQAVDYSLGCQQPDGHWVAPVMADATFTAQYVFFKHQIPELSLDEDGPEIQRWLLGEQTADGSWTLAPDLPGNLSTTVEAYLALRILGVPKSDQAMLRARDFVVRNGGVEGVRFFTRFFLATFGLVPWTAIPQMPAELILLPTFMFLNIYVLSSWARSTLIPILLVRHHEPVYALPNGQSANNNFLDELWCNPGEKNIPFALPLWDLLRRYQWIEFAFTLLDHILALFGGLRRWPCRHMALKRCTAWLLEHQEESGDWAGFFPPIHGSIWALLLDGFSFQSEVIRLGMEALERLVVIDPKGKWVQSTVSPCWDTALMANALCDAGMSGDTRLAKATQWLRDRQLMVSHGDWRNYANTQQAGGWSFQYFNSFYPDVDDTAVVIMTLIKEDPNCTNSDCVMNGVEWMLGMQSRDGGWGAFDVNNNARWLHKIPFSDMDSLVDPSTSDVTGRILECLGLLLSQRKSPLSPRWRHRLQASSAKAIAFLAKEQESSGAWWGRWGNNYHYGTANVLRGLAWFAQTDPSAQMMCMRTLSWIDETQNADGGWGETLASYVDKSLAGLGRSTAAHTAWALESLLRFRLPSDQAIERGVRWLIDNQQPNVDGYYYGTKWQAGAGQGASWRFDHAYVGTGFPSVLYLGYPYYHHLFPIQALSRYIDKASRQGIETLRIPSSSAVILDRPNVLLMAMGSRGDIQVFLNVTKRLSSCRVRIATHPAHQAKVEGHGFEFYDVGGSPEVFSAALANGHGILRSIIDGRFRELQHLLRSIYRSFWVAALDDVQSHSPLKPESSSRPFIADVVVSGPSTSVHVHAAERAQAPLVIISTQPAIITGDFQSPLTMSRAQFNPSRLWNRISFHMLAFFDWLSFGPSFNRMRANSYQLRSLDLAWALFEFVKVSVPHVCLWSTSLAPKPEDWDNNVIIAGYSSMSDDADDVASKSLQAFLETRQPVVAISFGSATIEDPMKLIKLMSAALVKVGASSVVCRSWDSSFEAEADLPSNVFLVDSIPHGWLLQHVEGFVHHGGAGHTAAGAKAGVSQLVMPQFLDQFFWATKVSEMGLGPTPLPLRELFLDELAPRMEDLLSSKYTKACTNMALQLRGDVDGADVAGDEILRQVEAITTCCIFPELSAHWYCTESDLSLSGAAAASLVSSKEIQWQDLELRPAKDWEQQWRTVRSSSNLVRIWRAIVQLLYGFTTTILALFGWLKGTHGYLDGDRHLIKMEDPLRQARLEQAQFDLHLIHQACDSGSSTSLDAKIIENWKARKAVVIHEVFDDDSGASESSRSSLDGGHADSVLDIEEK

2.4.1.-; 5.4.99.-

carbohydrate metabolic process [GO:0005975]; cellular glucuronidation [GO:0052695]; lipid glycosylation [GO:0030259]; triterpenoid biosynthetic process [GO:0016104]

endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]; membrane [GO:0016020]

enzyme binding [GO:0019899]; intramolecular transferase activity [GO:0016866]; sterol 3-beta-glucosyltransferase activity [GO:0016906]

PF06722;PF03033;PF13243;PF13249;

1.50.10.20;3.40.50.2000;

Terpene cyclase/mutase family; Glycosyltransferase 28 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30051576}.

FUNCTION: Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of enfumafungin, a glycosylated fernene-type triterpenoid with potent antifungal activity, mediated by its interaction with beta-1,3-glucan synthase and the fungal cell wall (PubMed:30051576). The pathway begins with the terpene cyclase-glycosyl transferase fusion protein that most likely uses 2,3-oxidosqualene as substrate and catalyzes glycosylation immediately after cyclization (Probable). The fernene glycoside then could be processed by the desaturase efuI which catalyzes isomerization of a double bond established by efuA to form the core structure (Probable). The latter would then undergo a series of hydroxylations in unknown order at C-2, C-19, C-23 and C-25, which would be catalyzed by two of the three cytochrome P450 monooxygenases efuB, efuG or efuH (Probable). The hydroxy-group at C-25 becomes oxidized by the dehydrogenase efuE to enable a spontaneous, non-enzymatic hemiacetal formation with C-23 (Probable). After hydroxylation at C-2, acetylation by the acetyltransferase efuC takes place (Probable). The final steps in enfumafungin biosynthesis require expansion of the 5-membered ring by lactonization via a Baeyer-Villiger reaction mediated by one of the BGC's cytochrome P450 monooxygenases (efuB, efuG or efuH) followed by ring cleavage (Probable). This type of reaction would establish a double bond between C-20 and C-21 which could be reduced by the reductase efuL to form the final product (Probable). {ECO:0000269|PubMed:30051576, ECO:0000305|PubMed:30051576}.

Hormonema carpetanum

A0A2Z5D854

C71Z4_PASSA

MDPAAIFLILAIPIASVYLLFYHKKRVNGLSSPPGPRGLPFIGHFYQIYKSECAHEYISNLSKQYGSLMTLHLGSVPALVVSSPKMAQEVLKTQDLVFCSRAQMTGSGKLSYNGLEMAFAPYGEHWRNVRKMCTLELFTQKRAQFNFRPVREDEVSRMVGRLSEAAAASEDVNAYECFTNFATSIISRVAFGKRYDEDNLGKEKFQRMVADIEAMFAAFFVSDFFPMFGWIDRLSGVKAVLDRNFNEMDTFYQELIDEHLKPDRPESLNGDLIDVMLKNKGSFLTMDSIKAILLNVFSGGIGTTGSALVFAMTALLRNQRVMKKAQEEVRSVIGKKEIVDEDDIQKLPYLRAVVKETLRLYPPGPLLIPRVAMESCVLGEDEDHMYMIKPNTIVYVNTWGIGRDPKYWKNPLEFMPERFFERPDLNYTGQQFEYLPFGSGRRICAGIIIGQNNVEVGLANLLYSFDWEPPTGKTFEDIDDQPCNGLTLAKKNPLYIRPKIYVHP

1.14.14.-

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1};

coumarin biosynthetic process [GO:0009805]; response to wounding [GO:0009611]

endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=O2 + psoralen + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + xanthotoxol; Xref=Rhea:RHEA:68548, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15709, ChEBI:CHEBI:27616, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:29971079}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68549; Evidence={ECO:0000269|PubMed:29971079}; CATALYTIC ACTIVITY: Reaction=6-methoxycoumarin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + scopoletin; Xref=Rhea:RHEA:68564, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17488, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:178005; Evidence={ECO:0000269|PubMed:29971079}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68565; Evidence={ECO:0000269|PubMed:29971079};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.3 uM for psoralen (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMed:29971079}; KM=9.5 uM for 6-methoxycoumarin (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMed:29971079}; KM=762.2 uM for scopoletin (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMed:29971079}; KM=159.9 uM for 7-methoxy-3-methylcoumarin (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMed:29971079}; KM=72.5 uM for 7-methoxycoumarin (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMed:29971079};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29971079}.

FUNCTION: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes (PubMed:29971079). Catalyzes the conversion of psoralen into xanthotoxol and of 6-methoxycoumarin into scopoletin (PubMed:29971079). Can also convert with a lower efficiency scopoletin into fraxetin and 7-methoxycoumarin into daphnetin-7-methylether, and use 7-methoxy-3-methylcoumarin as substrate (PubMed:29971079). {ECO:0000269|PubMed:29971079, ECO:0000303|PubMed:29971079}.

Pastinaca sativa (Wild parsnip) (Anethum pastinaca)

A0A2Z5QKZ7

ORS_RHODA

MALVNHRENVKGRAQILAIGTANPKNCFRQVDYPDYYFRVTKSDHLIDLKAKFKRMCEKSMIEKRYMHVNEEILEQNPSMNHGGEKMVSSLDVRLDMEIMEIPKLAAEAATKAMDEWGQPKSRITHLVFHSTLGTVMPGVDYELIKLLGLNPSVKRFMLYHLGCYGGGTVLRLAKDLAENNPGSRVLVLCCEMMPSGFHGPPSLQHAHLDILTGHAIFGDGAGAVIVGCVDPSGGTNGVVERGVRRYEQPLFEIHSAYQTVLPDSKDAVGGRLREAGLIYYLSKRLSNDVSGKIDECCLAEAFSAAIKDNFEDWNSLFWIVHPAGRPILDKLDAKLGLNKEKLRASRNVLRDYGNMWSSSVLFVLDEMRKGSIAQRKTTTGEGFEWGVLLGFGPGVTVETVVLRSVPTAKLK

2.3.1.-

aromatic compound biosynthetic process [GO:0019438]; orcinol biosynthetic process [GO:0046197]; polyketide biosynthetic process [GO:0030639]; terpenoid biosynthetic process [GO:0016114]

acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]

PF02797;PF00195;

3.40.47.10;

Thiolase-like superfamily, Chalcone/stilbene synthases family

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA = 4 CO2 + 4 CoA + orcinol; Xref=Rhea:RHEA:63072, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16536, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384; Evidence={ECO:0000269|PubMed:27729920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63073; Evidence={ECO:0000269|PubMed:27729920}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + orsellinate; Xref=Rhea:RHEA:62972, ChEBI:CHEBI:15378, ChEBI:CHEBI:16162, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384; Evidence={ECO:0000269|PubMed:27729920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62973; Evidence={ECO:0000269|PubMed:27729920}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + tetraacetate lactone; Xref=Rhea:RHEA:63064, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:133952; Evidence={ECO:0000269|PubMed:27729920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63065; Evidence={ECO:0000269|PubMed:27729920}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2 H(+) + 2 malonyl-CoA = 2 CO2 + 3 CoA + triacetate lactone; Xref=Rhea:RHEA:63068, ChEBI:CHEBI:15378, ChEBI:CHEBI:16458, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384; Evidence={ECO:0000269|PubMed:27729920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63069; Evidence={ECO:0000269|PubMed:27729920}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA = 2-acetylphloroglucinol + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:63076, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:64344; Evidence={ECO:0000269|PubMed:27729920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63077; Evidence={ECO:0000269|PubMed:27729920};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.6 uM for tetraacetic acid lactone (with acetyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=11.7 uM for triacetic acid lactone (with acetyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=9.98 uM for orcinol (with acetyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=9.88 uM for orsellinic acid (with acetyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=10.8 uM for phloroacetophenone (with acetyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=17.1 uM for 4-hydroxy-6-propyl-2-pyrone (with butyryl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=26.4 uM for 4-hydroxy-6-pentyl-2-pyrone (with hexanoyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; Note=kcat is 0.0573 min(-1) with tetraacetic acid lactone as substrate (with acetyl-CoA as cosubstrate) (PubMed:27729920). kcat is 0.243 min(-1) with triacetic acid lactone as substrate (with acetyl-CoA as cosubstrate) (PubMed:27729920). kcat is 1.46 min(-1) with orcinol as substrate (with acetyl-CoA as cosubstrate) (PubMed:27729920). kcat is 0.0675 min(-1) with orsellinic acid as substrate (with acetyl-CoA as cosubstrate) (PubMed:27729920). kcat is 8.81x10(-3) min(-1) with phloroacetophenone as substrate (with acetyl-CoA as cosubstrate) (PubMed:27729920). kcat is 0.405 min(-1) with 4-hydroxy-6-propyl-2-pyrone as substrate (with butyryl-CoA as cosubstrate) (PubMed:27729920). kcat is 0.289 min(-1) with 4-hydroxy-6-pentyl-2-pyrone as substrate (with hexanoyl-CoA as cosubstrate) (PubMed:27729920). {ECO:0000269|PubMed:27729920};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:27729920}.

FUNCTION: Involved in the biosynthesis of acetate-derived aromatic tetraketides natural products, precursors of daurichromenic acid, an anti-human immunodeficiency viruses (HIV) meroterpenoid consisting of sesquiterpene and orsellinic acid (OSA) moieties (PubMed:27729920). Accepts acetyl-CoA as starter substrate and produces orcinol as the major reaction product, along with four minor products including OSA, tetraacetate lactone, triacetate lactone and 2-acetylphloroglucinol (PubMed:27729920). {ECO:0000269|PubMed:27729920}.

Rhododendron dauricum (Azalea daurica)

A0A2Z5XAU0

PHM7_PYRSX

MSEPTSSSSLDITSNCIIETPLQPSDFLPKSANLFPKFPERISVDSWELWEFDTFDTNGSVAFGCSLYRDARGVEQGGFHAEVNALWPDGTHWGETLYFAVSEVVENSDGTTGGKWLSKDGGSITFHIASDYTAAALDFNVPGKVSGTMELRNHANVSPTSNLPASDAEAQLCPGVYYTFPMGPVATSVTATFSSVGANGESRELFISSGYGGMVRGWSARPWPTFMNDAYYVVAQVGPYMLQILRTLGSVFVQHKPFAVARLYLDGSLVSAANTVVGDELTAHADDVKGDAVRLTKVQPDEKSQGLSGKFRDGNVGYVLEFAKKDSEHGWTFQISHKRAVWSEPTSAPGPDGTGKSGWIEAISGGAKGENYEGHGFGGQLQIPVP

5.5.1.-

isomerase activity [GO:0016853]

Diels-Alderase family

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29972614}.

FUNCTION: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of the trans-fused decalin-containing tetramic acid phomasetin, the stereochemical opposite of the HIV-1 integrase inhibitor equisetin (PubMed:29972614). The PKS module of phm1 together with the enoylreductase phm4 catalyze the formation of the polyketide unit which is then conjugated to L-serine by the condensation domain of the phm1 NRPS module (PubMed:29972614). Activity of the Dieckmann cyclase domain (RED) of phm1 results in release of the Dieckmann product intermediate (PubMed:29972614). The Diels-Alderase phm7 then uses the Dieckmann product of phm1 as substrate and catalyzes the Diels-Alder cycloaddition to form the decalin ring of N-desmethylphomasetin (PubMed:29972614, PubMed:34121297). N-desmethylphomasetin is further methylated to phomasetin by the methyltransferase phm5 (PubMed:29972614). {ECO:0000269|PubMed:29972614, ECO:0000269|PubMed:34121297}.

Pyrenochaetopsis sp

A0A2Z5Z9X0

ACT1_CRIJA

MNRLIILCLVAATIYSTIALPMKEDISNEERPTSVNEKPVKKSVAVAGAVIQGAALAFQVLDKILTSLGGIGRKIAIGVDNESGMKWAARNVYFYSGTSDTVLPYSVPHSKAFLYGARKTRGSVRGAVGVLAYSMSDGNTLGILFSVPYDYNWYSNWWNIKVYRGYKRANKWMYHDLYYYARPHKGNNEWHEKSLGYGLKSKGFMTSSGQTKLEIRVSRA

cytolysis in another organism [GO:0051715]; monoatomic cation transport [GO:0006812]; pore complex assembly [GO:0046931]

extracellular region [GO:0005576]; nematocyst [GO:0042151]; other organism cell membrane [GO:0044218]; pore complex [GO:0046930]

channel activity [GO:0015267]; toxin activity [GO:0090729]

PF06369;

2.60.270.20;

Actinoporin family, Sea anemone subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29649486}. Nematocyst {ECO:0000250|UniProtKB:P07845}. Target cell membrane {ECO:0000305|PubMed:29649486}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000250|UniProtKB:B9W5G6}.

FUNCTION: Probably acts in predation (PubMed:29649486). Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers (By similarity). Shows hemolytic activity on equine erythrocytes (PubMed:29649486). Hemolysis is moderately inhibited in presence of sphingomyelin, suggesting that this protein targets sphingomyelin (PubMed:29649486). {ECO:0000250|UniProtKB:Q86FQ0, ECO:0000269|PubMed:29649486, ECO:0000305|PubMed:29649486}.

Cribrinopsis japonica (Deep-sea anemone)

A0A336U966

TYRP_ASPTE

MGFYRNLVLVAASCTQALGLCPAPRCDSPDIRHEWGELSREDRLSYISAVQCMKDRPPELSVEEVPAVRSRYDDFTAVHINYTLQIHNSGIFLPWHRHFIWLWEKALREECGFTGTLPYWDWVMWPNLAASPLFDGTETSLSGDGEFNATEQPTELNPEPGLTITIPRGAGGGCVRTGPFKDWVINMGPFAFNESYEPALPDHAFDYNPRCLVRSLNDWVIQTYNNQTVVDTLLDSPDIVEFQNIMGGFPNPPIPIGPHAMGHRSLGPDMLDFFASPQDPAFWQHHGMVDRLWTVWQDADEPWRRFALNGSSTTWYKDDTPEVTLQTTVEFGILDEPRPLYELMSPTAGPYCYTYT

1.14.18.-

COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q9ZP19}; Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};

endoplasmic reticulum lumen [GO:0005788]; Golgi lumen [GO:0005796]

metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]

PF00264;

1.10.1280.10;

Tyrosinase family

PTM: Glycosylated. {ECO:0000269|PubMed:27133313}.

SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Golgi apparatus lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Note=The oxidizing environment of Golgi or endoplasmic reticulum (ER) is required for tyrP to be active. {ECO:0000269|PubMed:29270299}.

CATALYTIC ACTIVITY: Reaction=aspulvinone E + O2 = (5Z)-3-(3,4-dihydroxyphenyl)-5-[(3,4-dihydroxyphenyl)methylidene]-5-oxo-2,5-dihydrofuran-3-olate; Xref=Rhea:RHEA:74195, ChEBI:CHEBI:15379, ChEBI:CHEBI:58240, ChEBI:CHEBI:193114; Evidence={ECO:0000269|PubMed:27133313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74196; Evidence={ECO:0000269|PubMed:27133313}; CATALYTIC ACTIVITY: Reaction=aspulvinone E + O2 = (2Z)-2-[(3,4-dioxocyclohexa-1,5-dien-1-yl)methylidene]-4-(4-hydroxyphenyl)-5-oxo-2,5-dihydrofuran-3-olate + H2O; Xref=Rhea:RHEA:74199, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:58240, ChEBI:CHEBI:193115; Evidence={ECO:0000269|PubMed:27133313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74200; Evidence={ECO:0000269|PubMed:27133313};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-7. {ECO:0000269|PubMed:27133313};

FUNCTION: Tyrosinase; part of the gene cluster that mediates the biosynthesis of Asp-melanin, a pigment that confers resistance against UV light and hampers phagocytosis by soil amoeba (PubMed:27133313, PubMed:29270299). The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:27133313, PubMed:29270299). The tyrosinase tyrP then performs hydroxylations of both aromatic moieties of aspulvinone E (PubMed:27133313). The product of tyrP is highly unstable, and, due to the high reactivity of methides and ortho-diquinones, the polymeric Asp-melanin forms spontaneously (PubMed:27133313). {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}.

Aspergillus terreus

A0A343URW6

TEX1_CATRO

MEFVVSLFAFVVSCFILLKVAKNSKNPKRNTNLELPPGPKQLPIIGNLHQLGGGLAHHVLRNLGKQYGPLMHLKIGELSTIVVSSTEIAKEVFKTHDIHFSNRPSHILVFKIVSYDYKDIVLSQYGKYWRELRKVCNLELLSPNRVQSFRSIREDAVLNMMKSISSNDGKVVNLSEMILSLIYGITARAAFGVWSKKHEEFIRLESEIQRLATTFVLADMFPSIKFLGALSGLRYKVEKVHKKVDDILEGILKEHRRQNNNMTEENGKKDLVDVLLNIQKNGDMETPFTDQHIKAIIFDMFSAGTLTSTIAVDWAMAEMMKNPSVLKRAQDEVRNVYNGIGNVDESKLDELKYLQAVIKETLRIHPGTPIVHRETREECEINGYRIPAKARVMVNAWAISRDPNYWPEPDIFKPERFLGSEVDFKGTHFEYIPFGAGRRICPGISYAIANVQLPLAQLLYHFEWKLPGGMKPEELDMTEILGTAAQRKENLLLIPNSHSCSSLKQV

1.14.14.-

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242};

indole alkaloid biosynthetic process [GO:0035835]

endoplasmic reticulum membrane [GO:0005789]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29934299}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + lochnericine + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61056, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:57893, ChEBI:CHEBI:58210, ChEBI:CHEBI:144374; Evidence={ECO:0000269|PubMed:29934299, ECO:0000269|PubMed:31009114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61057; Evidence={ECO:0000269|PubMed:29934299, ECO:0000269|PubMed:31009114};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.08 uM for tabersonine (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:29934299}; Vmax=0.254 pmol/sec/ug enzyme with tabersonine as substrate (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:29934299};

PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31009114}.

FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Cytochrome P450 catalyzing the conversion of tabersonine to lochnericine (PubMed:29934299, PubMed:31009114). {ECO:0000269|PubMed:29934299, ECO:0000269|PubMed:31009114}.

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

A0A348FUE1

PVCPS_TALVE

MSPMDLQESAAALVRQLGERVEDRRGFGFMSPAIYDTAWVSMISKTIDDQKTWLFAECFQYILSHQLEDGGWAMYASEIDAILNTSASLLSLKRHLSNPYQITSITQEDLSARINRAQNALQKLLNEWNVDSTLHVGFEILVPALLRYLEDEGIAFAFSGRERLLEIEKQKLSKFKAQYLYLPIKVTALHSLEAFIGAIEFDKVSHHKVSGAFMASPSSTAAYMMHATQWDDECEDYLRHVIAHASGKGSGGVPSAFPSTIFESVWPLSTLLKVGYDLNSAPFIEKIRSYLHDAYIAEKGILGFTPFVGADADDTATTILVLNLLNQPVSVDAMLKEFEEEHHFKTYSQERNPSFSANCNVLLALLYSQEPSLYSAQIEKAIRFLYKQFTDSEMDVRDKWNLSPYYSWMLMTQAITRLTTLQKTSKLSTLRDDSISKGLISLLFRIASTVVKDQKPGGSWGTRASKEETAYAVLILTYAFYLDEVTESLRHDIKIAIENGCSFLSERTMQSDSEWLWVEKVTYKSEVLSEAYILAALKRAADLPDENAEAAPVINGISTNGFEHTDRINGKLKVNGTNGTNGSHETNGINGTHEIEQINGVNGTNGHSDVPHDTNGWVEEPTAINETNGHYVNGTNHETPLTNGISNGDSVSVHTDHSDSYYQRSDWTADEEQILLGPFDYLESLPGKNMRSQLIQSFNTWLKVPTESLDVIIKVISMLHTASLLIDDIQDQSILRRGQPVAHSIFGTAQAMNSGNYVYFLALREVQKLQNPKAISIYVDSLIDLHRGQGMELFWRDSLMCPTEEQYLDMVANKTGGLFCLAIQLMQAEATIQVDFIPLVRLLGIIFQICDDYLNLKSTAYTDNKGLCEDLTEGKFSFPIIHSIRSNPGNRQLINILKQKPREDDIKRYALSYMESTNSFEYTRGVVRKLKTEAIDTIQGLEKHGLEENIGIRKILARMSLEL

2.5.1.29; 5.5.1.12

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 4 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};

alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744]

mitochondrion [GO:0005739]; transferase complex [GO:1990234]

isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659]

PF00348;

1.50.10.160;1.50.10.20;1.10.600.10;

Terpene synthase family; FPP/GGPP synthase family

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654; Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464}; CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635, ChEBI:CHEBI:58756; EC=5.5.1.12; Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24317; Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for DMAPP (for prenyltransferase activity) {ECO:0000269|PubMed:31978464}; KM=190 uM for IPP (for prenyltransferase activity) {ECO:0000269|PubMed:31978464};

FUNCTION: Bifunctional terpene synthase that possesses both prenyltransferase and type II terpene cyclase activity, converting isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into geranylgeranyl diphosphate (GGPP) and further converting GGPP into copalyl diphosphate, respectively. {ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464}.

Talaromyces verruculosus (Penicillium verruculosum)

A0A383ZFX3

ASAH1_BALAS

MLGRSRLTFVLLSVTVTCSVAQHVPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMVDKAPALKVIVNYLKNMINAFEPSGKIVQLVDQKLPGLLGSFPGPFEEEMKGIAAVTEIPLGEIILFNIFYEFFTICTSIITEDKEGHLLHARNMDFGVFLGWNVNNNTWVVTEELKPLTVNLDFQRNSKTVFKAAGFAGYVGMLTGFKPGLFSLTLNERFSTNGGFMGVIEWILGKKDAKWIGFIIRSVLENSTSYEEAKTILTKSKILAPAYFILGGSKSGEGCVITRDRVQSLDIYELDPKQGIWYVVQTNYDRWKNPFFLDNRRTPAKMCLNRTTQENISFATMYDVLSTKPVLNKLTVYTALIDVTKGQFETYLRDCPDPCIGW

3.5.1.-; 3.5.1.23

fatty acid metabolic process [GO:0006631]; sphingolipid metabolic process [GO:0006665]

extracellular region [GO:0005576]; lysosome [GO:0005764]

ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-acylsphingosine amidohydrolase activity [GO:0017040]

PF02275;PF15508;

Acid ceramidase family

PTM: N-glycosylated. {ECO:0000269|PubMed:29692406}.; PTM: Proteolytically cleaved into two chains alpha and beta that remain associated via a disulfide bond (PubMed:29692406). Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates. The beta chain may undergo an additional C-terminal processing (By similarity). {ECO:0000250|UniProtKB:Q13510, ECO:0000269|PubMed:29692406}.

SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000250|UniProtKB:Q13510}.

CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57756, ChEBI:CHEBI:72956; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41293; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetradecanoylsphing-4-enine = sphing-4-enine + tetradecanoate; Xref=Rhea:RHEA:41287, ChEBI:CHEBI:15377, ChEBI:CHEBI:30807, ChEBI:CHEBI:57756, ChEBI:CHEBI:72957; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41289; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:72959; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38893; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoylsphing-4-enine = octadecanoate + sphing-4-enine; Xref=Rhea:RHEA:41279, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629, ChEBI:CHEBI:57756, ChEBI:CHEBI:72961; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41280; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41281; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoyl-(4R)-hydroxysphinganine = (4R)-hydroxysphinganine + dodecanoate; Xref=Rhea:RHEA:41303, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:64124, ChEBI:CHEBI:78001; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41305; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(dodecanoyl)-sphinganine = dodecanoate + sphinganine; Xref=Rhea:RHEA:45448, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57817, ChEBI:CHEBI:85261; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45450; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(acetyl)-sphing-4-enine = acetate + sphing-4-enine; Xref=Rhea:RHEA:58484, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58485; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(hexanoyl)sphing-4-enine = hexanoate + sphing-4-enine; Xref=Rhea:RHEA:41295, ChEBI:CHEBI:15377, ChEBI:CHEBI:17120, ChEBI:CHEBI:57756, ChEBI:CHEBI:63867; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41296; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-octanoylsphing-4-enine = octanoate + sphing-4-enine; Xref=Rhea:RHEA:45092, ChEBI:CHEBI:15377, ChEBI:CHEBI:25646, ChEBI:CHEBI:45815, ChEBI:CHEBI:57756; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45093; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine; Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57603, ChEBI:CHEBI:85263; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457; Evidence={ECO:0000250|UniProtKB:Q13510};

PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q13510}.

FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (By similarity). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (By similarity). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (By similarity). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (By similarity). Has also an N-acylethanolamine hydrolase activity (By similarity). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (By similarity). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (By similarity). {ECO:0000250|UniProtKB:Q13510}.

Balaenoptera acutorostrata scammoni (North Pacific minke whale) (Balaenoptera davidsoni)

A0A384E129

O16A_CONMB

MKLTCVVIVAVLFLTACQLITADDSRSTQRHRALRSTTKLSMSTRCKPPGSKCSPSMRDCCTTCISYTKRCRKYYN

extracellular region [GO:0005576]

calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729]

PF02950;

Conotoxin O1 superfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30194442}.

FUNCTION: [Omega-conotoxin MoVIA]: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin potently blocks mammalian N-type calcium channels (Cav2.2/CACNA1B) (IC(50)=330 nM on human channels). It is 9-fold more potent in displacing radiolabeled omega-conotoxin GVIA from fish brain membranes than from human SH-SY5Y cells. {ECO:0000269|PubMed:30194442}.; FUNCTION: [Omega-conotoxin MoVIB]: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin potently blocks mammalian N-type calcium channels (Cav2.2/CACNA1B) (IC(50)=600 nM on human channels). It is 60-fold more potent in displacing radiolabeled omega-conotoxin GVIA from fish brain membranes than from human SH-SY5Y cells. In vivo, when tested on rat neuropathic pain model, this toxin shows an analgesic activity (PubMed:30194442). {ECO:0000269|PubMed:30194442}.

Conus moncuri (Sea snail)

A0A386CAB9

NLRP1_DANRE

MSSDYTDRNNLASAIKTLGDMLEKDEAFQRLMYNASTKGEINRGRVNKVFLKALLSAGDKVGEFLNELIDHLNLFKVLGDFSWNPPVLKEAELNERTSQLRTQQHKYVERVSGFSHYGFGETGTPARGDITSPRGPQVASIEEDLATSKLAELLLAVGDHLEKIEKKGQFLPENVERFSLDCFITSESVKLSSEAVELAPCYTEPVIIQRSKEQTEKYCQEYVRSPHTSSHLLSNDKTQSIRIGQLFSPDSDGNTPKTVILCGDSGRGKSFVLEKIILDWVHLEHHFENFDAVFLLKYEELKCLSEEMSLTELLSRSCSLTSDQISQILQLTPEKVLFLIDGIDDFSFNAHIQISSPTDPSQKAPVISIIHCLMRDLLLVESSVIVTTRYTAAAELSSLCKRPQRFTEIEGFSERRVQEYFQKFFQDEQLFKKAYESMKTNETLLTFCSVPLLCWMVCFCLKKDADQVMTELKTTTSIYVHFVSTLLEDHHQSQSFLRSLGQLAEEGMKNRQNLFDEKSVTRTGLDPATRVFMNKIYLKRKKKHELLFKFKHLSFQEFFAALYYIMLDEEESWCKVSELFNMMESEALIHRSPPIFRGRLSNPIPSVMMFLCGLFNKKVSSSLFEKMKSTFSHNVKLKKKELKKKLMKMIPAMIRQYGFELFALHCLYELQDERFVTKVLETHKFIDLSNVSLRSTDCLVLCYCLRLCPNIRELNFMNCDLTAAKLKILQPALGLCETLRFSVEHLSEIGDLIQILSESKILRELKVREDEYGVESPRWSFNLSVTRGDVLLTLSSSEKNPSFSSVLNIRLTCAQSQISRTDWTLFLQRLRKTGTLTEDSSADDDHVSLQLSSLHSVGLKSLDLTLVSLNESWASGIISLIQNCTSLQQLKVSVTGLLLEEGLKLLKKSLTDPHCTVIIEGRRNCSEPSEEHLRQSYEKVEIHFKPKLLEELAELSICNPGSSALNIHCQSCVDVADSDQWVQVEPSVCRGEGGTEFRITTPAGRFQCSRTRMRWVCDGDVTLHYRAVDGHFLNAELERLQCERVAPVLDVNVISGKLEEAHLPHYMCLAESDPALTNAVKLLSVEDEGISLESVELTRFHAKILQPMFSPKTVLVKLGIPVKVHCDLLIFMTHTCPIILNVYFFPSDSLVEENIKTEEKSSHQIKCSRPEAPLQMKKQHSLEVPDAVVQPEAIKLRGNMKPNFFQVKQPVVNDITMILSRVDDQKSVWTGTIWKKLIDIKLNKTESDLFQSGQKHKTSQPAHSFDKAQFFDTHWCNLIKSVENVDTVADKLLQKQIIHEQFYSEIIHHKSTSEESMRKICVIVRKGSAAVKEIFISILLQENPNLLNHLPSSDS

3.4.-.-

inflammatory response [GO:0006954]; innate immune response [GO:0045087]; pattern recognition receptor signaling pathway [GO:0002221]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; programmed cell death [GO:0012501]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]

canonical inflammasome complex [GO:0061702]; cytoplasm [GO:0005737]; NLRP1 inflammasome complex [GO:0072558]

ATP binding [GO:0005524]; peptidase activity [GO:0008233]

PF00619;PF13553;PF05729;PF17776;PF17779;

1.10.533.10;3.40.50.300;3.80.10.10;

NLRP family

PTM: [NACHT, LRR and PYD domains-containing protein 1 homolog]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating pro-inflammatory caspases (caspa and/or caspb) binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000250|UniProtKB:Q9C000}.; PTM: [NACHT, LRR and PYD domains-containing protein 1, N-terminus]: Ubiquitinated in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and forms the nlrp1 inflammasome. {ECO:0000250|UniProtKB:Q9C000}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, caspa and caspb in the cytoplasm. {ECO:0000269|PubMed:30150286}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Inflammasome {ECO:0000269|PubMed:30150286}.

FUNCTION: Acts as the sensor component of the nlrp1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed:30150286). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:30150286). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, and mediates the formation of the inflammasome polymeric complex (By similarity). In response to pathogen-associated signals, the N-terminal part of nlrp1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome recruits and activate pro-inflammatory caspases (caspa and/or caspb), leading to pyroptosis (By similarity). {ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:30150286}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1 homolog]: Constitutes the precursor of the nlrp1 inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1, N-terminus]: Regulatory part that prevents formation of the nlrp1 inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, C-terminus), preventing activation of the nlrp1 inflammasome (By similarity). In response to pathogen-associated signals, this part is ubiquitinated and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the nlrp1 inflammasome (By similarity). {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Constitutes the active part of the nlrp1 inflammasome (By similarity). In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, N-terminus), preventing activation of the nlrp1 inflammasome (By similarity). In response to pathogen-associated signals, the N-terminal part of nlrp1 is degraded by the proteasome, releasing this form, which polymerizes to form the nlrp1 inflammasome complex: the nlrp1 inflammasome complex then directly recruits and activates pro-inflammatory caspases (caspa and/or caspb) activation, leading to subsequent pyroptosis (By similarity). {ECO:0000250|UniProtKB:Q9C000}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A386KZ50

DABA_PSEMU

MKFATSIVAAIATTGAAFTVIPQKLSHPSQLNALNTMGSISSITAESPKEVLSRVQDAGLTLTNPNDLYWMVDFLKEKYYDNGDYYYPIKTVCDGESIDVKFYCPFEPSLSPHYLELYGSRDERASIYETTMKKYNRINSEKTSAICTPYSSYGDTQIVAYFYSMMYYINDQTAHLKLPESEIESELIDILNDDILIYLNEFMSIFEPEDAQDLERIWDFLDFYQPYFSKVDGKIVLDEKYLVRTPSQMPLIKTICEYVSEQFAPSKNITQVIWEVVRYIKGVKDEIHIRGDKSFTLSLQEYDDFRDKVTASPMAHAVSDLTHERFSYEAYTNPAFMELENRCSEIITYFNDVCTSDRERLDEDPFNSVFILMDLDPSLNFAKSCDVVVEHAYNKMQAFLKLKEEILESASDEEERLALARMIKTREDSLIGYVLHEVCCVEDGYARDHKPLMKAFLEEEITKSLAEKVKFNPVESESVRLN

2.5.1.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32457155}; Note=Can also use Mn(2+) ions as cofactors with a lower efficiency. {ECO:0000269|PubMed:32457155};

cellular response to carbon dioxide [GO:0071244]; cellular response to phosphate starvation [GO:0016036]

metal ion binding [GO:0046872]; transferase activity [GO:0016740]

PF19086;

1.10.600.10;

Terpene synthase family

CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + L-glutamate = diphosphate + N-geranyl-L-glutamate; Xref=Rhea:RHEA:68156, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:172365; Evidence={ECO:0000269|PubMed:30262498, ECO:0000269|PubMed:32457155}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68157; Evidence={ECO:0000269|PubMed:30262498, ECO:0000269|PubMed:32457155};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 uM for geranyl diphosphate {ECO:0000269|PubMed:32457155}; KM=21 mM for L-glutamic acid {ECO:0000269|PubMed:32457155}; Note=kcat is 4.3 min(-1) with geranyl diphosphate as substrate (PubMed:32457155). kcat is 4.8 min(-1) with L-glutamic acid as substrate (PubMed:32457155). {ECO:0000269|PubMed:32457155};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30262498}.

FUNCTION: Magnesium-dependent glutamate N-prenyltransferase: part of the gene cluster that mediates the biosynthesis of domoic acid (DA) and derivatives, natural products with neurochemical activity acting as ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins causing amnesic shellfish poisoning (ASP) (PubMed:30262498). Catalyzes the conversion of L-glutamic acid (L-Glu) to N-geranyl-L-glutamic acid (NGG) in the presence of geranyl diphosphate (GPP) (PubMed:30262498, PubMed:32457155). Also able to catalyze the formation of farnesyl-L-glutamate from farnesyl diphosphate (FPP) (PubMed:32457155). Cannot use dimethylallyl diphosphate (DMAPP) as substrate (PubMed:32457155). {ECO:0000269|PubMed:30262498, ECO:0000269|PubMed:32457155}.

Pseudo-nitzschia multiseries (Marine planktonic diatom) (Nitzschia pungens f. multiseries)

A0A396GMX6

DELA2_MEDTR

MKREHKLEHEDMSSGSGKSGVCWEDDGGGMDELLAVVGYKVKSSDMAEVAQKLEQLEQAMMGNNFHDHDESTIAQHLSNDTVHYNPSDISNWLQTMLSNFDPQPNNPSVNSDDNDLNAIPGKAIYAADEFTSRKRVKRNESVTVTTESTTTRPIMVVETQEKGIRLVHSLMACAEAVEQNNLKMAEALVKQIGYLAVSQEGAMRKVATYFAEGLARRIYGVFPQHSVSDSLQIHFYETCPNLKFAHFTANQAILEAFQGKSSVHVIDFSINQGMQWPALMQALALRPGGPPAFRLTGIGPPASDNSDHLQQVGWRLAQFAQTIHVQFEYRGFVANSLADLDASMLELRSPETESVAVNSVFELHKLNARPGALEKVFSVIRQIRPEIVTVVEQEANHNGPAFLDRFTESLHYYSTLFDSLEGSSVEPQDKAMSEVYLGKQICNVVACEGTDRVERHETLNQWRNRFNSAGFSPVHLGSNAFKQASMLLALFAGGDGYKVEENDGCLMLGWHTRPLIATSAWKLAAANSVVVSH

arbuscular mycorrhizal association [GO:0036377]; cellular response to phosphate starvation [GO:0016036]; gibberellic acid mediated signaling pathway [GO:0009740]; hyperosmotic salinity response [GO:0042538]; jasmonic acid mediated signaling pathway [GO:0009867]; negative regulation of gibberellic acid mediated signaling pathway [GO:0009938]; negative regulation of seed germination [GO:0010187]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of seed dormancy process [GO:2000033]; response to abscisic acid [GO:0009737]; response to ethylene [GO:0009723]; response to symbiotic fungus [GO:0009610]; salicylic acid mediated signaling pathway [GO:0009863]

nucleus [GO:0005634]

DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]

PF12041;PF03514;

1.10.10.1290;

GRAS family, DELLA subfamily

PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to its subsequent degradation. {ECO:0000250|UniProtKB:Q7G7J6}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A396IUP1}.

FUNCTION: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway (By similarity). Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes (By similarity). Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway (By similarity). Together with DELLA1, required to enable arbuscule development during arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme) via the regulation of RAM1 which, in turn, regulates various AM genes (e.g. NSP1, NSP2, PT4, LEC5, RAM2, EXO70I, STR and RAD1) (PubMed:24297892). {ECO:0000250|UniProtKB:Q7G7J6, ECO:0000269|PubMed:24297892}.

Medicago truncatula (Barrel medic) (Medicago tribuloides)

A0A396IUP1

DELA1_MEDTR

MKREHQESFGGGVISNNNKTNTNHLNSSKNINFGECSSMQNTNTKQNMWREEKETNGGGMDELLAALGYKVRSSDMADVAQKLEQLEMVMGSAQEEGINHLSSDTVHYDPTDLYSWVQTMLTELNPDSSQINDPLASLGSSSEILNNTFNDDSEYDLSAIPGMAAYPPQEENTAAKRMKTWSEPESEPAVVMSPPPAVENTRPVVLVDTQETGVRLVHTLMACAEAIQQKNLKLAEALVKHISLLASLQTGAMRKVASYFAQALARRIYGNPEETIDSSFSEILHMHFYESSPYLKFAHFTANQAILEAFAGAGRVHVIDFGLKQGMQWPALMQALALRPGGPPTFRLTGIGPPQADNTDALQQVGWKLAQLAQTIGVQFEFRGFVCNSIADLDPNMLEIRPGEAVAVNSVFELHTMLARPGSVEKVLNTVKKINPKIVTIVEQEANHNGPVFVDRFTEALHYYSSLFDSLEGSNSSSNNSNSNSTGLGSPSQDLLMSEIYLGKQICNVVAYEGVDRVERHETLTQWRSRMGSAGFEPVHLGSNAFKQASTLLALFAGGDGYRVEENNGCLMLGWHTRSLIATSAWKLPQNESK

arbuscular mycorrhizal association [GO:0036377]; cellular response to phosphate starvation [GO:0016036]; gibberellic acid mediated signaling pathway [GO:0009740]; hyperosmotic salinity response [GO:0042538]; jasmonic acid mediated signaling pathway [GO:0009867]; negative regulation of gibberellic acid mediated signaling pathway [GO:0009938]; negative regulation of seed germination [GO:0010187]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of seed dormancy process [GO:2000033]; regulation of transcription by RNA polymerase II [GO:0006357]; response to abscisic acid [GO:0009737]; response to ethylene [GO:0009723]; response to symbiotic fungus [GO:0009610]; salicylic acid mediated signaling pathway [GO:0009863]

nucleus [GO:0005634]

DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]

PF12041;PF03514;

1.10.10.1290;

GRAS family, DELLA subfamily

PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to its subsequent degradation. {ECO:0000250|UniProtKB:Q7G7J6}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24297892}.

FUNCTION: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway (By similarity). Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes (By similarity). Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway (By similarity). Together with DELLA2, required to enable arbuscule development during arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme) via the regulation of RAM1 which, in turn, regulates various AM genes (e.g. NSP1, NSP2, PT4, LEC5, RAM2, EXO70I, STR and RAD1) (PubMed:24297892, PubMed:26511916). {ECO:0000250|UniProtKB:Q7G7J6, ECO:0000269|PubMed:24297892, ECO:0000269|PubMed:26511916}.

Medicago truncatula (Barrel medic) (Medicago tribuloides)

A0A396JG59

EX70I_MEDTR

MHKKQLMALLMVPQTSDSQDATITKLESAYSDLESLLRSSKQMEQNIETMETRFDLLHGSITTASRRVHPLQSLSMSRKALDTRINRAISPALALLETFKLAESLQNNLLNLSSKLSTEKTHQKRLSKLLDYMDCVDQLNEAINSISEVVEPVIMRLQEVVEFISRTKAADQYRTQRLREALITLKALYETEVDEMRFEGLLDQALLHMQDEFEVLLLKLKHRKLGDMSHMQNGGEDCDDHFEVSFELGSELEIEVLRRISNTLAANDCLDICIDIYVKVRYKRAAKALMKLNPDYLRTYTPEGIDEMEWENLETSITLWTQHFEVATKKVLLSEKKLCESVLGEIIDGLIHPECFVKISDKIMAVFFRFGEGVARSNKEPQKLFKLLDMFESLEKLKPYVLEIFDGESGEDICARFRELEKLIIDASSKVFWEFGLQIEGNVDGFLPPPQDGSVPKIVRYAVNYLKYLSTENYRTTMAKVLRTELTWKTELMLSSKQSETDEDLLKHAICNVMEALQRNIESKRLSCKDKILVNIFMMNTYWYMYMRTKNTELGDLLGEKYIKESYKAVAEESAYLYQKQAWLVLVKILDQDDDDIKEQKQGKEKSIGRLVNEKIETFFKCLSEICDRHRSFYSIPDVDLREQMRDSTVKLLVPVYAEFLESYSGFLQRKVYPSPQRLQGLLGKAFGSTNDWNLNGGRNSGSLETDIRRSR

arbuscular mycorrhizal association [GO:0036377]; exocytosis [GO:0006887]; protein transport [GO:0015031]; response to symbiotic bacterium [GO:0009609]; response to symbiotic fungus [GO:0009610]

exocyst [GO:0000145]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886]

phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]

PF03081;

1.20.1280.170;

EXO70 family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26234213}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=During arbuscule branching, restricted to zones adjacent to the periarbuscular membrane (PAM) around the arbuscule hyphal tips. {ECO:0000269|PubMed:26234213}.

FUNCTION: Component of an exocyst subcomplex specifically required for periarbuscular membrane (PAM) biogenesis during arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme), especially critical during the early branching phase of arbuscule development; probably involved in STR and STR2 delivery into the PAM. {ECO:0000269|PubMed:26234213}.

Medicago truncatula (Barrel medic) (Medicago tribuloides)

A0A3B6UES5

VINC_OSCPE

MPVKFHTKTLESVIDPVAQQVGQLVLFHEQAESGLLKEDLTPLVQGVGIAVTNLVQVAASMVETSNDEDFKAELPPSMQEVQQAAVFLSDAARLLKADQGSPEGKRKLLDGARGVINGMSDLLMCADRSEVRKMVKVCRSVQEYLDVAKVIDVEADLATFLQNLTPGMTSMMKVVEQRHPELTNLAHAQMLKSELGTVREQIPILISSIRVCCLVIVKDGSSGMKDAAFGRDYVIQKLFIAIEEIIRVLQLTTTFEEEEVGGAGAASAASLAHMFHQAQDALASGDISRSTLDAVRKCISEGRRVAALAATDETRAKLLAAADELDQILKELEELQAKGLGDSRQARALAHAAAVKLQELEQEIRKALAERVATDFVNVGGPIKALEDAALASPSDPNRQANFAQKAKEFEAHTARLADTAELVASSGGCSDAVAAELRKEAAKLRDISTAVVPAARVVLENPGNQAAKDYLRTVKEKWLEAAESMGRSVDGVIDSLEFMKVSEARIQADVKEAKRIALAEEDSMKLIAKASSVARQANRVIQVAKVEADNSENPEFVAKLSSASESLAKSISPMVIEAKAVVTSPQNKDIQRKFCSSADKVVEGVAAVRSVIEDNWVPPRPPLPELEEEEEPPELPPPPEDPASLLPAEMQEAEEMLRAPLPPKDQNPIHHAAASVFREADQWDEKGNDLISLVKQMARKMAMMSKYTRGESGEVRSKADLIRMAKEIALNAQELLKLARQIANACMDKRAKTNLLQLLDRIPTISTQLKILATVKATSMGGGDARADADATDMLVGNAENLMRTVKDVIRASEAACIRLRPDSPIASILWRKKGGQGRRISVSY

cell adhesion [GO:0007155]

adherens junction [GO:0005912]; cell-cell contact zone [GO:0044291]; cortical cytoskeleton [GO:0030863]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]

actin filament binding [GO:0051015]; alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]

PF01044;

1.20.120.230;1.20.120.810;

Vinculin/alpha-catenin family

SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:29880641}. Cell projection, filopodium {ECO:0000269|PubMed:29880641}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29880641}. Note=Localizes to points of cell-cell contact in the pinacoderm. Localizes to the base of the microvillar collar in choanocytes. Detected in filopodial extensions in migratory cells of the mesohyl. Colocalizes with F-actin. {ECO:0000269|PubMed:29880641}.

FUNCTION: Actin filament (F-actin)-binding protein which may play a role in cell-cell adhesion. {ECO:0000269|PubMed:29880641}.

Oscarella pearsei (Sponge)

A0A3B6UEU3

INLPE_STRC4

MQIDEQPGNAIGAAVEGFDHATASDADIDALKSTIYTKKIAVLKGQDLSPQQFLALGKRLGRPEAYYEPMYQHPEVTEIFVSSNVPENGKQIGVPKTGKFWHADYQFMPDPFGITLIYPQVIPEKNRGTYFIDMGRAYDRLPEDLKKEISGTYCRHSVRKYFKIRPHDVYRPISEIIEEVERKTPAVVQPTTFTHPMTGETVLYISEGFTVGIEDQDGKPLDEELLKRLFDATGQLDESFEHDNIHLQSFEQGDLLVWDNRSLIHRARHTTTPEPTVSYRVTVHDERKLHDGIQAA

1.14.11.78

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:29906336, ECO:0000269|PubMed:32074393, ECO:0000269|PubMed:33361191};

heterocycle metabolic process [GO:0046483]; organic cyclic compound metabolic process [GO:1901360]

dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872]

PF02668;

3.60.130.10;

TfdA dioxygenase family

CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + a (3R)-3-[(carboxymethyl)amino]fatty acid + 2 O2 = a (3R)-3-isocyanyl-fatty acid + 3 CO2 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:74931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:193080, ChEBI:CHEBI:193084; EC=1.14.11.78; Evidence={ECO:0000269|PubMed:29906336, ECO:0000269|PubMed:32074393, ECO:0000269|PubMed:33361191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74932; Evidence={ECO:0000305|PubMed:29906336}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a (3R)-3-[(carboxymethyl)amino]fatty acid + O2 = a (3R)-3-{[carboxy(hydroxy)methyl]amino}fatty acid + CO2 + succinate; Xref=Rhea:RHEA:74939, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:193080, ChEBI:CHEBI:193082; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74940; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a (3R)-3-{[carboxy(hydroxy)methyl]amino}fatty acid + O2 = a (3R)-3-isocyanyl-fatty acid + 2 CO2 + 2 H2O + succinate; Xref=Rhea:RHEA:74943, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:193082, ChEBI:CHEBI:193084; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74944; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191}; CATALYTIC ACTIVITY: Reaction=(3R)-3-[(carboxymethyl)amino]butanoate + 2 2-oxoglutarate + 2 O2 = (3R)-3-isocyanylbutanoate + 3 CO2 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:74935, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:193081, ChEBI:CHEBI:193085; EC=1.14.11.78; Evidence={ECO:0000269|PubMed:29906336, ECO:0000269|PubMed:32074393, ECO:0000269|PubMed:33361191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74936; Evidence={ECO:0000305|PubMed:29906336}; CATALYTIC ACTIVITY: Reaction=(3R)-3-[(carboxymethyl)amino]butanoate + 2-oxoglutarate + O2 = (3R)-3-{[carboxy(hydroxy)methyl]amino}butanoate + CO2 + succinate; Xref=Rhea:RHEA:74947, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:193081, ChEBI:CHEBI:193083; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74948; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191}; CATALYTIC ACTIVITY: Reaction=(3R)-3-{[carboxy(hydroxy)methyl]amino}butanoate + 2-oxoglutarate + O2 = (3R)-3-isocyanylbutanoate + 2 CO2 + 2 H2O + succinate; Xref=Rhea:RHEA:74951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:193083, ChEBI:CHEBI:193085; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74952; Evidence={ECO:0000305|PubMed:32074393, ECO:0000305|PubMed:33361191};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=286 uM for (3R)-3-[(carboxymethyl)amino]butanoate {ECO:0000269|PubMed:29906336}; KM=20.9 uM for 2-oxoglutarate {ECO:0000269|PubMed:29906336}; Note=kcat is 21.9 min(-1) with (3R)-3-[(carboxymethyl)amino]butanoate as substrate. {ECO:0000269|PubMed:29906336};

FUNCTION: Involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs) (PubMed:28634299). Catalyzes the conversion of (3R)-3-[(carboxymethyl)amino]fatty acids such as (3R)-3-[(carboxymethyl)amino]butanoate (CABA) to (3R)-3-isocyanylbutanoate (INBA) through an oxidative decarboxylation mechanism, thereby generating the isonitrile group of INLPs (PubMed:29906336, PubMed:32074393, PubMed:33361191). {ECO:0000269|PubMed:28634299, ECO:0000269|PubMed:29906336, ECO:0000269|PubMed:32074393, ECO:0000269|PubMed:33361191}.

Streptomyces coeruleorubidus

A0A3L7I2I8

PLPL9_CRIGR

MQFFGRLVNTLSSVTNLFSNPFRVKEISVADYTSHERVREEGQLILFQNASNRTWDCILVSPRNPHSGFRLFQLESEADALVNFQQFSSQLPPFYESSVQVLHVEVLQHLSDLIRSHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNSQVLQLLGKNASAGLNQVNKQGLTPLHLACQMGKQEMVRVLLLCNARCNVMGPSGFPIHTAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCDVDSTSAAGNTALHVAVMRNRFDCVMVLLTYGANAGTPGEHGNTPLHLAISKDNMEMIKALIVFGAEVDTPNDFGETPAFMASKISKLITRKALLSLLRTVGADHRFPLIQGVPTDQSSAATPHPIFSLDKTQPPAISLNNLELQDLMPISRARKPAFILSSMRDEKRIHDHLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEVIREPRFNQNINLKPPTQPADQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRKGQGNKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWSEMVGIQYFRLNPQLGSDIMLDEVNDAVLVNALWETEVYIYEHREEFQKLVQMLLSP

3.1.1.4; 3.1.1.5; 3.1.2.2

antibacterial humoral response [GO:0019731]; cardiolipin acyl-chain remodeling [GO:0035965]; cardiolipin biosynthetic process [GO:0032049]; phosphatidic acid metabolic process [GO:0046473]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylethanolamine catabolic process [GO:0046338]; platelet activating factor metabolic process [GO:0046469]; positive regulation of ceramide biosynthetic process [GO:2000304]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]

extracellular space [GO:0005615]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]

1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; calcium-independent phospholipase A2 activity [GO:0047499]; identical protein binding [GO:0042802]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; serine hydrolase activity [GO:0017171]

PF12796;PF01734;

1.25.40.20;3.40.1090.10;

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60733}. Cell membrane {ECO:0000250|UniProtKB:O60733}. Mitochondrion {ECO:0000250|UniProtKB:P97819}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:O60733}. Note=Recruited to the membrane-enriched pseudopods upon MCP1/CCL2 stimulation in monocytes. {ECO:0000250|UniProtKB:O60733}.

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-sn-glycero-3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:63304, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72859; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63305; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000305|PubMed:15908428, ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000305|PubMed:15908428, ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40831, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395, ChEBI:CHEBI:74344; Evidence={ECO:0000269|PubMed:15908428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40832; Evidence={ECO:0000305|PubMed:15908428}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40827, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395, ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:15908428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828; Evidence={ECO:0000305|PubMed:15908428}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:55430, ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9079687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000305|PubMed:9079687}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000250|UniProtKB:O60733}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000250|UniProtKB:O60733}; CATALYTIC ACTIVITY: Reaction=1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H(+); Xref=Rhea:RHEA:40463, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77253, ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:O60733}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40464; Evidence={ECO:0000250|UniProtKB:O60733}; CATALYTIC ACTIVITY: Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1',3'-bis-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H(+); Xref=Rhea:RHEA:40467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77256, ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:O60733}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40468; Evidence={ECO:0000250|UniProtKB:O60733}; CATALYTIC ACTIVITY: Reaction=1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H(+); Xref=Rhea:RHEA:52812, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:83580, ChEBI:CHEBI:83581; Evidence={ECO:0000250|UniProtKB:P97819}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:52814; Evidence={ECO:0000250|UniProtKB:P97819}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoethanolamine + 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+); Xref=Rhea:RHEA:63256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75036, ChEBI:CHEBI:78832, ChEBI:CHEBI:146277; Evidence={ECO:0000250|UniProtKB:P97570}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63257; Evidence={ECO:0000250|UniProtKB:P97570};

FUNCTION: Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles. Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position (PubMed:15908428, PubMed:9079687). Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity) (PubMed:9079687). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (By similarity). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species. Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (By similarity). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (By similarity). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (PubMed:9079687). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (By similarity). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types (PubMed:9079687). Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent pro-inflammatory signaling lipid (PubMed:9079687). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (By similarity). {ECO:0000250|UniProtKB:O60733, ECO:0000250|UniProtKB:P97570, ECO:0000250|UniProtKB:P97819, ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:9079687}.

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

A0A3Q0KDV9

SEP10_SCHMA

MTADVLKALPPDVRTLKLSGHVGFDSLPDQLVNKAISQGFVFNILCVGETGIGKSTLLETLFNQKFDFSPSNHDLTDPKLKAVTYDLKEANVKLKLTVVETCGYGDQINKENNIKPVVDYIDNQFENYLQEELKMKRSMQAFHDTRVHVCLYFIAPTGHSLKSIDLVAMKKLENKVNVIPVIAKSDTITKSELQKFKARILSEIQSNEIGIYQFPTDDEAVSETNSVMNQHIPFAVVGSSEEVKINGKTVRVRQYPWGSVQVENENHCDFVRLREMLLRVNMEDLRERTHGVHYETYRRQRLIEMGFRDDEKMSLQETYEKRRELQRKELQQKEEEMRQMFVQRVKEKEQVLKEAERELQTKFESLKKTHAEEKKKLEEKKRFLEEEIAAFERRKQLAEQARQGNLTMKKRK

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24464615}; Note=Mg(2+) is essential for the GTP-binding, but GDP-binding does not require a metal cofactor. {ECO:0000269|PubMed:24464615};

cytoskeleton-dependent cytokinesis [GO:0061640]; protein homooligomerization [GO:0051260]

cell division site [GO:0032153]; microtubule cytoskeleton [GO:0015630]; septin complex [GO:0031105]; septin ring [GO:0005940]; vesicle [GO:0031982]

GDP binding [GO:0019003]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; molecular adaptor activity [GO:0060090]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]

PF00735;

3.40.50.300;

TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8C1B7}. Note=Colocalizes with actin in the longitudinal and circular muscles of the sporocyst. {ECO:0000269|PubMed:24367716}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable at wide pH range from 4 to 9. {ECO:0000269|PubMed:27687162};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Temperature-sensitive. Stable at 15 degrees Celsius. Starts to aggregate at 37 degrees Celsius. {ECO:0000269|PubMed:27687162};

FUNCTION: Filament-forming GTP-binding protein. Lacks GTPase activity, which is likely due to absence of an essential threonine residue important for hydrolytic activity in septins. May be involved in membrane remodeling, potentially by its nucleotide-dependent cellular membrane association/dissociation ability (PubMed:24464615). Able to bind to phosphatidylinositol-4,5-bisphosphate (PIP2)-containing giant unilamellar vesicles (GUVs), which serve as a model of biological membranes. Self-assembles into ordered cage-like structures on the vesicle membrane. Binds also to 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS)-containing vesicles suggesting the requirement for negatively charged membranes. Is also able to promote deformation of the GUVs (PubMed:27687162). {ECO:0000269|PubMed:24464615, ECO:0000269|PubMed:27687162}.

Schistosoma mansoni (Blood fluke)

A0A3Q0KR05

NPRS_SCHMA

MPQSTAQLKSPLLHTLLENLTQSSICTSTAIWHVPNPVNFVCNHNENSFDNKNNSVTTITTTDVSTNNHKNTNYDYEQQEQWSNEEINSNQESNEIYTMTFLKLNNAANRVAMNLANYLERKWSSITNKINRTQLNQHSLSIDEPIELRNQSDTVIALFMPPGIDRIVVQIACMKLHLAYMPLDRNVPAGRITQILHKLKPILILIDKDYYDFIYDDDHNDNDKMSDLSSSIDNNNKSLLSRKLSSNDFIIGNLNQLKLTFQLFDVKVYEYIKLMKLSKYYSRSDIYTASIPIRVCLFPFESDPIVLVLFTSGSTSSGPKPVKLRTTQLFNRLEWQWDSTSDMDLPNFENATCNSNTSVKRIGLAKTAWGFVDAFTELFSCLLAGIPVVVPGGSACPSEKSITDVQQLINLTKHFKISHITTVPTQMNLWLKQLRLKPKEIVTSHLSSLRTVIVSGDIVHPKMACEFFQLFKNPEMRLINLYGTTEVAGDVTGLVFRGEIDVKKHTKVVPCGLERENNKSGKPVLSVGTVIQGTAIFIVQDDDDHHLHHEKDNENQPDKWSNPSLSIIGSVDRKPNWDKFPFKILPKGHIGHVCILGQQVSDSASRCQRIESLPEDLNCVDTNKCKSDVESCENNSSKEIRVFMPGDLGFIDPQTNHLYICGRTNELIKINGIRFHANDIDNLFIELKKNWKAKNMTNCTREELLVNKVSETVTLTIQTVHGRDLKLVCFYVLHMNENQNTMNIEPKENYDKLEDLPKQDDFIAVFSHYLPPYLSPTFINIDHIPLMRTSGKVDKEYLRQYYYSKHHCEISEITKVLQPGWVNDPVKHMTENNNSTSDQSFGKNSRDFKLSRGRERARKVLAEVLGIRGPNGDVIPGRPKDDEDFYLLGGDSLLTVLTTEQLRQLGFNVNLDVFTKTGKIGSILTSLQNTESDFLKTQEPFTSDSWTVKEISMNKVLKKSHTCNLINRIPLMEDECYLSPTICPQGSYEIFIEQWNDGNFSVTERHEIVDVLVNAFIEKDRLSHALKLDRTDLTEAIEVFLNAHKSNPGIVLTARYYYENPYEHTFVKNKLVGVIISLPAKHVPSLHLTPKLALVQRFFDECSNKDQFQDISMDNLLATQMVAITSQSPYSKSKYLQYMLSNWKKISLKLLTRLERDLLRIAAKQGYSGVITFNTNEVTEEVCSQLGYKVIQTTMLKSFMNKENLLLLPQYERIRCSYMIKELNPSS

6.3.2.-

COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258};

amino acid adenylylation by nonribosomal peptide synthase [GO:0043042]; female genitalia development [GO:0030540]

beta-alanyl amine synthase activity [GO:0003833]

PF00501;PF00550;

3.30.300.30;3.40.630.30;3.40.50.12780;

NRP synthetase family

CATALYTIC ACTIVITY: Reaction=ATP + beta-alanine + tryptamine = AMP + beta-alanyl-tryptamine + diphosphate + H(+); Xref=Rhea:RHEA:73335, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57887, ChEBI:CHEBI:57966, ChEBI:CHEBI:192794, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:35385687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73336; Evidence={ECO:0000269|PubMed:35385687}; CATALYTIC ACTIVITY: Reaction=ATP + beta-alanine + H(+) = beta-alanyl-5'-AMP + diphosphate; Xref=Rhea:RHEA:73339, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:192795; Evidence={ECO:0000269|PubMed:35385687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73340; Evidence={ECO:0000269|PubMed:35385687}; CATALYTIC ACTIVITY: Reaction=beta-alanyl-5'-AMP + holo-[peptidyl-carrier protein] = AMP + beta-alanyl-[peptidyl-carrier protein] + H(+); Xref=Rhea:RHEA:73343, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:18218, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:192795, ChEBI:CHEBI:192796, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:35385687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73344; Evidence={ECO:0000269|PubMed:35385687}; CATALYTIC ACTIVITY: Reaction=beta-alanyl-[peptidyl-carrier protein] + tryptamine = beta-alanyl-tryptamine + H(+) + holo-[peptidyl-carrier protein]; Xref=Rhea:RHEA:73347, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:18218, ChEBI:CHEBI:15378, ChEBI:CHEBI:57887, ChEBI:CHEBI:64479, ChEBI:CHEBI:192794, ChEBI:CHEBI:192796; Evidence={ECO:0000269|PubMed:35385687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73348; Evidence={ECO:0000269|PubMed:35385687};

FUNCTION: Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT) (PubMed:35385687). Beta-alanyl-tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing (PubMed:35385687). {ECO:0000269|PubMed:35385687}.

Schistosoma mansoni (Blood fluke)

A0A3Q0NBH7

PGDA_LISMG

MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFVTIDELYGEKLQIGKQYFDKTDSRMVK

3.5.1.104

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8DP63};

autolysis [GO:0001896]; carbohydrate metabolic process [GO:0005975]; cell wall modification [GO:0042545]; evasion of host innate immune recognition [GO:0141043]; negative regulation of lysozyme activity [GO:1903591]

extracellular region [GO:0005576]; Gram-positive-bacterium-type cell wall [GO:0009275]; plasma membrane [GO:0005886]

chitin deacetylase activity [GO:0004099]; lysozyme inhibitor activity [GO:0060241]; N-acetylglucosamine deacetylase activity [GO:0050119]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]

PF01522;

3.20.20.370;

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8Y9V5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:Q8Y9V5}. Secreted, cell wall {ECO:0000305|PubMed:19809250}.

CATALYTIC ACTIVITY: Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate.; EC=3.5.1.104; Evidence={ECO:0000269|PubMed:19809250};

FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PG). Deacetylates also N-acetylated PG. Does not deacetylate N-acetylmuramic acid (PubMed:19809250). Confers host lysozyme resistance. Critical for virulence and escape from innate immune response of the host. Required for intracellular survival of bacteria in macrophages of the host. Required for successful host colonization (By similarity). Controls the production of inflammatory mediators in the bone marrow derived macrophages (BMMs) of the infected mouse (By similarity). Suppresses Toll-like receptor 2 (TLR2)-dependent secretion of interleukin 6 (IL-6) and interferon-beta (IFN-beta) in the macrophages of the infected mouse. May decrease accessibility of pattern recognition receptors (PRRs) such as nucleotide-binding oligomerization domain protein (NOD) 1 of the host to the bacterial cell wall components (By similarity). Protects cells from autolysis induced by lysozyme or by other autolysis-inducing agents (PubMed:19809250). {ECO:0000250|UniProtKB:A0A0H3GDH9, ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000269|PubMed:19809250}.

Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness)

A0A3Q2TTB3

PRIPO_CHICK

MKRKWEERVKKVEELASYYERNPLPTVYKPRLSKPLQPSRVWKIFCRQADAFRFVKTCKEDVHVFALERNTQNGQRFYLVTTYQELWYYYTKGYKTSLMHCYEVIPEKDACKLYFDLEFYKAANPGADGKDMVAKLIELVSQKLKELYDVNCSARDVLNLDSSTDEKFSRHLIFLPCKTVFKDNIHVGNFVRTILQPAIRLVGSNVAAPIAEGGAGYTSQCSAPTVELDGPLTNLTAVEDASKGWPAIADQRKETETSHHGENSEFSFLIVNNKEGDKQLFVDLGVYTRNRNFRMYKSSKAGKNVILTIAEDNKFVPNCEENVSLEEAYFLSSLVCNVRFEDGTKILSSNFVEEEIKMSAFLRSKTTRSTREPMEGYQESPYPEIDCFVRSLINKDGVQGGIRQWNYFSGEEILVYDISGYRWCENIGRAHRSNNIMILVDLKKEVWYQKCHDPVCREKNFKSQSLPLPSRICLSSLFIEEEDHMVTDERENTEVTSHSNPADLSESSAYLAINTSQDTQWDNASDDAYLVETAEDVELAEAADYSLGYDTEEIPDEVLLEMSWKQDTCSKDDS

2.7.7.102; 2.7.7.7

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96LW4}; Note=Can act both with Mn(2+) and Mg(2+) as cofactor in vitro, but Mn(2+) is the preferred cofactor in vivo. {ECO:0000250|UniProtKB:Q96LW4};

error-prone translesion synthesis [GO:0042276]; mitochondrial DNA repair [GO:0043504]; mitochondrial DNA replication [GO:0006264]; R-loop processing [GO:0062176]; replication fork processing [GO:0031297]; response to UV [GO:0009411]; translesion synthesis [GO:0019985]

DNA-directed RNA polymerase complex [GO:0000428]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]; replication fork [GO:0005657]

chromatin binding [GO:0003682]; DNA primase activity [GO:0003896]; DNA-directed DNA polymerase activity [GO:0003887]; manganese ion binding [GO:0030145]; zinc ion binding [GO:0008270]

PF03121;

Eukaryotic-type primase small subunit family

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LW4}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q96LW4}. Chromosome {ECO:0000250|UniProtKB:Q96LW4}.

CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.102; Evidence={ECO:0000269|PubMed:30478192}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:Q96LW4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22509; Evidence={ECO:0000250|UniProtKB:Q96LW4};

FUNCTION: DNA primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them (PubMed:26626482, PubMed:30478192). Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions (PubMed:26694751, PubMed:27230014). Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (By similarity). Provides different translesion synthesis alternatives when DNA replication is stalled: able to synthesize DNA primers downstream of lesions, such as UV lesions, R-loops and G-quadruplexes, to allow DNA replication to continue (PubMed:26694751, PubMed:27230014, PubMed:26626482). Can also realign primers ahead of 'unreadable lesions' such as abasic sites and 6-4 photoproduct (6-4 pyrimidine-pyrimidinone), thereby skipping the lesion. Repriming avoids fork degradation while leading to accumulation of internal ssDNA gaps behind the forks (By similarity). Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase (By similarity). Also required for reinitiating stalled forks after ultraviolet (UV) damage during nuclear DNA replication (By similarity). Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides (By similarity). In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (By similarity). {ECO:0000250|UniProtKB:Q96LW4, ECO:0000269|PubMed:26626482, ECO:0000269|PubMed:26694751, ECO:0000269|PubMed:27230014, ECO:0000269|PubMed:30478192}.

Gallus gallus (Chicken)

A0A3Q7FGP1

IF4E2_SOLLC

MADELNKAALEEYKSSSVEDRGEEGEIVGESDDTASSLGKQITMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTAEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCANGGKWTMNFSRGKSDTCWLYTLLALIGEQFDYGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDTIGFIFHDDAKKLDRAAKNRYSV

defense response to virus [GO:0051607]; translational initiation [GO:0006413]

cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]

RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]

PF01652;

3.30.760.10;

Eukaryotic initiation factor 4E family

PTM: According to the redox status, the Cys-119-Cys-157 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.

FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (PubMed:22242134, PubMed:26850324, PubMed:27655175). {ECO:0000250|UniProtKB:P29557, ECO:0000250|UniProtKB:Q4VQY3, ECO:0000269|PubMed:22242134, ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection (e.g. potato virus Y (PVY) and tobacco etch virus (TEV)) by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:22242134, ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175}.

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

A0A3Q7GYG2

MOMT2_SOLLC

MASNNNICAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYASKERTEKEWEKLFLEAGFSGYKIITSLGLRSLIEIYP

2.1.1.-; 2.1.1.155; 2.1.1.82

aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259]

O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF08100;PF00891;

3.40.50.150;1.10.10.10;

Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family

CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = H(+) + rhamnetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73115, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73116; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=kaempferol + S-adenosyl-L-methionine = H(+) + kaempferide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15105, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58573, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789; EC=2.1.1.155; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15106; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=myricetin + S-adenosyl-L-methionine = 7-O-methylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74719, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58395, ChEBI:CHEBI:59789, ChEBI:CHEBI:194065; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74720; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=kaempferide + S-adenosyl-L-methionine = 7,4'-O-dimethylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74775, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789, ChEBI:CHEBI:194067; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74776; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=isorhamnetin + S-adenosyl-L-methionine = 3',4'-O-dimethylquercetin + 2 H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74723, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:144055, ChEBI:CHEBI:194064; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74724; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,7-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16181, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57928, ChEBI:CHEBI:59789, ChEBI:CHEBI:77710; EC=2.1.1.82; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16182; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=rhamnetin + S-adenosyl-L-methionine = 7,4'-O-dimethylquercetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74731, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706, ChEBI:CHEBI:194068; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74732; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + syringetin = 7,3',5'-O-trimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58412, ChEBI:CHEBI:59789, ChEBI:CHEBI:194069; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74736; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=3',4',5'-O-trimethylmyricetin + S-adenosyl-L-methionine = 7,3',4',5'-O-tetramethylmyricetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74739, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194070, ChEBI:CHEBI:194071; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74740; Evidence={ECO:0000250|UniProtKB:F2YTN5};

PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:22711283}.

FUNCTION: Flavonoid 7/4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects (PubMed:22711283). Catalyzes S-adenosylmethionine-dependent regioselective 7/4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates (PubMed:22711283). {ECO:0000269|PubMed:22711283}.

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

A0A3Q7HJG4

CURE1_SOLLC

MGNIKFLLLVFFLIVVVVNGCWEEERNALLELQTNIMSSNGELLVDWAGYNAAHFVDCCFWDRVKCSLETGRVIKLDLEADFGTGDGWLFNASLFLPFKSLQVLLLSSQNIIGWTKNEGFSKLRQLPNLKEVDLQYNPIDPKVLLSSLCWISSLEVLKLGVDVDTSFSIPMTYNTNMMSKKCGGLSNLRELWFEGYEINDINILSALGELRNLEKLILDDNNFNSTIFSSLKIFPSLKHLNLAANEINGNVEMNDIIDLSNLEYLDLSDNNIHSFATTKGNKKMTSLRSLLLGSSYSNSSRVIRSLKSFSSLKSLSYKNSNLTSPSIIYALRNLSTVEYLYFKGSSLNDNFLPNIGQMTSLKVLNMPSGGNNGTLPNQGWCELKYIEELDFLNNNFVGTLPLCLGNLTSLRWLSLAGNNLHGNIASHSIWRRLTSLEYLDIADNQFDVPLSFSQFSDHKKLIYLNVGYNTIITDTEYQNWIPNFQLEFFAIQRCIALQKLPSFLHYQYDLRILAIEGNQLQGKFPTWLLENNTRLAAIYGRDNAFSGPLKLPSSVHLHLEAVDVSNNKLNGHIPQNMSLAFPKLLSLNMSHNHLEGPIPSKISGIYLTILDLSVNFLSGEVPGDLAVVDSPQLFYLRLSNNKLKGKIFSEEFRPHVLSFLYLNDNNFEGALPSNVFLSSLITLDASRNNFSGEIPGCTRDNRRLLQLDLSKNHLQGLIPVEICNLKIINVLAISENKISGSIPSCVSSLPLKHIHLQKNQLGGELGHVIFNFSSLITLDLRYNNFAGNIPYTIGSLSNLNYLLLSNNKLEGDIPTQICMLNNLSIVDLSFNKLYGPLPPCLGYLTQTKKDAEISWTYFAENYRGSWLNFVIWMRSKRHYHDSHGLLSDLFLMDVETQVQFSTKKNSYTYKGNILKYMSGIDLSSNRLTGEIPVELGNMSNIHALNLSHNHLNGRIPNTFSNLQEIESLDLSCNRLNGSIPVGLLELNSLAVFSVAYNNLSGAVPDFKAQFGTFNKSSYEGNPFLCGYPLDNKCGMSPKLSNTSNINGDEESSELEDIQCFYIGFVVSFGAILLGLAAALCLNRHWRRAWFRMIEALMFYCYYFVLDNIVTPIKSRWYKNVG

activation of innate immune response [GO:0002218]; cell surface pattern recognition receptor signaling pathway [GO:0002752]; defense response to parasitic plant [GO:0002242]; immune response-regulating cell surface receptor signaling pathway [GO:0002768]; pathogen-associated molecular pattern receptor signaling pathway [GO:0140426]; plant-type hypersensitive response [GO:0009626]

cell surface [GO:0009986]; plasma membrane [GO:0005886]

pattern recognition receptor activity [GO:0038187]

PF00560;PF13855;

3.80.10.10;

RLP family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27471302}; Single-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:27471302}. Cell surface {ECO:0000305|PubMed:27471302}.

FUNCTION: Involved in plant defense. Contributes to resistance against parasitic plant C.reflexa (PubMed:27471302, PubMed:33082345). Acts as a receptor for the 11 kDa glycine-rich protein (GRP) of C.reflexa inducing immune responses such as emission of stress-related phytohormone ethylene, reactive oxygen species (ROS) release, and hypersensitive cell death (PubMed:27471302, PubMed:33082345). Recognizes a specific pathogen-associated molecular pattern (PAMP), a cysteine-rich peptide 21 (crip21), from GRP located on the cell wall of C.reflexa (PubMed:33082345). {ECO:0000269|PubMed:27471302, ECO:0000269|PubMed:33082345}.

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

A0A3Q7HRZ6

MYC2_SOLLC

MTEYSLPTMNLWNNSTSDDNVSMMEAFMSSDLSFWATNNSTSAAVVGVNSNLPHASSNTPSVFAPSSSTSASTLSAAATVDASKSMPFFNQETLQQRLQALIDGARETWTYAIFWQSSVVDFSSPSVLGWGDGYYKGEEDKAKRKLSVSSPAYIAEQEHRKKVLRELNSLISGAPPGTDDAVDEEVTDTEWFFLISMTQSFVNGSGLPGQALYSSSPIWVAGTEKLAASHCERVRQAQGFGLQTIVCIPSANGVVELGSTELIVQSSDLMNKVRVLFNFSNDLGSGSWAVQPESDPSALWLTDPSSSGMEVRESLNTVQTNSVPSSNSNKQIAYGNENNHPSGNGQSCYNQQQQKNPPQQQTQGFFTRELNFSEFGFDGSSNRNGNSSVSCKPESGEILNFGDSTKKSASSANVNLFTGQSQFGAGEENNNKNKKRSATSRGSNEEGMLSFVSGTVLPSSGMKSGGGGGEDSEHSDLEASVVKEADSSRVVEPEKRPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNVSKMDKASLLGDAISYINELKSKLQNTESDKEDLKSQIEDLKKESRRPGPPPPPNQDLKMSSHTGGKIVDVDIDVKIIGWDAMIRIQCNKKNHPAARLMAALMELDLDVHHASVSVVNDLMIQQATVKMGSRHYTEEQLRVALTSKIAETH

defense response [GO:0006952]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]

nucleus [GO:0005634]

DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]

PF14215;PF00010;

4.10.280.10;

SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.

FUNCTION: Transcriptional activator that binds to the G-box motif (5'-AACGTG-3') found in the promoter of the jasmonate-induced gene LAPA1 (PubMed:15231736). Acts as a negative regulator of blue light-mediated photomorphogenesis and positively regulates root growth (PubMed:24483714). Promotes growth in response to the phytohormones abscisic acid (ABA) and jasmonate (JA) (PubMed:24483714). Binds to the G-box motif (5'-CACGTG-3') of the RBCS-3A gene promoter (PubMed:24483714). Acts downstream of the jasmonate (JA) receptor to orchestrate JA-mediated activation of plant responses (PubMed:28733419). Positively regulates both wound-responsive and pathogen-responsive genes through MYC2-targeted transcription factors (MTFs) involved in early response to JA (PubMed:28733419). With JA2L forms a transcription module that regulates wounding-responsive genes (PubMed:28733419). With ERF.C3 forms a transcription module that regulates pathogen-responsive genes (PubMed:28733419). Plays a critical role in orchestrating JA-mediated defense gene expression during Botrytis cinerea infection (PubMed:28733419). Negatively regulates defense responses to root-knot nematodes, potentially by mediating crosstalk among the hormones strigolactones, abscisic acid (ABA) and jasmonate (JA) (PubMed:30576511). Regulates the termination of JA-mediated defense responses by specifically binding the G-box (5'-CACATG-3') motifs in the promoters of MTB1, MTB2 and MTB3, which are transcription factors that negatively regulates JA signaling (PubMed:30610166). May be involved in JA-induced chilling tolerance, possibly by ameliorating the antioxidant enzyme system of fruit and increasing proline and lycopene levels (PubMed:29528226). {ECO:0000269|PubMed:15231736, ECO:0000269|PubMed:24483714, ECO:0000269|PubMed:28733419, ECO:0000269|PubMed:29528226, ECO:0000269|PubMed:30576511, ECO:0000269|PubMed:30610166}.

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

A0A3Q7HYF0

MOMT3_SOLLC

MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLRAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGNVHTSYNLTPLSQSLILDKDGTSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRFNGVFNKAMQNVTCIDMKRVLECYNGFEGVKEIIDVGGGLGISLASIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDECCVKILKNCWRALPKDGKVVVIEQMQPEYPEINLISKNSFSVDMLMMTMLDGGKERTKQQFEDLAKQAGFTVFKIVARAYYCWVIELYK

2.1.1.-; 2.1.1.76

aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259]

3',4',5'-trimethylmyricetin 3-O-methyltransferase activity [GO:0102440]; kaempferol 3-O-methyltransferase activity [GO:0102449]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; quercetin 3-O-methyltransferase activity [GO:0030755]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF08100;PF00891;

3.40.50.150;1.10.10.10;

Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family

CATALYTIC ACTIVITY: Reaction=3',4',5'-O-trimethylmyricetin + S-adenosyl-L-methionine = 3,3',4',5'-O-tetramethylmyricetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74771, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194070, ChEBI:CHEBI:194076; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74772; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=kaempferol + S-adenosyl-L-methionine = 3-O-methylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74743, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58573, ChEBI:CHEBI:59789, ChEBI:CHEBI:194073; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74744; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = 3',4',5,7-tetrahydroxy-3-methoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17673, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:57928, ChEBI:CHEBI:59789; EC=2.1.1.76; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17674; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=myricetin + S-adenosyl-L-methionine = 3-O-methylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74747, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58395, ChEBI:CHEBI:59789, ChEBI:CHEBI:194072; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74748; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=kaempferide + S-adenosyl-L-methionine = 3,4'-O-dimethylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74755, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789, ChEBI:CHEBI:194074; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74756; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=isorhamnetin + S-adenosyl-L-methionine = 3,3'-O-dimethylquercetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74759, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:144055, ChEBI:CHEBI:194063; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74760; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=rhamnetin + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,7-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77710, ChEBI:CHEBI:192706; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74764; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=laricitrin + S-adenosyl-L-methionine = 3,3'-O-dimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74779, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:60006, ChEBI:CHEBI:194066; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74780; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + syringetin = 3,3',5'-O-trimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58412, ChEBI:CHEBI:59789, ChEBI:CHEBI:194075; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74768; Evidence={ECO:0000269|PubMed:22711283};

PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:25128240}.

FUNCTION: Flavonoid 3-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects (PubMed:25128240). Catalyzes S-adenosylmethionine-dependent regioselective 3-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates (PubMed:22711283, PubMed:25128240). Active with myricetin, quercetin, kaempferol, 4'-methyl kaempferol (kaempferide), 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin), 3',4',5'-trimethyl myricetin, 3'-methyl myricetin (laricitrin) and 3',5'-dimethyl myricetin (syringetin), thus producing 3-methyl myricetin, 3-methyl quercetin, 3-methyl kaempferol, 4',3-methyl kaempferol, 3',3-methyl quercetin, 7,3-dimethyl quercetin, 3',4',5',3-tetramethyl myricetin, 3',3-dimethyl myricetin and 3',5',3-dimethyl myricetin, respectively (PubMed:22711283). Inactive with flavonol substrates methylated at the 3-hydroxyl position such as 3-O-methyl quercetin (PubMed:22711283). {ECO:0000269|PubMed:22711283, ECO:0000269|PubMed:25128240}.

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

A0A3Q7I7R4

IFI4E_SOLLC

MATEAPVEATEIPSVAAAETVEKQPHKLERKWTFWFDNQSKPKQGVAWGSSLRKAYTFETVEEFWSLYDQIFKPSKVTVNADFHLFKAGIEPKWEDPECANGGKWTATSSRKANLETMWLETLMALVGEQFDESEDICGVVASVRRSQDKLSLWTKTATNEAAQMGIGRKWKEIIDAEKISYSFHDDSKRERSAKSRYTV

response to virus [GO:0009615]; translational initiation [GO:0006413]

eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]

RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743]

PF01652;

3.30.760.10;

Eukaryotic initiation factor 4E family

PTM: According to the redox status, the Cys-99-Cys-138 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}. Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.

FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (Ref.1). {ECO:0000250|UniProtKB:O04663, ECO:0000250|UniProtKB:P29557, ECO:0000269|Ref.1}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|Ref.1}.

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

A0A3Q8GL18

NEPS1_NEPRA

MASTANPMQVMKKKLEGKVVIVTGGASGIGQTAARVFAQHGARAVVIADIQSEVGKSVAKSIGDPCCYVQCDVSDEEEVKSMIEWTASAYGGLDMMFSNVGIMSKSAQTVMDLDLLEFDKVMRVNARGMAACLKHAARKMVELGTRGTIICTTTPLSSRGGQSMTDYAMSKHAVMGLVRSASIQLGAHGIRVNCVTPSVVLTPLAQRMGLATPDDFHTHFGNFTSLKGVYLTPEQVAEAVVYLASDDAAFITGHDLVLDGGLLCLPFFAPS

1.1.1.419; 5.5.1.34

isoprenoid metabolic process [GO:0006720]

isomerase activity [GO:0016853]; oxidoreductase activity [GO:0016491]

PF13561;

3.40.50.720;

Short-chain dehydrogenases/reductases (SDR) family

CATALYTIC ACTIVITY: Reaction=(S)-8-oxocitronellyl enol = cis-trans-nepetalactol; Xref=Rhea:RHEA:61416, ChEBI:CHEBI:71494, ChEBI:CHEBI:144481; EC=5.5.1.34; Evidence={ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61417; Evidence={ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302}; CATALYTIC ACTIVITY: Reaction=cis-cis-nepetalactol + NAD(+) = cis-cis-nepetalactone + H(+) + NADH; Xref=Rhea:RHEA:61424, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144482, ChEBI:CHEBI:144485; EC=1.1.1.419; Evidence={ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61425; Evidence={ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302}; CATALYTIC ACTIVITY: Reaction=cis-trans-nepetalactol + NAD(+) = cis-trans-nepetalactone + H(+) + NADH; Xref=Rhea:RHEA:61428, ChEBI:CHEBI:7518, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:71494; EC=1.1.1.419; Evidence={ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61429; Evidence={ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for cis-trans-nepetalactol (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:30531909}; KM=4.9 uM for cis-cis-nepetalactol (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:30531909}; KM=3.5 uM for NAD(+) (in the presence of cis-trans-nepetalactol at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:30531909}; Note=kcat is 0.148 sec(-1) with cis-trans-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius). kcat is 0.32 sec(-1) with cis-cis-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius). kcat is 0.173 sec(-1) with NAD(+) as substrate (in the presence of cis-trans-nepetalactol at pH 8.0 and 25 degrees Celsius).;

FUNCTION: Bifunctional enzyme that possesses cyclase and dehydrogenase activities (PubMed:30531909, PubMed:30664302). Functions as a non-oxidoreductive cyclase to promote the formation of cis-trans-nepetalactol (PubMed:30531909, PubMed:30664302). Functions as dehydrogenase to oxidize cis-cis-nepetalactol and cis-trans-nepetalactol into nepetalactones, metabolites that are both insect-repellent and have euphoric effect in cats (PubMed:30531909, PubMed:30664302). Binds NAD(+) as classical short-chain dehydrogenase/reductase (SDR), but does not utilize it for its redox-neutral cyclase activity (By similarity). {ECO:0000250|UniProtKB:A0A3Q8GLE8, ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302}.

Nepeta racemosa (Catmint) (Raceme catnip)

A0A3S5YBC7

EGCSE_RHOH1

MRKTVVAFAAAIAACSAVLSSTTTSAAPPATPITTLQADGTHLVDGYGRTVLLHGVNNVDKDAPYLPAGETLTPQDIDILVRHGFNTVRLGTSFDALMPQRGQIDEAYLDRLTGVVDALTARGMHVLLDNHQDGLSKAWGGNGFPEWAIESRPREWEPNPGFPLYYLMPSLNAGWDEVWGNTHGALDHLGTALGALAERVEGKPGVMGIELLNEPWPGSRFLSCFPNGCPDFDRTYQAAMQKLTDAVRAQNPTIPVYWEPNVTWNQMMPSNLFAPPVTPALTTADVVFAPHDYCIPSQLAIYLGLPQALRGLCVPQQDLTWSNIDAITERANVPTVITEFGDGDPTVLKNTLARADERFIGWQYWHFGAGNATDPFLGEVGRQLVRTYPQATAGEPGRMIFDADNGDFAYRFTPRAATRPTEIFVSDLHYPDGYAVQVDGGQVTSAPGARIVTVVADGSGPVTVKINRPGSAGAEVPDGPIETSSSGSSGSS

3.2.1.123

galactosylceramide catabolic process [GO:0006683]

extracellular region [GO:0005576]; membrane [GO:0016020]

endoglycosylceramidase activity [GO:0047876]

PF00150;PF18564;

3.20.20.80;2.60.40.1180;

Glycosyl hydrolase 5 (cellulase A) family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28179425}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.

CATALYTIC ACTIVITY: Reaction=an oligoglycosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + an oligoglycosyl-(1->4)-D-glucose; Xref=Rhea:RHEA:22288, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273, ChEBI:CHEBI:136875, ChEBI:CHEBI:156536; EC=3.2.1.123; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22289; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM3 + H2O = an N-acyl-sphingoid base + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-D-glucose; Xref=Rhea:RHEA:65540, ChEBI:CHEBI:15377, ChEBI:CHEBI:79210, ChEBI:CHEBI:83273, ChEBI:CHEBI:156068; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65541; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + H2O = an N-acyl-sphingoid base + beta-D-Gal-(1->3)-beta-D-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-D-Gal-(1->4)-D-Glc; Xref=Rhea:RHEA:65544, ChEBI:CHEBI:15377, ChEBI:CHEBI:82639, ChEBI:CHEBI:83273, ChEBI:CHEBI:156537; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65545; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a ganglioside Fuc-GM1 + H2O = alpha-Fuc-(1->2)-beta-Gal-(1->3)-beta-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-Gal-(1->4)-Glc + an N-acyl-sphingoid base; Xref=Rhea:RHEA:65548, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273, ChEBI:CHEBI:90189, ChEBI:CHEBI:156538; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65549; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + lactose; Xref=Rhea:RHEA:65552, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:79208, ChEBI:CHEBI:83273; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65553; Evidence={ECO:0000269|PubMed:28179425};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for monosialotetrahexosylganglioside (GM1) {ECO:0000269|PubMed:28179425}; Note=kcat is 10.5 sec(-1) with monosialotetrahexosylganglioside as substrate. {ECO:0000269|PubMed:28179425};

FUNCTION: Hydrolyzes glycosphingolipids; exhibits broad substrate specificity including monosialodihexosylganglioside (GM3), monosialotetrahexosylganglioside (GM1), fucosyl-GM1, lactosylceramide, globotriosylceramide, globotetraosylceramide, ganglioside GD1a, and ganglioside GD1b (PubMed:28179425). No activity towards glucosylceramide and galactosylceramide (PubMed:28179425). {ECO:0000269|PubMed:28179425}.

Rhodococcus hoagii (strain 103S) (Rhodococcus equi)

A0A3S7WQS5

SPCS_LEIDO

MDDRSLKLAEDFVSARYIEAGRESLRATARIMRSILAQRCCPDEGLTDAAIELILRQLSLMDTNNLAHHVGGGEREGRVVSALVRMRHFHLTHGIGRSGDLFSEQPKAAGSSLLYKITNVLMLDLIRQAGAPSTAAAVVVPMATGMTLALVLRCVAKTHMKELMKEAEAVQLQRTVTKDSTSATSAAPVQEPPMSEADRDRHDRTSLPVPATPRYVIWPRIDQKTALKCIDAAGLVPVPVQLRPAVPLARSAAPCVSTNRDSLDRGQDSIGSPSTPTSSSSLFLECHVDDVAAAVNAVGGPSQVVCVLSTTSCFAPRLPDNTVAIAQYCKKAGIPYVVNNAYGVQSRRIMTRLDAAQRLGRVDFVVQSGDKNFLVPVGGSIICSGDKERCKAVAALYAGRASMSPIVDLFITALSLGRRGMQTLWSDRYKCRARLIRQLRVFARERREVLLVDDSDDDKADEDTVGGSQRTSNAVVPRNDISVAVTMRAYGLPAAEASSSGAQLGSEQAGRVTNWAAARALGAQLFRSAVTGPRVITPAPSTPTTIAGCTFRNYGMHQDREPPCPLLVIACGIGMSESEVDALMARLRDLWPVPA

2.9.1.2

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|PIRNR:PIRNR017689, ECO:0000255|PIRSR:PIRSR017689-50};

conversion of seryl-tRNAsec to selenocys-tRNAsec [GO:0001717]; selenocysteine incorporation [GO:0001514]

cytoplasm [GO:0005737]

O-phosphoseryl-tRNA(Sec) selenium transferase activity [GO:0098621]; selenotransferase activity [GO:0016785]; tRNA binding [GO:0000049]

PF05889;

3.40.640.10;

SepSecS family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + 2 phosphate; Xref=Rhea:RHEA:25041, Rhea:RHEA-COMP:9743, Rhea:RHEA-COMP:9947, ChEBI:CHEBI:15377, ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78551, ChEBI:CHEBI:78573; EC=2.9.1.2; Evidence={ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914};

PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2. {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.

FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.

Leishmania donovani

A0A411EZW9

PA21_AGKPL

MRTLWIMAVLLLGVEGDLMQFETLIMKIAKRSGMFWYSAYGCYCGWGGQGRPQDATDRCCFVHDCCYGKVTGCDPKLDSYTYSVENGDVVCGGNDPCKKEICECDRAAAICFRDNKVTYDNKYWRFPPQNCKEESEPC

3.1.1.4

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:28063838}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418};

arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]

extracellular region [GO:0005576]

calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]

PF00068;

1.20.90.10;

Phospholipase A2 family, Group II subfamily, D49 sub-subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28063838}.

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:28063838};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.75 mM for 4-nitro-3-(octanoyloxy) benzoic acid (NOBA) {ECO:0000269|PubMed:28063838}; Vmax=25.9 nM/min/mg enzyme {ECO:0000269|PubMed:28063838};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:28063838};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:28063838};

FUNCTION: Snake venom phospholipase A2 (PLA2) that triggers a high neuromuscular toxicity in chick biventer cervicis preparations, but not in mouse phrenic nerve-diaphragm (PND) preparations, suggesting a selective neurotoxin activity towards birds (PubMed:28063838). Does not induce myotoxic, coagulant, anticoagulant, edema, and antibacterial activities (PubMed:28063838). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:28063838). {ECO:0000269|PubMed:28063838}.

Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma)

A0A411KUP8

UCSA_ACRSP

MGPPSQATAANEPIAVIGSGCRFPGSASSPSKLWQLLSQPRDVLSEIPKSRFDPHGFYNKNGETGGHSNVLHSYVLDEDIRAWDADFFKVSASEAAAIDPQQRLLMETVYEALEAGGQQIHALRGSDTAVYVGLMGEEYSDIQGRELDMMPTYHATGTARSIVSNRISYFFDWHGASMTIDTACSSSLVAVHQCVQAIRSGYSRVAVAAGTNLCLGPEPYISESTFHMLSPRGRSHMWDASADGYGRGEGVAAVILKKLSDAIADGDHIECVIRETGVNQDGRTNGITVPSPDAQVALIQDTYRRAGLDLARPEDQPQFFEAHGTGTGAGDPLEAEAIYRAIGTRMAEGKRLYVGSIKTIIGHTEGTAGIAGLMKASLALQNRTIPPNMLFNTLNPKIEPFIKKLQIPQEPRDWPDVPVKRASVNSFGFGGTNAHAILERYEPDAYRQAEGGDAAFAGPYTFSAVSKTSLKQMLVNTLEFLDDNPAVKPRDLAYTLNSRRSTFTFRTSFAGRDVDALRKRITASIESPDWESQAVIRPAKQPLKILGIFTGQGAQWPGMGKQLLDSSPSAQARIQELELALATLQPGDRPCWSLKAELLAEGSKSRLSQAEFAQPLCTALQILLIDLLTAAGVQFSAVVGHSSGEIGAAYAAGVLSARDAIVVAYYRGVHTKLARGDGDQPGAMLAAGTTFEDAQDLVSLPELEGRIAIAACNSPSSVTLSGDADAIEAAVEMLSDEQKFARTLRVDKAYHSHHMRPCSEPYVNSLRRAGVAARDPRPETKWFSSVHAGRVLTSAAAEQLSDTYWALNMAQTVLFSAAVEEAVASEQYTAAIEVGPHGTLKGPAIDTIKAAGRPVPTYLSCLARNMDSLDTFSTAIGQLWATSPEGSLDLERYSITAFGPSQGANSPLKGFPSYPWDNKRRFWSESRRSRAFRLRPEPGHPLLGTLGADSTATDWSWHNVLRLTSLPWVNGHQLQGQTVWPAAGYVALAVEAANQLAKGHGGLSHIIELEDLDIGKAIAFENDKAGVELLFSLHVNNITVVNGQKVLEAGFSSRSSVGEASTEAALNASGHIRLTITDFESPEPSPALPVQDSARIAMTEVDQNLFYNELKVLGYNYTGPFRALHSLSRKLDHGRGRLARVSKSDMHDSERGLLVHPGYLDAAFQAMFLAYAYPGDGQIWSLHVPVSIGRIRIDATQSRANADSYLTFDSATNAVSQNNGQRGLAGDVNIFSADGQTGLVQVENIRLIPFAAASEANDAQVYYHNVWNTATPDGLLASEAFKAGEGVAQEGLGQAAGILAHVVGQITHINPHARLLQIGDESHEVAQRVLGKIGGAFSHYTLTSPSPDAVEEARDALHAKSRHLGFMELRPNEDFVAQGLREQSFEVAISALAAHTVQDAEAYIKKIHQVLRPGGYLLMLEPTLDSLRGSLSGKGKGTRGIPTAEWHSLLLRAGFTGVETSASDSDRSGPPFNVLVSRAANDHVNLLLEPSTIPSPEARAEHTLIVSGRSLASVRLAETMRRLLTPHTDRISVVSTVGDLTSLDLSVRPVVLYLADLDEPVFSHYTAEAHAGLQALWTTAQTVLWTTRGAQKHDPHSLQSIGFGRAMAVEHAHAKLNAQFFDFAPGARVDPHALLDDLLRLQILGKRSSNTQGDFVWTKEPEIQVDELGRRWIPRLVPHSDFNNGYNAARRSIVADADPSRHVVEVVSSRNSDGSLQRSLLRLTVPRTANVDSQEPLTKLRVLYTAETPFHPPSSAQLYASIGLDVTTSKPFVALSSTISSIIEVPTSSLIEYNHRLAEGPAHLHGITTSMLASLIIRTAKQDAATVLLEPSRELVSLLSKDAAAQDLKLAFVTASPATPKSESIHLGAYSTDSAIRRALSFNIASVLDFTNRGSWSERILKQLAPDVIVESADSFRAHGLAPAEIIEAFRSFIDAAPIAVQDHELVSADDFVASQRSSPSILDWAGSSTVSVSVQTPDSQPIFRGDRTYILFGLAGAGGLGLPLAEYMASLGARYIVLTSRNPEVDQDLVAEYASRGVHLRFMANDITNENQVSNLVSEIRASWPPIAGVANGANVLNDMQFKDMTHDDMVKVLRPKVEGSKTLDRLFFDDPLEFFIGFSSISIVFGRSGQSNYDAANIFMLGLASQRRARGLNASVIDIGPISGVGLMARDVSENVMGLLVNHGYRKMSGRDFLQLFLNGITCGRVESGEPEELITGLTVHPKNGDFKPTWTDNARFSHLFLNTDDSSGSSADGTGQMESIQDLLLRSSTKNDVARVLRHAILNKMQNVLSLSDESVLDSESLLQRDTSSLGLDSLLAVELRTWMLGELEVDLPVLKILSDTPIQGLVDFAVDNLPPALAPSVTPEGKDSITEEDLTAPKAKTDAPAAAPTPASATAPGSKSDGNVSSIARSADQSPSHKDTLPQPTAILTNATAGTKPVSPSLSVTGSTSSAAGDDETPTSSQAASLESSQVIDSRPVIDYKPVIEKTLPMSYGQSRFWVMNQIVQDPTAFNITCDIEISSEVDKAVLSRAVDIIGARHEALRTCFLNDENHEPIQAVMNTSTLRLEVVSDDQSQVDSYFEQVKKTVYDLSNGYLMRALLVSTSKTSHHLIVGYHHVNMDSTSFVVFMSDLLKIYAGQTLSPPKVQYPDFAQYQLQRLRNGQWASHINYWTREFAKLPDPLPLLSISPKASRPRPYLTNYQNIDAETRVSATVARQIQSTSRRLKVTPFHVYTTVLQIVLARLSGTDDVCIGMADANRTDIGAIDSIGNFLNLLPLRLTTDAKQSFETLVKVTKNKILHALSHSAVPFDVILEKVGVQRSPTHSPLFQAFIDYRHVTEKLPFGTGFLEGKRYAVSETPYDIMVEMIDTPTGEASLKILVQEALYTSEDAQTIMDCYINLLDAVTKDDRQAVGKPQIFNSSKVQKALELGQGETLNLQHATILPELDDIAAVQPTLTALQDSIGGSLSWSEMKAKSIAIGRNLDQLRLAPQSRVGVFQAPEVDWVCSMLGVWRSGHIYVPLETTQGIKRLSDVAQQARLDAILLHDPTVSLFSQLSLPNPLPTINVSAVPFAHLTDQRHFSTLKPDDQAMIVYTSGSTGVPKGITIAHRVVVNAVRSFLHRWPMTPQTVLQQTALSFDVSWWATVVGLATKGSVVVAGSDSRRDPRALTDLIVSKDITFTFAVPSESVSWLESGNADALRASSWAYHCSGGEPYSLNLIDKLKTLNKPDLTAINIYGPTETMIPNAHVVEYRTLTADDLPVPIGTTMPNYLARVVDLEGHPVPAGVPGELIFVGPGIASGYVDNAALTAERFPKDSLAGPEYVKNGWDVAHNSGDHGYLDGKTGEFVLQARIKGDTQVKLRGLRIDMQDVEANILTASNRQITDAIVHVRKPELNNPSADFLLAHVVLSREARLRYPTPADQSAFFRDIVRDLRVPDYMRPALVVALDSLPLTHHGKADRRAIANLPLDQIASQLQKEPVPLTNKGGLKETPVARPTRYQNDPIPRQVLSSSPFSSLDQVKDLWLDILGTAVNAHTLDPESDFFLVGGNSLLLIRIQGELRKRAGLDVPLTQLFQNSTLGQMASLLDGKDRAKQQGASGIDWVSEIKIQPNLARLRANRAPLPQDGLVMALTGATGFLGLELTRRLIDLPNVRTVHALSVRDSRKLSQLQSPKLVVHSGDLSRPSLGMDSGVLAQIFKTSHVVIHNGADVSFLKSYGSVRATNLESTKEIAKLALQHNNVRALHYVSTAGIATMLSHDLYEESIGSFPPSSSPEGYVLTKWAAELYLERVAAVTNLPVTIHRPTAIVGENAPHLDVMSNILHYSQKLNTVPSMTALEGTFQFVPVEDVANGLVGRVVAGHSSTLSAVEYQNHNGAIEDTVDVHGLAPYLSNKHGRSVTVTPDAEWIALASRAGMADEVVQYMGGVNMSDRKGEKWRFPRALNGSKP

2.3.1.-; 6.3.2.-

amide biosynthetic process [GO:0043604]; antibiotic biosynthetic process [GO:0017000]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolite biosynthetic process [GO:0044550]

fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08241;PF07993;PF21089;PF00550;PF14765;

3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150;

NRP synthetase family

PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:29373009}.

FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties (PubMed:29373009). These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment (PubMed:29373009). The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:29373009). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG (PubMed:29373009). Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction (PubMed:29373009). Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL (PubMed:29373009). This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition (PubMed:29373009). Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine (PubMed:29373009). The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable). {ECO:0000269|PubMed:29373009, ECO:0000305|PubMed:29373009}.

Acremonium sp

A0A411MR89

SZNF_STRC2

MSHVPPHVPFELSGAELRDAIVQYATNPIYHDNLDWLNHDNPYRRQLRPQVLPHLDYDKVPGRENILNYASLAVQRLLTSVYEADLVFFPKSGLKGKEEDFRAFYSPANRALGERIRPALERYAFGFLDDEVETSGTWTAQSLDAYLDSLDTAGGAEQSPVEKAILGSADRERAARMWLVQFAPDFLSEASPMMRNVLGYYGPAQSEWFKVVIDEYGYGVHDTKHSTLFERTLESVGLESDLHRYWQYYLNSSLLLNNYFHYLGKNHELFFRYVGALYYTESSLVDFCRRADHLLREVFGDTVDTTYFTEHIHIDQHHGRMAREKIIKPLVEAHGDGIIPEIVRGIEEYRVLLEIGDFDFSEQIAWMDAQPELKKLHDPVFEGLKQGKVDAPVAHLVEPRGELSNTHCHDGDELCHIVSGTMRFESGLGSSLTLQAGEGVVIKRNRLHGANIESDECVYEIHSVGDYRKCL

1.14.13.250

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082, ECO:0000269|PubMed:32511919, ECO:0000269|PubMed:33468680}; Note=Binds 3 Fe(2+) ions per subunit (PubMed:33468680). Two Fe(2+) bind the HO-like central domain and one Fe(2+) binds the C-terminal cupin domain (PubMed:33468680). {ECO:0000269|PubMed:33468680};

antibiotic biosynthetic process [GO:0017000]

metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]

PF07883;PF14518;

1.20.910.10;2.60.120.10;

CATALYTIC ACTIVITY: Reaction=H(+) + N(omega)-methyl-L-arginine + 2 NADH + 3 O2 = 3 H2O + N(delta)-hydroxy-N(omega)-methyl-N(omega)-nitroso-L-citrulline + 2 NAD(+); Xref=Rhea:RHEA:69052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:114953, ChEBI:CHEBI:143209; EC=1.14.13.250; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082, ECO:0000269|PubMed:32511919}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69053; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082, ECO:0000269|PubMed:32511919}; CATALYTIC ACTIVITY: Reaction=H(+) + N(omega)-methyl-L-arginine + NADH + O2 = H2O + N(delta)-hydroxy-N(omega)-methyl-L-arginine + NAD(+); Xref=Rhea:RHEA:69056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:114953, ChEBI:CHEBI:143207; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082, ECO:0000269|PubMed:32511919}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69057; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082, ECO:0000269|PubMed:32511919}; CATALYTIC ACTIVITY: Reaction=N(delta)-hydroxy-N(omega)-methyl-L-arginine + NADH + O2 = H2O + N(delta),N(omega')-dihydroxy-N(omega)-methyl-L-arginine + NAD(+); Xref=Rhea:RHEA:69060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:143207, ChEBI:CHEBI:143208; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:32511919}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69061; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:32511919}; CATALYTIC ACTIVITY: Reaction=N(delta),N(omega')-dihydroxy-N(omega)-methyl-L-arginine + O2 = H2O + N(delta)-hydroxy-N(omega)-methyl-N(omega)-nitroso-L-citrulline; Xref=Rhea:RHEA:69064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:143208, ChEBI:CHEBI:143209; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:34004115}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69065; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:34004115}; CATALYTIC ACTIVITY: Reaction=AH2 + 2 N(delta)-hydroxy-N(omega)-methyl-N(omega)-nitroso-L-citrulline = A + 2 N(delta)-hydroxy-N(omega)-methyl-L-citrulline + 2 nitric oxide; Xref=Rhea:RHEA:69068, ChEBI:CHEBI:13193, ChEBI:CHEBI:16480, ChEBI:CHEBI:17499, ChEBI:CHEBI:143209, ChEBI:CHEBI:143210; Evidence={ECO:0000269|PubMed:30728519}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69069; Evidence={ECO:0000269|PubMed:30728519};

PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable and active at pH 3-8, but loses its activity above pH 9 (PubMed:30763082). Shows reduced activity in phosphate buffer at pH 4-6 (PubMed:30763082). {ECO:0000269|PubMed:30763082};

FUNCTION: Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN) (PubMed:30728519, PubMed:30763082). Catalyzes a complex multi-step reaction: the overall reaction is an oxidative rearrangement of the guanidine group of N(omega)-methyl-L-arginine (L-NMA), generating an N-nitrosourea product (PubMed:30728519, PubMed:30763082, PubMed:32511919). SznF first hydroxylates L-NMA to form N(delta)-hydroxy-N(omega)-methyl-L-arginine (L-HMA), which is further hydroxylated to give N(delta)-hydroxy-N(omega)-hydroxy-N(omega)-methyl-L-arginine (L-DHMA) (PubMed:30728519, PubMed:32511919). Subsequently, an oxidative rearrangement converts this intermediate to N(delta)-hydroxy-N(omega)-methyl-N(omega)-nitroso-L-citrulline (PubMed:30728519, PubMed:34004115). This product is unstable, and degrades non-enzymically into nitric oxide and the denitrosated product N(delta)-hydroxy-N(omega)-methyl-L-citrulline (PubMed:30728519). {ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082, ECO:0000269|PubMed:32511919, ECO:0000269|PubMed:34004115}.

Streptomyces achromogenes subsp. streptozoticus

A0A445AGS0

IFI4E_ARAHY

MATETAGAVVESSSAATVPSPAPEAGSKHKLERKWTFWFDNQSKPKQGAAWGTSLREVYTFDTVEEFWCLYDQVFKPSKLPGNADFHLFKTGIEPKWEDPECAKGGKWTVTSNRKANLDNMWLETMMALIGEQFDDAEDICGVVASVRQRQDKLSLWTKTAANEAAQMGIGRKWKEIIDVTDKIIYNFHDDSRTRSSKSRYSV

defense response to virus [GO:0051607]

cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]

RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743]

PF01652;

3.30.760.10;

Eukaryotic initiation factor 4E family

PTM: According to the redox status, the Cys-102-Cys-141 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}. Note=(Microbial infection) Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with viral helper component proteinase (HC-Pro) in the cytoplasm. {ECO:0000269|PubMed:28344571}.

FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses such as peanut stripe virus (PStV) (PubMed:28344571). {ECO:0000250|UniProtKB:Q66WU1, ECO:0000269|PubMed:28344571}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:28344571}.

Arachis hypogaea (Peanut)

A0A452E9Y6

PERL_CAPHI

MLVCLHLQVFLASVALFEVAASDTIAQAASTTTISDAVSKVKTQVNKAFLDSRTRLKTALSSEAPTTRQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFINTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLLAKKSKLMNQNKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKILAKKLLDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHVTKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN

1.11.1.7

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304};

antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]; thiocyanate catabolic process [GO:0046265]

basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]

calcium ion binding [GO:0005509]; heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; peroxidase activity [GO:0004601]; thiocyanate peroxidase activity [GO:0036393]

PF03098;

1.10.640.10;

Peroxidase family, XPO subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}.

CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137; Evidence={ECO:0000250|UniProtKB:P80025}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O2 + thiocyanate = H2O + hypothiocyanous acid; Xref=Rhea:RHEA:69416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:18022, ChEBI:CHEBI:133907; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417; Evidence={ECO:0000250|UniProtKB:P80025}; CATALYTIC ACTIVITY: Reaction=H2O2 + iodide = H2O + hypoiodite; Xref=Rhea:RHEA:69420, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:29232; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69421; Evidence={ECO:0000250|UniProtKB:P80025};

FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism (PubMed:10894086). Shows antibacterial properties against several Gram-positive bacteria including some Staphylococcus species and Gram-negative bacteria including E.coli, P.aeruginosa and some Salmonella species (PubMed:10894086). Inhibits the growth of several fungi including A.niger, Trichoderma species, C.cassicola, P.meadii and C.salmonicolor (PubMed:10894086). Does not have anti-fungal activity towards C.albicans and Pythium species (PubMed:10894086). May protect the udder from infection and may promote growth in newborns (PubMed:10894086). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity). {ECO:0000250|UniProtKB:P22079, ECO:0000250|UniProtKB:P80025, ECO:0000250|UniProtKB:Q5SW46, ECO:0000269|PubMed:10894086}.

Capra hircus (Goat)

A0A455R4Z0

ASCI_ACREG

MPQLAGKLILAGLIPLGAWVLHGFASCNGLIQMFEDFGKQTVLSDGVTDYTGAFTGLEGLDRLLRTLLNFFWPVANGHDWALSLHAFMFAGQGVPLLVLNMLEGARPGNKSLVVSYVTVFGILYMVVGLAIMAPLYLFLHLLTSRTATAPSKAKVAVDPNTAKAVGFGVFVGYVLPTIFMSLPHPSLLSTDTKVLSVVFWQAVPLWASVCAYFASTALGQSATSRSSSNLPSALGAVYAASLIIATATHVATFAISANLSDTWSGIFTFLIPPNPFNTDMRISSFLEGATWFLQWDYTMMSLAYMVWAIGIRHGVEVPRSSHHFETLGKIALRSMAKLLVMGPIGAALSLVWERDQLLWQLDSESGEKGEKNRSRRMSRKWMFS

5.4.99.-

terpenoid biosynthetic process [GO:0016114]

membrane [GO:0016020]

isomerase activity [GO:0016853]

Membrane-bound ascI terpene cyclase family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=16-hydroxy-ilicicolin A epoxide = ascofuranol; Xref=Rhea:RHEA:63108, ChEBI:CHEBI:146158, ChEBI:CHEBI:146159; Evidence={ECO:0000269|PubMed:30952781, ECO:0000269|PubMed:35418536}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63109; Evidence={ECO:0000269|PubMed:30952781, ECO:0000269|PubMed:35418536};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50.4 uM for the product of ascH {ECO:0000269|PubMed:30952781}; Vmax=129 nmol/min/mg enzyme toward the product of ascH {ECO:0000269|PubMed:30952781};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:30952781, ECO:0000269|PubMed:35418536}.

FUNCTION: Epoxide hydrolase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis (PubMed:30952781, PubMed:35418536). The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781). On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781). Finally, ascofuranol is oxidized into ascofuranone by ascJ (PubMed:30952781, PubMed:35418536). {ECO:0000269|PubMed:30952781, ECO:0000269|PubMed:35418536}.

Acremonium egyptiacum (Oospora egyptiaca)

A0A481NV25

TYRDC_ENTFC

MKDMDIKAVFIGDKAENGPVYKMLLNKMVDEHLGWRENYIPSDMPAISEGDKLTPDYLATRDHMIEVLDEVSQRLRAGSIPWHSAGRYWGQMNAETLMPALLAYNYAMLWNPNNVALESSMATSQMEAEVGQDFASLFNMADGWGHIAADGSIANLEGLWYARCIKSIPLAVKEVLPEKVKNMSEWALLNLSVEEILEMTESFTDEEMDEVKAASSRSGKNIQKLGKWLVPQTKHYSWMKALDICGVGLDQMVAIPVQEDYRMDINALEKTIRELADQKIPILGVVAVVGTTEEGQVDSVDKIIQLREKLKDEGIYFYLHVDAAYGGYARSLFLNEAGEFVPYASLAEFFEEHHVFHHYVTIDKEVYEGFRAISEADSVTIDPHKMGYVPYAAGGIVIKHKNMRNIISYFAPYVFEKSVKAPDMLGAYILEGSKAGATAAAVWTAHRVLPLNVTGYGQLIGASIEAAQRFREFLEQLHFTVKGKTIEVYPLNHPDFNMVNWVFKVQDCTDLNAINELNEKMFDRSSYMDGDVYGERFITSHTTFTQEDYGDSPIRFIERMGLSKEEWQKEQQITLLRAAIMTPYLNDDRIFNFYTKEIAKAMEKKLNEIIK

4.1.1.-; 4.1.1.25

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:30659181};

L-dopa metabolic process [GO:1903184]

L-dopa decarboxylase activity [GO:0036468]; pyridoxal phosphate binding [GO:0030170]; tyrosine decarboxylase activity [GO:0004837]

PF00282;PF21391;

3.40.640.10;

Group II decarboxylase family, Tyrosine decarboxylase subfamily

CATALYTIC ACTIVITY: Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315, ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000269|PubMed:30659181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346; Evidence={ECO:0000305|PubMed:30659181}; CATALYTIC ACTIVITY: Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:30659181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12273; Evidence={ECO:0000305|PubMed:30659181};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for L-tyrosine (at pH 5.0) {ECO:0000269|PubMed:30659181}; KM=0.4 mM for L-dopa (at pH 5.0) {ECO:0000269|PubMed:30659181}; Vmax=4.4 umol/min/mg enzyme for the decarboxylation of L-tyrosine (at pH 5.0) {ECO:0000269|PubMed:30659181}; Vmax=3.4 umol/min/mg enzyme for the decarboxylation of L-dopa (at pH 5.0) {ECO:0000269|PubMed:30659181}; Note=kcat is 435.6 min(-1) for the decarboxylation of L-tyrosine. kcat is 342.4 min(-1) for the decarboxylation of L-dopa (at pH 5.0). {ECO:0000269|PubMed:30659181};

PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:30659181}.

FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:30659181). Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecium (By similarity). {ECO:0000250|UniProtKB:Q838D6, ECO:0000269|PubMed:30659181}.; FUNCTION: Also involved in drug metabolism, being able to catalyze decarboxylation of levodopa (L-dopa) to dopamine. In gut microbiota this enzyme is in fact exclusively responsible for the decarboxylation of levodopa, and thus reduces in situ levels of levodopa in the treatment of Parkinson's disease. It was shown that abundance of bacterial tyrosine decarboxylase in the proximal small intestine - the primary site of levodopa absorption - contributes to interindividual variation in drug efficacy and can explain the requirement for an increased dosage regimen of levodopa treatment in Parkinson's disease patients. {ECO:0000269|PubMed:30659181}.

Enterococcus faecium (Streptococcus faecium)

A0A481WNP4

TRAA_PENCR

MVLPQPEPIAIVGSGCRFPGSSSSPSSLWDLLEKPRDVSKEPTNERFELRGYYHPNGAHHGTMNVQRAYMLDEDVGTFDATFFNISPNEAESIDPQQRLLMEVVYEALEAGGHRLDILRGSDTAVYVGTMSVDYNDIMLRDINSIPTYFSTGTSRAILANRISYFFDWHGPSMTIDTACSSSMVALHQSVQALRSGESRVAIAGGTELLLGPEQFVGESKMNLLSPTGQSRMWDASANGYARGDGIAAIVLKKLSDAIADGDHIECLIRQTGINQDGKSTGLTVPSSAAQADLIRSTYTKGGLDIDNPRDWPQFFEAHGTGTKAGDPREASAISQCFGSQPIHGNPLYVGSIKTIIGHTEGTAGLAGVFKASLAIQHGIIPPNMLLHQLNDEVAQYCDNLRVPNAPTAWPKLPDGVPRRASVNSFGFGGTNGHAILEEYQPPTETRNTATTGRDENNASVFRIFPFSAASEESLTANLRAYATSLKTRTTVDLVDLAWTLQSRRSALPFKTSLTAECIEGLITKIDSTLEKAKANSGLKVGTRSAPTKPKVLGIFTGQGAQWATMAAGLIRTSETVRRKIEQLDGSLATLPEANRPTWRIADQLCADAEDSRLNEAALSQPLCTAIQVVLIDLLRSSGITFEAVVGHSSGEIAAAYAADYISAHDAIRIAYYRGVYAKHARGPKDQKGAMMAVGTTWEDAEELLNLPAFRGRVKIAAQNSAASLTLSGDVEALSHAKRVFDEEKKFTRLLVVDTAYHSHHMLLCSERYIHSLRTCGIQVNYNRNTSCTWYSSVKHGEPMHPEPSLGDLYWNDNMVNTVLFADAVKGAAKGSQLNLAIEVGPHPALKGPALQTLSDFEMSLPYTGVLKRKGNDLEAFSDALGFVWTHCGPGAVDFQTYEELIYPACKTPSLAIGLPAYQWDHKRVYWYQSRLAKKTQTRGEAFHELLGVPSPNNTDRDLRWSNFLKTNEIPWLNGHQLQGQTVFPAAGYVAMALEAGLKLAQGRSVKVLQIDDLTIDKAVTFDDGANFAVETLVALTGVTQGQSRTKKQTADFAVYSCANTGSSTELGVVSRGKVTVIYGTPSFSTLHSSPHNEKNMVDIQAEQFYSSLHELGYGYNGPFKTLSSTKRTLNQASARVETYGYGEDENTLIVHPTMLDVAFQASFLARMSPGDDQLWSLHVPTFIKCIRVNPELCASIPSSPTSLSLSAVLHESDSLSMLSSVDVFTEDGQETMIQVEGLSMKPFSPATADDDRSMFSTTVYGSMSPDLAMDVGNGRPPSEGLAFSQCNVALACVAQQIVHRYPHAKILEIGAGEGHATRAVLESIGSKLSYTFTDSSTEVIEKAAESFKDFKEKVLLKTFDPLGKPSSQGLDEHAYDLVIASNILASNSVSHTELENIRRLLKPGGYLLASGLTGDAPTRTLGGGTVEGNDARKHGPVNTAQWHGALRKAGFSGIDSITPQTSGMASPFSAIVTQAVDKRINFLRKPLSTPSFVRLDELVIVGNQSLKAAQLTEEIYDHLIQFCGKITVLDGLPTDDDDISSMATFINLADIHEPIFRDISAEQFEGLKCLFELASNILWVTEGARADEPYHNASIGFGRSIAYEMPHLSLQFLDLNDTGSTASRVISEAVLRLVALREWEETEHNFKDKTLWSREPELYVEKERLMVPRLLQVDDQNDRINSLRRVVTKMVDPDNSSVLISKAVDGSFVLREEVLRQSGQNFVQIKHSVLSAINVAPEAFLFLGAGFSQVTDEVVITLSDANASMSTPLAHVPAQWHTGGLSTLISAVARQLLARRLISMVVAHSHLLVHGLDENESFVSILKQHAGLKDIDIKFSAANPAANSEWIQVTPWTSSHVTRQSIPATTTHFLDLSADDKNQDAAVIIREALPVICKHIGVSDLFRPESFVPAGSKDSILRALQDAVREAKTTASSEIPSASIRPTELIDATVLKSPLSVVDWTVDGEVPVQVQPIDATQLFSQHKTYVLVGLSGRLGQSISQWMSQNGAGCICLTSRTPKADPEWQAEMEKKGTTVKLIPMDVTNRADVERVFADLRANSPPIAGVASGAAVFHDATFSEMTHEILEKVMNPKVVGTKNLDEVLGDTKLDFFIVFSSLTSVVGNSGQSNYTAANAYMTGLVGQRRKRGLAATSLDIGSIVGIGYLERASDTAREQLIRNGFMAVSETDLHQLLAEAIRAGATNSSASPMVTTGCRNVQEGEEFPVPWIDDPRMQHKVILGEHSSKAEMAGKKSALPVRDQLAVSKSTADALEILKELSECFAAKLAMISRLADGQVGHDIPLVELGIDSLVAVEVRGWFLKELKTDIPVLKVLGGGTVATLCQQALEKLPESILPNVESGGPSKTGSSKPTAKPSVAKPRSPPSPSGSETGSPGRWSENNTTSPQSTLSSDQSPSSTPATVLSNVPSNVDLTTVAKSEMALIPSSDFVKTELVSFQQSRFWFLGLLIDDQATFNVTFYLRITGNLRTGDLERAVRLVTNRHESLRTCFVAHEQEADLAYQKVLPNSLVRLKRKNINRVEDVDIEYAAMKQVPFDLASGNLMRLVLLTLSASEHYLLFNYHHILMDGVSLQNFLADLEKAYQRQPLGPPPCQVPEFSRVQRAAFESGVFNEDIAYWKNEFPNGHPVLPLLPMSHITSRMALNSFNVHQVECRVDSELMAKVREAARVNGCTTFHFYLATFKAMLFRFTDAGDLTIGIADANRISPDVEGTIGLLLNLLTLRFQRNPSQTFAQSVGEARGKALEALKHSNVPFDILLKELNVPRSSAYSPFFQAFFDYRQGHQEKLSFGSTEFEFLQVHPGRTAYDMTLDVTDGADSARILFRTQASLYDKTAAQLLLNTFIHLLDTFATNTSLKLDDFALFSDKELKLALNVGHGPNFESSWPGGTIPHRIDQIAKENDDKVALKDGHGTILTYGAMINRTQAIAAALQQVGVGESSRVLVFEDATVDWPCSMLAIMRLGAVYVPLDLRNPLPRLADVAGSCKPVAILVDSTTLDHVAQVNVTFAEVVNVSEVGVNSIKVANVSRSDAVAALLYTSGSTGKPKGIVVTHSGLRNEIEGYTSQWVLKAERVLQQSAFTFNHSSDQIYTGLVNGGFVYIVPWDKRGDPIEVTKIIKEENITYTKATPAEYSLWLDYGSGNLKQASSWRFAFGGGESLTGTITRSLATLQLPNLRFFNSYGPTEISISSTKMEVAYRDSPPDGRIPCGFMLPNYAAYILDDQRKPVPVGMPGELYIGGAGVSLGYLDNEELTEQHFLPNPYAIPEYVAQGWTRMYRTGDIAHLQGDGAMVFHNRIAGDTQVKIRGLRIELGDIESNIIKAAEGALKEVAVTLRDGDPPILVAHVVFAPHHHIVDTEAFLVQLLKNLDVPQYMVPVMAIPLERMPLSNHSKTDRKALKELPLPQRSNHDTGDNTESLTETMLELRRLWVDVLNTGELGLDIGPSTSFFTVGGNSLLIVRLQSRIRQTFNVTVRLFDLIDANTLSDMTQKIEESLNVDLIDWDKETALLSDFTMPEATKHQPLKTTDKVILVTGSGGFLGKHILTELIARPDVSKIHCIGLRDKPGNTPRRLALNSTKIITHSGDLTEPWLGLGEEKFASLTLEVDVILHMAATRSFWDNYSLLRPINVTPTKLLVQMATGRKIPIHYVSSAGVVSAEGVEILAGSAAKYQPRVDGSNGYVASRWASEQILEHAVSALDVPVSIHRFVPAKEPANQTVVVDALQHFVSFVDELSIMPDFSGTTGHFEMTPIHSAASQLAENLVKTPTQQSSLLEFVHHDCPIRIDIAEMVAFLEEQRGGKGLEKVPGLKFVGDMKRAGLAYFVTSQTLLMGGTNGTSVVLESRR

2.3.1.-; 6.3.2.-

amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; lactone biosynthetic process [GO:1901336]; methylation [GO:0032259]; organonitrogen compound biosynthetic process [GO:1901566]; polyketide biosynthetic process [GO:0030639]; toxin biosynthetic process [GO:0009403]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]

PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765;

3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150;

NRP synthetase family

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30811183}.

FUNCTION: Hybrid PKS-NRPS synthetase; part of the tra gene cluster that produces terrestric acid (PubMed:30811183). The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones (PubMed:30811183). The non-reducing PKS claF is responsible for the formation of clavatol from successive condensations of 3 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit, and 2 methylation steps (PubMed:30811183). The esterase claE probably collaborates with claF by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (By similarity). The clavatol oxidase claD then converts clavatol to hydroxyclavatol (PubMed:30811183). Spontaneous dehydration of hydroxyclavatol leads to the accumulation of the highly active ortho-quinone methide (PubMed:30811183, PubMed:31860310). On the other hand, the PKS-NRPS hybrid traA is involved in the formation of crustosic acid, with the help of traB and traD (PubMed:30811183). The polyketide synthase module (PKS) of traA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:30811183). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with L-malic acid (PubMed:30811183). Because traA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase traG (By similarity). Crustosic acid undergoes decarboxylation and isomerization to the terrestric acid, catalyzed by the 2-oxoglutarate-dependent dioxygenase traH (PubMed:30811183). Both acids are further converted to the 2 gamma-butyrolactones (R)-5-methyltetronic acid and (S)-5-carboxylmethyltetronic acid, with involvement of the cytochrome P450 monooxygenase claJ (PubMed:30811183). Spontaneous addition of the methide to these gamma-butyrolactones leads to peniphenone D and penilactone D, which undergo again stereospecific attacking by methide to give penilactones A and B (PubMed:30811183, PubMed:31860310). {ECO:0000250|UniProtKB:A0A0E0RXA7, ECO:0000250|UniProtKB:A0A161CKG1, ECO:0000269|PubMed:30811183, ECO:0000269|PubMed:31860310}.

Penicillium crustosum (Blue mold fungus)

A0A482A9N4

LP9A_TALVE

MPSTKVAALSAVLALASTVAGHGYVQNIVIDGESYSGYIVTQFPYESNPPAVIGWATTATDLGYVDPTEYTNADIICHKNATPGALSAPVAAGGTVELQWTTWPDSHHGPVISYLANCNGNCSTVDKTKLDFVKIDASGLIDDTTVPGTWASDQLIAANNSWTVTIPETIAPGNYVLRHEIIALHSAENTDGAQNYPQCINLEITGSGTASPTGTPGEELYTPTDPGILVNIYQSLSTYVIPGPTLWSGAANNAVASATAAASATATPTTLVTSVASATDSPSTVAPASSTTATSVLTSVVPSVTSFVPVVTVTDVVTVTTVITTTVF

3.2.1.4

COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|Ref.3}; Note=Binds 1 copper ion per subunit. {ECO:0000269|Ref.3};

cellulose catabolic process [GO:0030245]

extracellular region [GO:0005576]

cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; monooxygenase activity [GO:0004497]

PF03443;

2.70.50.70;

Polysaccharide monooxygenase AA9 family

PTM: The catalytically essential N-terminal histidine His-22 is post-translationally modified by methylation to prevent protonation of the histidine side chain, and protect the critical active site of the enzyme from oxidative damage. {ECO:0000250|UniProtKB:G3XAP7}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30847851}.

CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:30847851, ECO:0000269|PubMed:31672609};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:31672609};

FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (PubMed:30847851, PubMed:31672609). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (By similarity). Shows activity on cellulosic substrates (Avicel, carboxymethylcellulose) and xylan (PubMed:30847851). {ECO:0000250|UniProtKB:Q4WP32, ECO:0000269|PubMed:30847851, ECO:0000269|PubMed:31672609}.

Talaromyces verruculosus (Penicillium verruculosum)

A0A482D308

CS12F_UNCAX

MAKNTITKTLKLRIVRPYNSAEVEKIVADEKNNREKIALEKNKDKVKEACSKHLKVAAYCTTQVERNACLFCKARKLDDKFYQKLRGQFPDAVFWQEISEIFRQLQKQAAEIYNQSLIELYYEIFIKGKGIANASSVEHYLSDVCYTRAAELFKNAAIASGLRSKIKSNFRLKELKNMKSGLPTTKSDNFPIPLVKQKGGQYTGFEISNHNSDFIIKIPFGRWQVKKEIDKYRPWEKFDFEQVQKSPKPISLLLSTQRRKRNKGWSKDEGTEAEIKKVMNGDYQTSYIEVKRGSKIGEKSAWMLNLSIDVPKIDKGVDPSIIGGIDVGVKSPLVCAINNAFSRYSISDNDLFHFNKKMFARRRILLKKNRHKRAGHGAKNKLKPITILTEKSERFRKKLIERWACEIADFFIKNKVGTVQMENLESMKRKEDSYFNIRLRGFWPYAEMQNKIEFKLKQYGIEIRKVAPNNTSKTCSKCGHLNNYFNFEYRKKNKFPHFKCEKCNFKENADYNAALNISNPKLKSTKEEP

3.1.-.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30337455, ECO:0000269|PubMed:32246713}; Note=Mg(2+) is required for dsDNA cleavage (PubMed:32246713). Mg(2+) and Mn(2+) support ssDNA cleavage equally (PubMed:30337455). {ECO:0000269|PubMed:30337455, ECO:0000269|PubMed:32246713}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:33333018}; Note=Homodimeric Cas12f in complex with sgRNA and target DNA binds only 3 Zn(2+) ions. {ECO:0000269|PubMed:33333018, ECO:0000312|PDB:7C7L};

defense response to virus [GO:0051607]

DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]

PF07282;

CRISPR-associated endonuclease Cas12f family

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature for dsDNA cleavage is 46 degrees Celsius and occurs between 37-52 degrees Celsius, no cleavage at 55 degrees Celsius (PubMed:32246713). Optimum temperature for ssDNA cleavage is 45-55 degrees Celsius (PubMed:30337455). {ECO:0000269|PubMed:30337455, ECO:0000269|PubMed:32246713};

FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids (Probable). CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), which requires a trans-encoded small RNA (tracrRNA), but not this protein (in vitro) (Probable). Upon expression in E.coli of this protein, a mini CRISPR array and the probable tracrRNA, the protein associates with both RNAs (PubMed:30337455). The mini system is not active in E.coli against phiX174 phage, nor is it active in protection against transformation by foreign plasmids (PubMed:30337455, PubMed:32246713). In vitro the purified protein-tracrRNA-crRNA complex cleaves ssDNA complementary to the crRNA; target cleavage requires both tracrRNA and crRNA, but not a protospacer adjacent motif (PAM). The tracrRNA-crRNA can be replaced by a single guide RNA (sgRNA). 2-nucleotide mismatches in the middle of the crRNA:DNA heteroduplex decrease cleavage. Cleavage occurs just downstream of the heteroduplex (PubMed:30337455). Activation of this protein results in non-specific ssDNA degradation in vitro (PubMed:30337455, PubMed:32246713). In vitro and in E.coli (coexpressed with sgRNA) has dsDNA endonuclease activity, recognizing the 5' PAM sequence TTTR; both sgRNA and a PAM are required for activity. Cleaves the target strand 24 and the nontarget strand 22 bases upstream of the PAM (respectively), resulting in 5' overhangs (PubMed:32246713, PubMed:33333018). The 2 monomers interact differently with the sgRNA and target DNA. Mutagenesis of a dimeric construct shows that one of the RuvC monomers probably cleaves both DNA strands (PubMed:33333018). {ECO:0000269|PubMed:30337455, ECO:0000269|PubMed:32246713, ECO:0000269|PubMed:33333018, ECO:0000305|PubMed:30337455}.

Uncultured archaeon

A0A482N9V7

ICCA_TALVA

MAANDSNNQTKPQLPEEPVAIVGSSCRFPGSSNSPSKLWDLLRQPRDVLKEFDPDRLNLKRFYHPDGDTHGSTDVTNKSYLLEEDSRLFDASFFTINPAEAAGMDPQQRILLETVYEAFESAGMTLEQLRGSLTAVHVGTMTNDYAGIQLRDLETIAKYNATGTANSIVSNRISYVFDLKGPSETIDTACSSSLVALHHAARGLLNGDCETAVVAGVNLIYDAASYIAESKLHMLSPDSQSRMWDKSANGYARGEGAAALLLKPLSRALRDGDHIEGVIRATGVNSDGQSPGITMPFAPTQAALIRQTYRRAGLDPVKDRPQYFECHGTGTPAGDPVEARAISEAFEPSADNPIYVGSIKTIIGHLEGCAGLAGVMKVILALKNRTIPPNMLFNELNPAIAPFYGPLQIPKKAMPWPELPENTPIRASVNSFGFGGTNAHVIIESFESSTPSSDSEKCEEGALGPLLFSAGSGASLLHTVQAYVQYLDQNPSVDLRDLSWLLQTRRSTHRVRTHFSGTSSDAILESMIKFVNNNEKTPSTEVGHQPKLINPKEVPGILGVFTGQGAQWPQMGKELIGKSPIFRRTLEDCDATLQALPSSDIPKWSLVKELMANASSSRVAEAAISQPLCTAVQLGLVNMLKASGLNFDAVVGHSSGEIAATYASGIINLQAAIQIAYYRGFHAKLAKGEKGQQGGMLAAGLTLDKAKQLCLREEFVGRLQVAASNAPQTVTLSGDLDAIEEVKKYLDEENVFARQLKVDTAYHSHHMKPCAEPYLKSLLACDIEVRKPTPGQCIWNSSVRGDTGLLKGDLSSLKGPYWVANMVQTVLFSQAVESSIWHGGPWDLAIEVGPHPALKGPTEQTLKAVYGVVPLYTGVLKRGASDVEAFSTAIGVTWSQLGPSFVDFAGYRKTFYESEPPTPKVIKDLPGYSWDHDKVYWRESRISKRYRTGRDQTHELLGRRTPDDNEFELRWRNVLKLSEMPWLRGHEVLEEVLLPGAAYVSIAVEASKHIATSKGKSIELLEVEDVDIQRPVVVPDNKEGVETLFTARLLPGSSSDKVLKALFSYYICNDQSTGTMVHTCSGRLSVHLGEAKEDVLPQRDPVPQNLVNINTDRAYGMFKDIGLNYTGVFRSIKESSRTLQYSAATGIWPEGSLSDKYLVHPAMLDVAFQTLFIARAHPASRLITSALLPSHIERIQVSPSVPILHARENSDEIKADFDCWVVHQTASSLTGDLNIYDKVSGKTFLQVEGLTTKMVGEQDASGDRPVFTKTVWGSDGSLGLDEPERDPVGDAEGLSLAEAAERMALFYMKRVVKEISPEERTKFQWYHQRMFEAFEQHLVNVGSGSHPMLKSEWLSDDSSIMDGLDRIHPTSIDLKLLRACGENMPDVVREKTQLLEVMSKDDMLNRFYMDNCAARINNDIAKVVKQISFKFPRANILEIGAGTGGTTWSILKDINDAYDSYTFTDISSGFFPKAAEKFSDFAHKMIFKTLDVEKQPSEQGFAENSYDVIVAANVLHATRSLETTLRNARSLLRPGGYLILMEITNPESLRTTFIFGGFSGWWLSEEPHRKLGPVVTAMDWDTVLNDTGYSGADMVVHDLAEESKHLTSLIVSQAVDDDFLRLREPLSNLADMSAPTESILVIGGKKLLTSKMVNEINKLLPKSWKRHISSAGSIDDIDINELKPGTEVISLQELDDPLFSTPMTAERMSTIQNLMMSAKTLLWVTTAGKSHAPRASMFHGIARIVPSELQHLQIQVLGLEAGSTPAIATRHCVEAFLRLRGTSDTTREMLWAIEPEVEIMADGQVLIPRVVPDETLNQTYNASRRVVTKTVDATDLAVEAVAGPTKMMLQTAELQAGERKTRIQVKYALHLPAMDGKGIYVVYGQRQDDTSSFVLAVSKSNSSIVDVDSKHAVSVSDNCEPATLNVLATYLIARAIATLSKQAGSVLLSEPEESLAAIVATETAKQGTQAYFLSSKKVSPVEWIKVHANASKRAIQKAVPHDVQLLIDCSGIEASGNAVMASMPLHCVERQLDAHLLFDALESTESKPESLLEEAYQYATQLITQEQVQSECEVFPASDLPLTNMLSLVHKKYVTDWQQRDSLVVSVPPLDLEGIFKADKTYLMVGAAGGLGLSICEWMIRNGAKNLIITSRKPQVDQNMIEEASRVGATVKVMAMDVSSKESVAEVVQQAQEIMPPIAGVCNAAMVLSDKMFLDMDVDQLNGTLAAKVYGTEHLDAVFADAPLDFFIVLSSTATTIGNIGQANYHVANLFMTSLVAQRRARGLAGSVIHIGYVADVGYVTRQDRERQLEQHFRNVRLMALSETDVHHAFAEAVRGGRPGNTVGSPDIIMGLEPASVPLEPERQTLWLSNPCFGHLVPSTLQNDSSQTGGTGNGSSVRRQVEEAQTEDEAVDAVLDGFCAKLEAILQLREGSVKENVQRAVIDLGIDSLVAVEIRTWFLKELGAEVPVVKILGGDTVLQICTTAAKKVMANAMKKKEEDAVAEEGGREAASKKEPAPAASAPTPAPVAPSLLDVPARAFEPDSATISEVGDDSAFSNKGSSSSATGASSPKELSDSESVPDTSKDQSHVRPETVRDERMSPAQARIWFLTKHLDDPSAYNMVFHYRVKGPLKTVRLRHALQVATGHHESLRTLFYSRLEDGQPMQGVMPASAYELKHVPGADEADLKKELALLKAREWDLENGRTFSVSVLSRAADEHDVVFGYHHIIMDVVGWYFFVRDLDRAYRMQPFDKKISGSYVDYSVMQLSQKNTAAASDDLAFWQKEFSTVPDPIPLLPIAAVSARPTDSGRKVSHHEYLELDPAQNLAVKETCEKLRISPFHFHVAVLRALIGGYTNIDDMCIGVVDANRGDERFAQTVGCFVNMLPVRVEAPSDATFADIARSASRKALMAFAHSSAPLDMILDAVKAPRSSETTPLFQVAVNYRTGGVWDLPMGDCQMKLSLTDGKDAENPFDISLGIAETGKGCVIEMHCQKTLYSSDATRTLLNTYLRLVDTFCKNTHVKLKDCVIHDQAKVSEALQIGKGPTTDFGWPSTLSHRVLETCLKSPKNAAIQFKGELLSYEQLASRIHLVAAAIVRAGASKGSRVAVLCEPSADAIISMLATLHIGGVYIPMDVSLPTARHAAMMNGGQPTLLLSHAATKHRVEDLVNETGSTISVLQVDTISSVEEKETVSCAAEPHNNAVLLFTSGSTGTPKGIMLSQANFVNHLALKTDRLQLGQENVLQQSSMGFDMSLIQMFCALANGGCLVIAPSEMRRDPVELTNLVHNSQISLTIATPSEYLAWLRYGTASLKDHTIWRHACMGGEPVSRQLKTEFWRLDLANLQLTNCYGPTEITAAATFETIRLDDQDDDNDRAQHAVGKALPNYSVRILDTAGRPQPVDHIGEICIGGASVALGYLGLPEQTKAKFTVDPVSGERLYLTGDKGKLLSDGTLLCLGRLDGDTQIKHRGLRIELQEVESALIQTANGLFSSAVVSARGSILVAHATISQSQAEPSESDLAKILSRLKLPQYFIPATIGILPTMPTTANGKLDRKAIASLPLPQKVTGEEGPQEKMNIREGELRLLWERVLPDTATTTPLGPSSDFFLCGGNSMLLMKLQAAIKESIGIEISTRVLYQASTLREMALCVDEQREEQADALEQHFDWQAETSLPKWLLDQIEDLPKTTKQPPKPNGIDILMTGATSFIGGRLLRSLVRSPSVRKVHCVAVLADEQDQLYQDEKVKCYTGSLLSSTLGLNNGERDQLARNVDVVIHAGSSGHCLNTYGSLRTPNLVSLQFLASLALPRSIPLLLLSSNRVPLLSGNTALPPTSVAAFPPATDGREGYTATKWASEVFLEKLVGAVQKKAPRPWVASVHRPCVVVSEHAPNSDALNAILRYSASMKCVPHLESATGYLDFASVESIVDSMAESAIEMATGNVTDQPSIRFQHHSGGVKVPIGDFKVHMENVYGGNFEEVHLEEWMHRAAAAGLDPLITAYMEGIIEAGAPIVFPYLGETV

2.3.1.-; 6.3.2.-

fatty acid biosynthetic process [GO:0006633]; ilicicolin H biosynthetic process [GO:0140781]; methylation [GO:0032259]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; non-ribosomal peptide synthetase activity [GO:1904091]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218]

PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765;

3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150;

NRP synthetase family

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 8 AH2 + ATP + 4 H(+) + holo-[ACP] + L-tyrosine + 7 malonyl-CoA + 2 S-adenosyl-L-methionine = 8 A + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + N-[(4E,6E,10S,12Z,14E)-6,10-dimethyl-3-oxohexadeca-4,6,12,14-tetraenoyl]-L-tyrosyl-[ACP] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:64544, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16623, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17499, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:58315, ChEBI:CHEBI:59789, ChEBI:CHEBI:64479, ChEBI:CHEBI:155893, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:30905148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64545; Evidence={ECO:0000269|PubMed:30905148};

PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30905148}.

FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:30905148). IccA assembles the backbone of ilicicolin H (PubMed:30905148). The PKS portion and trans-acting enoyl reductase iccB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly (PubMed:30905148). The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate (PubMed:30905148). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (Probable) (PubMed:30905148). {ECO:0000269|PubMed:30905148, ECO:0000305|PubMed:30905148}.

Talaromyces variabilis (Penicillium variabile)

A0A482PDI9

NLEB_CITRO

MLSPLNVLQFNFRGETALSDSAPLQTVSFAGKDYSMEPIDEKTPILFQWFEARPERYGKGEVPILNTKEHPYLSNIINAAKIENERVIGVLVDGDFTYEQRKEFLSLEDEHQNIKIIYRENVDFSMYDKKLSDIYLENIHEQESYPASERDNYLLGLLREELKNIPYGKDSLIESYAEKRGHTWFDFFRNLAVLKGGGLFTETGKTGCHNISPCGGCIYLDADMIITDKLGVLYAPDGIAVYVDCNDNRKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGVGKGLKRHFNYSSLQDYNVFCNFIEFKHKNIIPNTSMYTNSSW

2.4.1.-

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B7UI21};

symbiont-mediated perturbation of host defense response [GO:0052031]; symbiont-mediated perturbation of host defense-related programmed cell death [GO:0034053]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034]

extracellular region [GO:0005576]; host cell [GO:0043657]

glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729]

3.90.550.20;

Glycosyltransferase NleB family

PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000250|UniProtKB:B7UI21}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16552063}. Host cell {ECO:0000269|PubMed:16552063}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:16552063}.

CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322; Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:31974499}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633; Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:31974499};

FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:16552063, PubMed:23955153, PubMed:24025841, PubMed:28522607). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TNFRSF1A and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:23955153, PubMed:28522607, PubMed:28860194). Has preference for host FADD as substrate compared to TNFRSF1A and RIPK1 (PubMed:28860194). Also acts on host proteins without a death domain: catalyzes GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2 and TRAF3, leading to inhibit NF-kappa-B signaling and type I interferon production, respectively (PubMed:23332158, PubMed:27387501, PubMed:28522607). Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB (PubMed:31974499). Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (By similarity). {ECO:0000250|UniProtKB:B7UI21, ECO:0000269|PubMed:16552063, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:28522607, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:31974499}.

Citrobacter rodentium

A0A494BA31

B3A4_MOUSE

MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGRLFGGLIQDVRRKACWYTSDFLDALHPQCFSAVFYIYLATVTNAITFGGLLGDATEGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWYVSATVISLAHIDSLRRESKACIPGEAPNFLGIREQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN

bicarbonate transport [GO:0015701]; monoatomic anion transport [GO:0006820]; regulation of intracellular pH [GO:0051453]; saliva secretion [GO:0046541]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085]

apical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886]

chloride:bicarbonate antiporter activity [GO:0140900]; sodium,bicarbonate:chloride antiporter activity [GO:0140892]; sodium:bicarbonate symporter activity [GO:0008510]

PF07565;PF00955;

1.10.287.570;

Anion exchanger (TC 2.A.31) family

SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12225984, ECO:0000269|PubMed:23610411, ECO:0000305|PubMed:34585968}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the basolateral membrane of the cortical collecting duct (CCD)and submandibular gland (SMG) duct. {ECO:0000269|PubMed:12225984, ECO:0000269|PubMed:23610411}.

CATALYTIC ACTIVITY: Reaction=chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) = chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72739, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:25745107, ECO:0000269|PubMed:27114614}; CATALYTIC ACTIVITY: Reaction=chloride(out) + 2 hydrogencarbonate(in) + K(+)(in) = chloride(in) + 2 hydrogencarbonate(out) + K(+)(out); Xref=Rhea:RHEA:75059, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:27114614}; CATALYTIC ACTIVITY: Reaction=chloride(out) + 2 hydrogencarbonate(in) + Li(+)(in) = chloride(in) + 2 hydrogencarbonate(out) + Li(+)(out); Xref=Rhea:RHEA:75063, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996, ChEBI:CHEBI:49713; Evidence={ECO:0000269|PubMed:27114614}; CATALYTIC ACTIVITY: Reaction=chloride(out) + 2 hydrogencarbonate(in) + Rb(+)(in) = chloride(in) + 2 hydrogencarbonate(out) + Rb(+)(out); Xref=Rhea:RHEA:75067, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996, ChEBI:CHEBI:49847; Evidence={ECO:0000269|PubMed:27114614}; CATALYTIC ACTIVITY: Reaction=chloride(out) + Cs(+)(in) + 2 hydrogencarbonate(in) = chloride(in) + Cs(+)(out) + 2 hydrogencarbonate(out); Xref=Rhea:RHEA:75071, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996, ChEBI:CHEBI:49547; Evidence={ECO:0000269|PubMed:27114614};

FUNCTION: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participate in salivary secretion (PubMed:25745107, PubMed:27114614). Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+) (PubMed:27114614). Does not contribute to Cl(-)/HCO3(-) exchanger in the apical membrane of the upper villous epithelium (PubMed:17170027). {ECO:0000269|PubMed:17170027, ECO:0000269|PubMed:25745107, ECO:0000269|PubMed:27114614}.

Mus musculus (Mouse)

A0A499UB99

OXDA_TALEM

MATNNIVVLGAGVSGLTTAWLLSKDPSNKITVAAKHMPGDYDIEYCSPWAGANYLPVGAENSRVGQWERATWPHLRDIAQNHPEAGIHFQDTVVYNRTKDQGSTTGQWFSELVKPNPWYGKVLPNFRELSKDELPPGIDNANRFTSVCINTAVYLPWLVGQCRKNGVVFKRAVFKHVAEAANAHHSGQKADLVVNCTGLSSRKLGGVQDNTLLPARGQIVVVRNDPGLMCSISGTDDGDDEVTYMMTRAAGGGTILGGTYQKHNWDSLPDPNLAVRIMKRCIELCPSLVAPGQGIEGLDIIRHGVGLRPVREDGPRIEKELIDGVWVVHNYGHGGYGYQTSFGCATTAVEVVREALQQQKQRRDKARL

1.4.3.3

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:31420577, ECO:0000269|PubMed:33135670};

D-amino acid catabolic process [GO:0019478]; D-amino acid metabolic process [GO:0046416]; nitrogen utilization [GO:0019740]

peroxisomal matrix [GO:0005782]

D-amino-acid oxidase activity [GO:0003884]; FAD binding [GO:0071949]

PF01266;

3.30.9.10;3.40.50.720;

DAMOX/DASOX family

PTM: The disulfide bond might contribute to the high thermal stability of the protein. {ECO:0000269|PubMed:33135670}.

SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q9HGY3}.

CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-glutamate + H2O + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:10028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29986; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10029; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-serine + H2O + O2 = 3-hydroxypyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70952; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-phenylalanine + H2O + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:57981; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70964; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-arginine + H2O + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32689, ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78220; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-methionine + H2O + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57932; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78208; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-leucine + H2O + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:143079; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78212; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-lysine + H2O + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:37583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32557, ChEBI:CHEBI:58183; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37584; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-valine + H2O + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78203, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:74338; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78204; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-histidine + H2O + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:78227, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58133, ChEBI:CHEBI:142967; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78228; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-glutamine + H2O + O2 = 2-oxoglutaramate + H2O2 + NH4(+); Xref=Rhea:RHEA:78215, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16769, ChEBI:CHEBI:28938, ChEBI:CHEBI:58000; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78216; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-isoleucine + H2O + O2 = (R)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:193151, ChEBI:CHEBI:228255; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78236; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-allo-isoleucine + H2O + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78223, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146, ChEBI:CHEBI:85306; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78224; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-threonine + H2O + O2 = (S)-3-hydroxy-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78251, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57757, ChEBI:CHEBI:228256; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78252; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-asparagine + H2O + O2 = 2-oxosuccinamate + H2O2 + NH4(+); Xref=Rhea:RHEA:78243, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735, ChEBI:CHEBI:74337; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78244; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-tryptophan + H2O + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:78247, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57719; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78248; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-tyrosine + H2O + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70959, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58570; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70960; Evidence={ECO:0000269|PubMed:31420577};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.213 mM for D-methionine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=0.628 mM for D-valine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=2.7 mM for D-alanine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=12.1 mM for D-glutamate (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=19.2 mM for D-arginine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; Note=kcat is 120 sec(-1) with D-methionine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 225 sec(-1) with D-valine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 189 sec(-1) with D-alanine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 90.7 sec(-1) with D-lutamic acid as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 45.6 sec(-1) with D-arginine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). {ECO:0000269|PubMed:31420577};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:31420577};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:31420577};

FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:31420577). Enables the organism to utilize D-amino acids as a source of nutrients (By similarity). Unusually, has high activity on D-glutamate (PubMed:31420577). {ECO:0000250|UniProtKB:Q9HGY3, ECO:0000269|PubMed:31420577}.

Talaromyces emersonii (Thermophilic fungus) (Rasamsonia emersonii)

A0A4P8DY91

COMTS_KITPR

MTTTELIPPTIQVDEEEEEACMFAMQLASASVLPMVLKSAIELDLLESIAKAGPGAYVSPSELAAKLPSSQPDTPVMLDRILRLLASYSVLKCKVQDLPQGGVERLYALAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNLGMSNHSTITMKKILQTYNGFAGLKTVVDVGGGTGATLNMIISKYPNIKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPEGDAIFMKWICHDWSDAHCLSFLKNCYKALPQNGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKEFEALGKMAGFKSFNKVCCAHNTWIMEFLK

2.1.1.-; 2.1.1.69; 2.1.1.70

aromatic compound biosynthetic process [GO:0019438]; coumarin biosynthetic process [GO:0009805]; methylation [GO:0032259]; response to hydrogen peroxide [GO:0042542]; response to UV [GO:0009411]

catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; O-methyltransferase activity [GO:0008171]; orcinol O-methyltransferase activity [GO:0102938]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF08100;PF00891;

3.40.50.150;1.10.10.10;

Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily

CATALYTIC ACTIVITY: Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11809; Evidence={ECO:0000269|PubMed:30934718}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + xanthotoxol = H(+) + S-adenosyl-L-homocysteine + xanthotoxin; Xref=Rhea:RHEA:17901, ChEBI:CHEBI:15378, ChEBI:CHEBI:15709, ChEBI:CHEBI:18358, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.70; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17902; Evidence={ECO:0000269|PubMed:30934718}; CATALYTIC ACTIVITY: Reaction=esculetin + S-adenosyl-L-methionine = H(+) + isoscopoletin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68944, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:81484, ChEBI:CHEBI:490095; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68945; Evidence={ECO:0000269|PubMed:30934718}; CATALYTIC ACTIVITY: Reaction=esculetin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + scopoletin; Xref=Rhea:RHEA:68948, ChEBI:CHEBI:15378, ChEBI:CHEBI:17488, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:490095; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68949; Evidence={ECO:0000269|PubMed:30934718};

PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:30934718}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30934718}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:30934718};

FUNCTION: O-methyltransferase involved in the biosynthesis of methoxylated coumarins natural products such as isoscopoletin, scopoletin, xanthotoxin and bergapten, photosensitizers used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses (PubMed:30934718). Catalyzes the methylation of esculetin, bergaptol and xanthotoxol, but seems inactive on scopoletin and isoscopoletin (PubMed:30934718). {ECO:0000269|PubMed:30934718}.

Kitagawia praeruptora (Peucedanum praeruptorum)

A0A4P8WAE5

PYIS_PYRGI

MAATFSEPVAIIGTGCRFPGQCNTPSKLWELLQTPKDLLKEIPENRFSTEAFYHPQNYHHGTCNVRHSYFLEEDLRGFDAQFFGINPVEAHSVDPQQRLLLETVYESLEAAGLSMKEMQGSDTAVYVGVMSADFTDMIGRDPETFPTYFATGTARSILSNRLSFFFDWRGPSMTIDTACSSSLIEPRTGANKPDCAEQVAGSNLILGSEQYIAESKLQMLSPTGRSRMWDADADGYARGEGVAAIVLKKLSQAIADGDHIECIIRETGANQDGRTPGITMPSATAQEALIRTTYKKAGLDISKRSDRPQFFEAHGTGTPAGDPIEARAVSNAFFGPRSHFSPTSPDDTLFVGSIKTVVGHTEGTAGLAAVIKASLALQAGVVPPNMHLSKLNPKIEPFYGNVQILSEARQWPKLAEGGVRRVSVNSFGFGGANCHAILEAYEPESTLDRRRYNKRTGKCFTPFLFSAATENALAAQLDKYRAHVACGNASAPGDLKKLSLTLSNRRSALPWRAVVPASNSVERLIENLDQCNDFTNETSASSLGTRPRILGIFTGQGAQWPRMGAALIESSPAAAKILARLDESLRLLPIRDRPTWSLREKILEGAESSSVAMAFISQPVCAAVQIMLVDMLRAAGIEFSGVLGHSSGEISAAYAAGYLSSEDAIRAAYYRGFHMKSLTQKKGAMIAVGTSYDDAKELCDLPAFEGRVCVAASNSPFSVTLSGDADAIDEVKALMDEEKKFNRLLQVDRAYHSHHMKACAAAYMASLQQCGVRTLTRTAASSRCQWVSSVYVRHSAELAAEGGLEAKYWASNLTMPVMFTEALQKLLGDCKDGKAYDLAIEVGPHPALKGPAVQTMSEFLGGQSIPYTGVLSRGKDDVESFSTTLGYIWRTLGEGAVDFLGYSRFMNEEQGEATITPLNGLPTYPWDHHRKFWHESRLSRAYRFNKDPVNELLGRQILDGAPDQLRWRNVLKRNELDWLDGHQVQRQTVFPFMGYVSACVEAAMKIRGDANVQSIELQNFKVGQAVAFNDDDSWIEILVVLDSIKESKVKGTKTISAHFAFHSSSNNETVDMTTHAGCDVLVTYGDSISDLLPPPEIQADDEYFMLGVESDRFYNVLDDIGLGYTGPFRALSGLQRKLGKATGRIKNPASSKLWRKPLLVHPAMLDAGIQSIMLAYCYPGDTMMRSIYLPTGIRRLIINPEHCQTFAGEETDVLFQSSASVDDPQGLSGDVSIYAPGGLSCKAIQVEGLQTQPLFNPTEANDLNIFTELVWGVDRPDAKEIVNKVDVQQLDGDLLFSLERVAYYYLRILDKSIPLSQRTGIDWHFGQLFAYVDHVLSRVERGTNRFARKEWQHDTKEIILEILERYPDNIDLRLMRAVGENIAAVIRGEITMLEPMLQNNMLNDFYVVAHGMPRYTKYLASLASQIGHRYPHMHVLEIGAGTGGATKSFLGALDDKFSTYTFTDISSGFFEKARSVFASYSAKMSFKMLNIEKDIGDQGFVEGSYDVVIASLVLHATRNLGQTLRNVRRLLKPGGYLLLLEITENDQMRFGLLFGGLEGWWLGYDDGRALSPCINIEEWEKYLKQTGFSGIDTLMPHDEILPVPLSVIVSQAVDERTELLKQPLQRLDPSTTLVPQLTIIGSGALAEEVHRLLRPFCGRVNVIESLGHMGADQLPVGGAVICLADIQEPVFKSMDADKLRGFQTIFKQSGSALWVTQGTLNGNPYSRMVIGFGRTIVLEMLHLRLQFLDLDHEAPADPTAIVETFIRLHLAENWKNDGVKITPLLHSVEPEMHIDKEGRGFIPRFKLNKKQNDRYNSGRRKIVKEVPLRQQPVELVPPKSEDASWLLAEGKNMPELKGAIDIDVFYTVTRAVEVSGGTFLYAVLGARRDTKEVVLALSPTQASIIRVPQAFIIPAQDSVEYLQLFYTELLARAVLRDVAAGTVVVVLRPTSMLSCAVDRLAADRGARVLHLADEPGSDWDYLHHKSSKVQVQDWVKSRLGTEAPPAVLLLDFGADQFLLAYLLECLPAEVTRAMVGAQSTSSKARMKLGQSEQEIRSFLADVRYALLPAQQTHQSSKGRSSLKVFTLEHLTTNRAGSDVSVVSWPAGTSTIPVQVQPVNSKVTFSNDKTYWLVGLSGTLGLSLCEWMAQQGARYIVITSRNPNVDERWKNKMEKLGIKVEIIANNICDRKSVRSVYSHICQTMPPIGGVAQGAMVLHDTAFSELDLERINKVMQPKVNGSIYLEEIFHNTPLEFFVFFSSMACVTGNPGQSAYAAANMFMSGLAVQRRKRGLNASVVHIGAIFGNGYVTRELSLEQQNFLRKVGNMWLSEQDFRQLFAEAVLAGQPENTGSPELSTGMMTIDNSEGTKENITWFDNPMFQHCIKESTDGKLGGQTAKGRAVPVKTQLLEAINSAEVYEIIHDAFAAKLRSSLQLEDDRPIVDQTADTLGIDSLFAVDIRSWFIKELQLEIPVLKILGGATVGEILETAQQLLPMELLPKMDPNDKSPARKLKAQPDSSPDKAASAERSRAKAQTAIENDGDRKFAATRAESGAKKGETVSKKVEAVTRPSVQWQVPVEPSTAVGDLDDKSFPGEDGVRLRAGSLDTTFTHKSSASSSASILDASEDQSADSVWSLDTVNNELAVSKKTPISFAQSRIWFLEKFLEDPASALNITLTIELDGSLDVDRFGKAVKLVGQRHEALRTRFVHGDDFDAPMQEVLVHSTLSLEQQDIASDAEADEVYRELQKYRYKLGEGENMRIILLKKSNQLFHLVIGYHHINMDGVSLEVVLRELQMAYDSKRLPNFGTILQYPDFAALQQKEYKSGAWQDEIEFWRKEFDGRPPSVLPLLPMAKTRSRTALTSYSSHTAEFSLDQITLAGIQSACESSKATPFQFHLATFYALLSRMVDAADICIGIGSANRHDTAMMQSVGIYLNLLPIVLKSQPNETFASTLKRVRSKVMTAFAHSRVPFDVIVNELGASRATTHNPLFQVLVNYRQGTATRRSFCGCQSEVRSFEQGQAAYDLGLDIIENPGGECKVIMTGQSTLFVPEDMDMLKDMYQRLLLAFSRNQALRLAIPSLYDPEMVKHALRIGRGPSYTHKWPETLIHQIDDIAKQKSHSLAIVDGSGTFLTYAHMSRRTNAIAASLRGIRRGSRVGVHLDPGADWVCSVLAIMRRDAVYLPLDAVSGYSRLSAILQDSKPDLVLVDNSTEKDATAYFSPILAADQIFNIDTVSVTPPETLAIAAKRGSVAALMYTSGSTGVPKGIIMKHESFRNNIEIISEKLGYNNGHTVTLQQSSFNFDMSLGQIFLALSTGGTLHVVPRHLRADPVAISSIIALHGITNTSATPSEFISWVRYGSVEELRNSAWAAVHSGGEPVRDSLKAAFLTVNKPGLRLLDCYGPTEVTFCSHISDVDYGAEETSMNKGLEVLPNYATYIVDSGMKPVPAGVPGEVLIGGAGVVAGYLHTELNTRGFAHDSFASDEFRKQGWEQLHRTGDFGRINKLNGRLLLEGRIADDTQVKLRGLRIDLKEIEAAMVRAAKGDILDCIVSVAQSADVSDEYLVAYATARPDASNHRLEHLMHQLPLPQYMKPATLVLLEKMPTNASGKIDRSAFKSIPLPKATEDNGMQPEVGQDLNDTESRLKQLWEGVLPKHVFSQHKFTAASDFFNVGGSSMLLISLRAKIQDTFAVVVSLFQLFEASTLGDMAALVDELSSGSAEKTAGPNSALDINWEDETAVSPALLGIPVEKKFFTNPEIVVLTGSTGFLGRAILTRLLNDGIVKEIHCFAVREEIPLFDSPKIIVHRGDLTLPGFGLSQKELASIFSKAHAVIHNGADVSFVKSYHSLKPANLEATKQLVDLCLPYQISFHYISTAAVVNLTGEKSWEQRSVGRFPPPAGTDGYIATKWASERYLEKFNDQYGLPIWIHRPSSITGPGAPANDLMANVVEFSRSTAATLNTNSWSGWLDFISVDEAALQIVDEVYEDYSWPGHVKYLYESGERVVALEDMKNVLEREVGSVFEVVDVEEWISRAEKQGFNPLLGEYLKRVANAPLVFPKLIRHEGFF

2.3.1.-; 6.3.2.-

amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403]

fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]

PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765;

3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150;

NRP synthetase family

PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31099577}.

FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable) (PubMed:31099577). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass (PubMed:31099577). The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine (PubMed:31099577). The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone (PubMed:31099577). The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor (PubMed:31099577). As the NRPS A-domain demonstrates substrate tolerance, pyiS can also use phenylalanine, tyrosine and even para-chlorophenylalanine as amino acid precursor, which leads to the production of novel cytochalasans, including halogenated cytochalasans (PubMed:31099577). Because pyiS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase pyiC (PubMed:31099577). Reduction by the hydrolyase pyiE leads to 1,5-dihydropyrrolone, which is substrate for dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase pyiF to yield the required isoindolone-fused macrocycle (PubMed:32039410). The tailoring cytochrome P450 monooxygenases piyD and piyG catalyze the hydroxylation at C-18 and C-7, respectivily, whereas the short-chain dehydrogenase/reductase pyiH reduces the carbonyl at C-21 in preparation for the transfer of an acetyl group by the acetyltransferase pyiB (PubMed:31099577). These 3 reactions whose order is not clear yet, lead to the production of O-methylpyrichalasin J, a deacetylated pyrichalasin H (PubMed:31099577). Finally, pyiB to converts O-methylpyrichalasin J into the final product pyrichalasin H via acetylation of C-21 (PubMed:31099577). {ECO:0000269|PubMed:31099577, ECO:0000269|PubMed:32039410, ECO:0000305|PubMed:31644300}.

Pyricularia grisea (Crabgrass-specific blast fungus) (Magnaporthe grisea)

A0A4V8GZX0

TXNA1_OMOSC

ECKGFGKSCVPGKNECCSGLTCSNKHKWCKVLL

extracellular region [GO:0005576]

ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729]

PF07740;

Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30784059}.

FUNCTION: Potently and reversibly inhibits some human voltage-gated sodium channels (Nav1.1/SCN1A (IC(50)=72.0 nM), Nav1.2/SCN2A (IC(50)=75.5 nM), Nav1.6/SCN8A (IC(50)=115.0 nM), Nav1.7/SCN9A (IC(50)=52.7-129.5 nM), Nav1.3/SCN3A (IC(50)=306.6 nM)) (PubMed:30784059). The hNav1.7/SCN9A channel inhibition occurs without any change in steady-state inactivation- and conductance-voltage relationships (PubMed:30784059). On adult mouse DRG neurons, this toxin is approximately 1000-fold more efficient to inhibit tetrodotoxin (TTX)-sensitive than TTX-resistant sodium currents (PubMed:30784059). In vivo, this toxin exhibits analgesic effects in mice pain models (PubMed:30784059). {ECO:0000269|PubMed:30784059}.

Omothymus schioedtei (Malaysian earth tiger tarantula) (Cyriopagopus schioedtei)

A0A4X1UM84

PCKGC_PIG

MPPQLSNGLNHSAKVVRGTLDSLPQAVRDFVESSAKLCQPDQIHICDGSEEENQQLLSHMEEEGVIKRLKKYDNCWLALTDPRDVARIESKTVIITQEQRDAVPIPRSGLSQLGRWMSPEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGSAVLDALGAGEFIKGLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGVTNPEGQKKYFAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDQQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQSNTIFTNVAETSDGGVYWEGIDQPLAPGIKLTSWKGTEWDPKDGEPCAHPNSRFCTPASQCPIIDPAWEAPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKDGRFLWPGFGENCRVLAWMFDRVQGKGGARLTPIGYVPEEAALDLRGLEAIRVSELFQVSKEFWEEEADEIHKYLEEQVNADLPYEIQSEVLALKQRISQM

2.7.11.-; 4.1.1.32

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P35558}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P35558};

cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; cellular response to potassium ion starvation [GO:0051365]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol biosynthetic process from pyruvate [GO:0046327]; hepatocyte differentiation [GO:0070365]; oxaloacetate metabolic process [GO:0006107]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of memory T cell differentiation [GO:0043382]; positive regulation of transcription by RNA polymerase II [GO:0045944]; propionate catabolic process [GO:0019543]; regulation of lipid biosynthetic process [GO:0046890]; response to bacterium [GO:0009617]; response to starvation [GO:0042594]; tricarboxylic acid metabolic process [GO:0072350]

cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]

carboxylic acid binding [GO:0031406]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; phosphoenolpyruvate carboxykinase (GTP) activity [GO:0004613]; protein serine kinase activity (using GTP as donor) [GO:0106264]

PF00821;PF17297;

3.90.228.20;3.40.449.10;2.170.8.10;

Phosphoenolpyruvate carboxykinase [GTP] family

PTM: Acetylated (By similarity). Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5, acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2 (By similarity). Deacetylated by SIRT1 (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000250|UniProtKB:Q9Z2V4}.; PTM: Ubiquitination by UBR5 leads to proteasomal degradation. {ECO:0000250|UniProtKB:P35558}.; PTM: Phosphorylated in a GSK3B-mediated pathway; phosphorylation affects the efficiency of SIRT1-mediated deacetylation, and regulates PCK1 ubiquitination and degradation. Phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity: phosphorylated PCK1 translocates to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2. {ECO:0000250|UniProtKB:P35558}.

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35558}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}.

CATALYTIC ACTIVITY: Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; Evidence={ECO:0000269|PubMed:26792594}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389; Evidence={ECO:0000250|UniProtKB:Q9Z2V4}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390; Evidence={ECO:0000250|UniProtKB:Q9Z2V4}; CATALYTIC ACTIVITY: Reaction=GTP + L-seryl-[protein] = GDP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:64020, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P35558}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64021; Evidence={ECO:0000250|UniProtKB:P35558};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=240 uM for phosphoenolpyruvate {ECO:0000269|PubMed:26792594}; KM=27.4 uM for GDP {ECO:0000269|PubMed:26792594}; KM=13.1 uM for oxaloacetate {ECO:0000269|PubMed:26792594}; KM=45.9 uM for GTP {ECO:0000269|PubMed:26792594}; Note=kcat is 6.8 sec(-1) with phosphoenolpyruvate as substrate (PubMed:26792594). kcat is 7.6 sec(-1) with GDP as substrate (PubMed:26792594). kcat is 46 sec(-1) with oxaloacetate as substrate. kcat is 39 sec(-1) with GTP as substrate (PubMed:26792594). {ECO:0000269|PubMed:26792594};

PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000250|UniProtKB:Q9Z2V4}.

FUNCTION: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:26792594). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (By similarity). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (By similarity). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (By similarity). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (By similarity). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000250|UniProtKB:Q9Z2V4, ECO:0000269|PubMed:26792594}.

Sus scrofa (Pig)

A0A4Y1WBN6

YYCJ_BACAN

MGLHFSVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLIGNIPTDQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDTGYVSDRMKGVIKGANAFVFESNHDVEMLRMGRYPWSIKRRILSDVGHVCNEDAALAMADVITDETKHIYLAHLSLDNNMKELARMSVSQVLEEKGFGVGEAFEIHDTDPKMPTKIQYV

3.1.11.-

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8ZRM2}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8ZRM2}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23491602}; Note=Binds 2 metal ions per subunit. The endogenous metal is unknown. {ECO:0000250|UniProtKB:Q8ZRM2};

exonuclease activity [GO:0004527]; metal ion binding [GO:0046872]

PF12706;

3.60.15.10;

Metallo-beta-lactamase superfamily

FUNCTION: 5'->3' double-stranded DNA exonuclease (PubMed:23491602). May play a role in mutation mismatch repair (MMR) (PubMed:23491602). Required for accurate coordination of cell division with DNA replication (By similarity). May play a role in cell wall metabolism (By similarity). {ECO:0000250|UniProtKB:C0SP91, ECO:0000269|PubMed:23491602}.

Bacillus anthracis

A0A4Y6HUD7

PALY2_PLEOS

MTILSGTTAAPRVNGTTMNGHSKPHTNGVHLNGHAPKATTESPWPQSEEKTLLDKFVEAYYEFESYKSGQTVKVDGKTLSLAGVVAAARHHAKISLDDSASIKDKVVKSRKVIADKVASGASVYGLSTGFGGSADTRTDQPLSLGHALLQHQHVGVLPSSSQPLDVLPLSDPMSATSMPEAWVRAAMLIRMNSLIRGHSGVRWELIEKIAEIFDANITPVVPLRSSISASGDLSPLSYIAGTVVGNPSIRVFDGPAAFGAREMVPSAKALASHGIDPLPLASKEPLGILNGTAFSAAVGALALNEAVHFAMLAQVCTAMGTEALVGTRLSFEPFIHATCRPHPGQIEAARNIYNLLEGTTFASVHHEEVHIAEDQGTLRQDRYPLRTSPQFLGPQLEDILHAYVSVTQECNSTTDNPLIDGETGEIHHGGNFQAMAVTNAMEKTRLALHHIGKLLFAQCTELVNPAMNNGLPPSLAATDPSLNYHTKGIDIATAAYVSELGYLANPVSTHIQSAEMHNQAVNSLALISARATVNSLDVLSLLISSYLYILCQALDLRALQMEFVKGVEEIIREELSLLFASVVSPAELEALTSKVLSAAQTSLDTSGSMDAPARMKKMASTTTIPLFDFLTELTLPDAISSGIAMVSIPSFRSHLASRATALLDQLRRDYLSGQRGAAPASPYLNKTRMVYEFVRLTLGVKMHGSENYARFAKGLGVEDETIGQNISRIHEAIRDGKMQAITVAMFA

4.3.1.24

cinnamic acid biosynthetic process [GO:0009800]; L-phenylalanine catabolic process [GO:0006559]

cytoplasm [GO:0005737]

phenylalanine ammonia-lyase activity [GO:0045548]

PF00221;

1.20.200.10;1.10.275.10;

PAL/histidase family

PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.

CATALYTIC ACTIVITY: Reaction=L-phenylalanine = (E)-cinnamate + NH4(+); Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; EC=4.3.1.24; Evidence={ECO:0000269|PubMed:31655558};

PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.

FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and a free ammonium ion (PubMed:31655558). Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids (By similarity). {ECO:0000250|UniProtKB:P11544, ECO:0000269|PubMed:31655558}.

Pleurotus ostreatus (Oyster mushroom) (White-rot fungus)

A0A4Z3

A3LT2_RAT

MALEGLRAKKRLLWRLFLSAFGLLGLYHYWFKIFRLFEVFIPMGICPMAIMPLLKDNFTGVLRHWARPEVLTCTSWGAPIIWDETFDPHVAEREARRQNLTIGLTVFAVGRYLEKYLEHFLVSAEQYFMVGQNVVYYVFTDRPEAVPHVALGQGRLLRVKPVRREKRWQDVSMARMLTLHEALGGQLGREADYVFCLDVDQYFSGNFGPEVLADLVAQLHAWHFRWPRWMLPYERDKRSAAALSLSEGDFYYHAAVFGGSVAALLKLTAHCATGQQLDREHGIEARWHDESHLNKFFWLSKPTKLLSPEFCWAEEIGWRPEIHHPRLIWAPKEYALVRT

2.4.1.87

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P14769}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};

carbohydrate metabolic process [GO:0005975]; cellular response to manganese ion [GO:0071287]; glycosphingolipid biosynthetic process [GO:0006688]; lipid glycosylation [GO:0030259]

Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; vesicle [GO:0031982]

alpha-1,3-galactosyltransferase activity [GO:0001962]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; N-acetyllactosaminide 3-alpha-galactosyltransferase activity [GO:0047276]

PF03414;

Glycosyltransferase 6 family

SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}; Single-pass type II membrane protein {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}. Note=Also found in numerous large vesicles throughout the cytoplasm of the soma.

CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:13013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507, ChEBI:CHEBI:138024; EC=2.4.1.87; Evidence={ECO:0000269|PubMed:10854427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13014; Evidence={ECO:0000305|PubMed:10854427}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = an isogloboside iGb3Cer (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:42000, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:52570, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; Evidence={ECO:0000269|PubMed:10854427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42001; Evidence={ECO:0000305|PubMed:10854427}; CATALYTIC ACTIVITY: Reaction=a globoside Gb3Cer + UDP-alpha-D-galactose = a globoside GalGb3Cer + H(+) + UDP; Xref=Rhea:RHEA:56740, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:88154, ChEBI:CHEBI:140743; Evidence={ECO:0000269|PubMed:10854427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56741; Evidence={ECO:0000305|PubMed:10854427};

FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addition of galactose to iGb3 itself to form polygalactose structures. Synthesis of iGb3 is the initial step in the formation of the isoglobo-series glycolipid pathway and is the precursor to isogloboside 4 (iGb4) and isoForssman glycolipids. Can glycosylate only lipids and not proteins and is solely responsible for initiating the synthesis of isoglobo-series glycosphingolipids. {ECO:0000269|PubMed:10854427, ECO:0000269|PubMed:12626403, ECO:0000269|PubMed:17206613}.

Rattus norvegicus (Rat)

A0A509ADH4

YOP1_PLABA

MRMSKLYKNKEKENEKPSNEPPIKQDSLKRMSSKFLGNSLNSFDLSGKLEQVDEYLKKYPFIIEFGYKLGIKPSYIVVFGGSALFISLVLGWGAALICNLVGFAYPAYQSFKAVESQGHAETKLWLTYWVVFSLFFFIEYLIDIILFWIPFYYVIKLLFLLYLYMPQVRGAETVYNYIIRPILLKHEKTIDDTVHKISQTATNHLNQFTGNIAEKLVQEGVRRRNV

endoplasmic reticulum tubular network membrane organization [GO:1990809]; vacuole organization [GO:0007033]

endoplasmic reticulum membrane [GO:0005789]

PF03134;

DP1 family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32432369}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the digestive (food) vacuole (PubMed:27484902, PubMed:32432369). Induces high curvature in membranes and causes membrane tubule formation (PubMed:27484902). {ECO:0000269|PubMed:27484902, ECO:0000269|PubMed:32432369}.

Plasmodium berghei (strain Anka)

A0A509AFG4

CDPK3_PLABA

MNQLCVERNLSISTAYIKSKPKKYIERIKKKKSSNKSIKSQHKFEGSKIANKNNELKDIKSKDPKHYENHINKNTKHKDILLKSKRSDNFKFSRRGFILSFTGNLEDFYNLSEEPLGKGTYGCVYKATDKLLKIQRAVKVVSKKKLKNIPRFRQEIDIMKNLDHPNVIKLLETFEDEEQIYLIMDLCTGGELFDKIIKKGSFVEMYASFIMKQIFSVLNYLHIRNICHRDIKPENFLFYDKSTESLIKIIDFGLAAYFNDIDYEMKTKAGTPYYVAPQVLTGCYDYKCDLWSAGVLFYIILCGYPPFYGESDHEILSMVKKGKYNFKGKEWNNISEEAKDLIKRCLTIDSGKRINASEALKHPWFKKKKGSFNLDVKMDIHVLENFKNYALLLKLQKLAMTIIAQQSNDYDLQQLKTVFLYLDEDGKGNITKNQLKKGLENSGLKLPQNFDVLLDQIDSDGSGRIDYTEFLAAALDRKHLSKKLIYCAFRVFDVDNDGEITTAELAHILYNGNKKGSITQKDVNQVKKMIQEVDKNNDGKIDFYEFCEMMKLKY

2.7.11.1

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IBS5};

intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; positive regulation of cell motility [GO:2000147]

cytoplasm [GO:0005737]; nucleus [GO:0005634]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]

PF13499;PF00069;

1.10.238.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16430692}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8IBS5}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8IBS5};

FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). In the mosquito midgut, regulates the gliding motility of the ookinete which is essential for the ookinete to invade the midgut epithelium (PubMed:16796674). However, another study showed that while required for ookinete invasion of the midgut epithelium, is not required for ookinete gliding motility (PubMed:16430692). {ECO:0000250|UniProtKB:Q8IBS5, ECO:0000269|PubMed:16430692, ECO:0000269|PubMed:16796674}.

Plasmodium berghei (strain Anka)

A0A509AH51

EIK2_PLABA

MLNMVDQKKGINNGSSTGVINNINGKIKNEFIFMYLIAAGGFSCVYKIKKKKSNKFYALKKIKFSANESNYEKKVLLNLREIECLRKLKNHPNIVSMNDFWLEVVQTLSKSKRERRGRRKEQQREQMGDKRREKRQQQRREKRKEQNTNTKKRVLITLSDHKKKKLKHLSCPENALNISNITNNERNVLKKDNWKNLILLKNFKKEKHNYNFNHQIELNKYNIMCLWKILNQMCVCKNEKKNIESLLPEQLIKNFKNFLFEKYILAIYDDCSYLNNKNNKTFIFFNNNLGNILHYLWWSYLGKNGKEKKNDIFKLLKYVSDNIIKDNTNLYNIILEFRHSLIELSRFPSNELGNVILNMRIPPNGSCELSEYISNMAKINKLEIYRNKNTLEKFIFKINCNNFDVYKMWINFKNDIIYEGKDVYKEHRKINLKRKIIKKKDIWIKGKKEKHLKNTIGNKCIKKINIYYEKPIHVFVYKSLTYKRQKHHKLWRKHYNNKKNWKYCLNKHENSKKYILFSKICRLMKTQMNKFKREEKFEKKKKIAITNIKVNYNDFEQDISSFNIQIYNKKNKNQLINRIKEQYEQLSISLNPYKLTYENENILRYNEHNYLFGLKNDNEKENIYNAIYFLNFYIWIRREINEYAIISKKRQICQNSRNYQSKKKFYIKRHNQKTYFFENIIFYHYIIMLFLDIEKYKNKFVSLFQYNLYRKLLKISKRIVLMLHRIETNVICIFLLKHFEDYFIRKGIHIVQDKSDRSNKGDEIGIHKMVKIWKSMIAISLIFGKKMYKKKKNIFNFFIELFLNNIQINIFKKFEILYLIIYFYNYFEKSKQFDIEGIGDIIYVWLSLINLFYDDKGKCIKILSKIFAKLNKKLYYVYWGKLYIIMNWTTIVDTIFIRNVLSINREGNYYWVIIVLKMINYFVNVAYTLTRMDIFFIKVMIKFYTRIGSAAATNSVSKNSYNEIFNNIFTLNFMNYIIYNSYFENEKKNYDIYTKYAILFIYCFIIQAYYFDTLFNIRSLESNEIANNLFPGYNYSYKNILLFYERLGRVIKNSNNTKICKYMWRKFINMWSNSIVIKENIISCLTTSRHIYFNILMNFMKIYCLDNILHIKKKKKKMNTPIVLTSKNDLKKWKDCELTKNPKSVKKGILIKKKNRNNNKKYKKKLKETHFIYNIKKVLFKKLVNINIETILYEQNGQCYILVFGSVIKKKNGQIKVKDTKIVRDINIIRDYRIYFYNYLEYFYKNNAHISDNINLIYARKWPYNNKNAVKQFCPYFDKIKDGNRKDIVSLYGNKILVKQNFSKIGNKIKNKKNNLCKKKMRTQKSIYNSNYWREKKENKLLNGNVNIIKKYKSEKIKKKELENFFDNIVYSSENDDFKIIFENATNSNACSTVDLASPNELNTKRNNINKKLKFFKHKKNSKKQKNYKNHKSHKKIFFKSVNNANRFFVTNVEPNPIMSNNHQIADSNDIYNNFSIQKKYEYNHKNCGNIYNTKDCDENDSSYICFLINEHEGQVLSHRHKELYKNMLGMERGNILYRDNACKLKDDFSCLHDQCDNSMIKACGTNELIKESTKIKRENMDKINKMNEVNQHISLETLKYKCSFKKIDKNLIQNKKKIIIRKICQINKTFYFKYNKINDKKRIYFDSVLCKSERHKTYKKRNENIKVILLKTLKGESNEYVLTTYLTEIYSDNINDPFENSRKKINSNEIFYQKTFDMYCIEDEGEVYEEQKRVNKNNKKKKYINEMIKMDTIRTDFEDNFTNSYNKKCNILKMASNINNKNNSGKKERDIKRQFLITNKKKHENNIKIFYNLFKLEESNVNSNPQTNPYYETVIHDNEDNIFYCLYKYIQQQVYRYCNCDIDEYTSNCIDKNVNKWEWYGFIKENENYDKIKTEINSNSFYNCREKHNICNSYNSVYQLEFRKLGNASKEKNFEEKKKIIKIEFRKSFNNFKLPSLLCILKWDNFFKPHFIIRCDNFLHTYNIYFDFFILLMNLFHKGEGSNLYRFNSNKSIIYNPYLSHQIYMVTKYFISNVHKINNKLPIHLENDILEIYSYNRFLTIPNKCSFKNCGNDNNNYDQRSKKHYFTKCGILNTEKVKPSKKRRIGWDGQRQRKRKDIINTLNEENQNMFCKNKEKKEENYKKIDTNISQFSEKNPVSNIDNEKNKQNFIKNKKYKFNLYIRMEYCKDTIENYINRRTRINIKRNIEIINMIIMGLNYIHNNNIMHRDLKPSNIFISNNDIVKIGDFGLASYDYLDDHKINTTKEEEIQKDLIINKNCDKIFFCNKKKLFSNYNSVFPLENGQISDVHNTKGDYNESSISKSKKFAIQNKNRNLRSCKRIFQWWSTIGELNILSKNRRRLTKFKSGSNTIHIRKSTLDENIIVRHANKCHNLSFSQNREHIDRNRMKKCNIIKNHIIKSNKSEKMNISMNVFLRCTKTRRYFTDEDKSVETRKKCSKTSEEENGNICDTKKKKNDIGEKMDKNKIAAQKKKKKKENKHPIGRRSTNSSISSAIVVKRNAYCRLEIEKYFLSKSFQNCRSNKKKKYINIKTIKNKFCSASNKNFGAKWMRIYRKGLHHDDIQEKSADQTTEQMGGCNKTVASDFSSNLKNKKESINHTLGIGTKLYSAPEQLEGNKYTKSVDIFSLGLIIIDLFIKTETNMERTQILCNARERILPDLLIKKHPNVASLCKKMLSLDYKSRPTSAQLYNKIISAGDIFLPDKCP

2.7.11.1

chromosome segregation [GO:0007059]; dormancy maintenance of symbiont in host [GO:0085015]; microtubule-based process [GO:0007017]; negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]

centrosome [GO:0005813]; cortical microtubule [GO:0055028]; membrane [GO:0016020]; nucleus [GO:0005634]

ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]

PF00069;

1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily

PTM: Auto-phosphorylated. {ECO:0000250|UniProtKB:Q8I265}.

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:20584882}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:20584882}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305};

FUNCTION: Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules. {ECO:0000269|PubMed:20584882}.

Plasmodium berghei (strain Anka)

A0A509AHB6

CDPK1_PLABA

MGCNQSKSANDVRGNKVNHVNSKKKNNKREDTNDGEEIAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCKEKNGHSEKAIKVIKKSQFDKGRYSDDNKNIEKFHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKNSLLNIKIVDFGLSSFFSKDYKLRDRLGTAYYIAPEVLKKKYNEKCDVWSCGVIMYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISDEAKELIKLMLTYDYNKRCTAEEALNSRWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNVLRNFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRRAFNLFDTDKSGKITKEELANLFGLTSISEKTWNDVLGEADQNKDNMIDFDEFVSMMHKICDHKTF

2.7.11.1

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P62344};

intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell motility [GO:2000147]; positive regulation of translation [GO:0045727]

cytoplasm [GO:0005737]; host cell plasma membrane [GO:0020002]; motile cilium [GO:0031514]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; symbiont-containing vacuole membrane [GO:0020005]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]

PF13499;PF00069;

1.10.238.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily

PTM: Myristoylated. Myristoylation and palmitoylation are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Palmitoylated. Palmitoylation increases in merozoites in response to low level of extracellular K(+) in the host blood. Myristoylation and palmitoylation are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Phosphorylation at Thr-230 may regulate CDPK1 kinase activity. Phosphorylation increases in response to an increase in intracellular Ca(2+) levels. Autophosphorylated in vitro. Autophosphorylation does not affect membrane localization in vitro. {ECO:0000250|UniProtKB:P62344}.

SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane {ECO:0000269|PubMed:22817984}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cytoplasm {ECO:0000250|UniProtKB:A0A2I0BVG8}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A0A2I0BVG8}. Host cell membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Note=Calcium and/or autophosphorylation does not affect membrane localization. {ECO:0000250|UniProtKB:P62344}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P62344}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P62344};

FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK4 and CDPK5 (PubMed:32866196). In the mosquito midgut and during the last stage of male gamete exflagellation, may play a role in the rupture of the host erythrocyte membrane (PubMed:22817984). In the mosquito midgut, required for the differentiation of the zygote into the ookinete by promoting the translational activation of a subset of repressed mRNAs; these mRNAs are kept repressed in the zygote by the DOZI- or CITH-containing mRNP complexes (PubMed:22817984, PubMed:24265753). Dispensable during the asexual blood stage (PubMed:24265753). {ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:22817984, ECO:0000269|PubMed:24265753, ECO:0000269|PubMed:32866196}.

Plasmodium berghei (strain Anka)

A0A509AJA5

ICP_PLABA

MKSITFFVFNICSILALLSHCEDNDIYSFDIVNETNWLKIAKNIFKGKSPSNFTIIPFNNTGSSNDNESNKEESVLLIRKKIKSNKNHDSSIISGDTVNGDISDLNYTASNFSDNSEDIEDNQKYPTTSYNSFNHLNSNIAFNEESEYIEINSESDLENKIKDINIKSNLEENNTMNESGKVDSKYELTGDEKCGKSLKLGNISNQTNQETITQSLSVGEILCIDLEGNAGTGYLWVLLGIHKDEPIINPENFPTKLTKKSFFSEEISVTQPKKYKIDEHDSSKNVNREIESPEQKESDSKPKKPQMQLLGGPDRMRSVIKGHKPGKYYIVYSYYRPFSPTSGANTKIIYVTVQ

extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; microneme [GO:0020009]; transport vesicle [GO:0030133]

cysteine-type endopeptidase inhibitor activity [GO:0004869]

PF12628;

2.60.40.2020;

Protease inhibitor I71 family

PTM: During the liver stage, proteolytically cleaved. {ECO:0000269|PubMed:20361051}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20361051}. Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269|PubMed:20361051}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:20361051}. Host cytoplasm {ECO:0000269|PubMed:20361051}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:20361051}. Note=During the asexual blood stage, localizes to the parasitophorous vacuole (PV) and to exomembrane structures beyond the limits of the PV (By similarity). Localizes to punctate peripheral structures in schizonts and rings (By similarity). Released after host erythrocyte rupture (By similarity). Secreted by gliding sporozoites (PubMed:20361051). Localizes partially with micronemes at the apical pole of sporozoites (PubMed:20361051). Released into the host cytoplasm by sporozoites (PubMed:20361051). During the host liver stage and in late schizont and cytomere stages, localizes mainly to the PV, but is also present in the parasite cytoplasm (PubMed:20361051). After completion of daughter parasite development, localizes to the host hepatocyte cytoplasm following the rupture of the PV membrane (PubMed:20361051). {ECO:0000250|UniProtKB:Q8I333, ECO:0000269|PubMed:20361051}.

FUNCTION: Cysteine protease inhibitor (PubMed:20361051, PubMed:21742259). Required for the invasion of host erythrocytes by merozoites (By similarity). In the mosquito vector, essential for the gliding motility of hemocoel sporozoites and, therefore, for salivary gland invasion and the subsequent transmission from the mosquito to the mammalian host (PubMed:24281719). Required for the invasion of host hepatocytes (PubMed:20361051). During the liver stage, may prevent host hepatocyte cell death likely by inhibiting host cysteine proteases (PubMed:20361051). {ECO:0000250|UniProtKB:Q8I333, ECO:0000269|PubMed:20361051, ECO:0000269|PubMed:21742259, ECO:0000269|PubMed:24281719}.

Plasmodium berghei (strain Anka)

A0A509AKL0

KGP_PLABA

MDDDEIIPKKNHPSNERNKKKAILSHEDFTGEDSLMENHLELRDKLTEDIVTIKASLKNNLVCSTLNENEILALSNYMQFFVFKSGDMVIKQGEKGSYFFIINSGKFDVYVNDKKVKTLTKGSSFGEAALIHNTQRSATIKAGTNGTLWGVQRSTFRATLKQLSNRNFNENRSFIDSVSVFDMLTEAQKNMITNACVIQNFKPGETIVKQGDYGDVLYILKDGKATVYINDEEIRVLEKGSYFGERALLYDEPRSATIIAKEVTSCASICRKLLNVVLGNLQVVLFRNIMTEALQQSEIFKQISPDQLNDLADTAIVRDYPANYNILHKDKIKSVKYIIVLEGKVELFLDDESIGILTRGKSFGDQYVLNQKQKFKHTLKSLEVCKIALITESCLADCLGNNNIDASIDYNNKKSIIKKMYIFRYLTDKQCNLLIEAFKTTRYEEGDYIIQEGEVGSRFYIIKAGEVEIVKNNKRLRTLGKNDYFGERALIYDEPRTASVISTVNNLECWYVDKSVFLQIIEGPMLAHLEERIKMQDTKVEMSELLTERIIGRGTFGIVKLVLHEPTKIRYALKCVSKKSIIELNQQNNIKLEREITAENDHPFIIRLVRTFKDSKYFYFLTELVTGGELYDAIRKLGLLSRSQAQFYLGSIILAIEYLHERSIVYRDLKPENILLDKQGYVKLIDFGCAKKIHGRSYTLVGTPHYMAPEVILGKGYGCTVDIWAFGVCLYEFICGPLPFGNDQEDQLEIFRDILTGQLTFPDYVTDTDSINLIKRLLCRLPQGRIGCSINGFKDIKENSFFADFDWDRLAGRLLEPPLISKSETYAEDIDVKQIEQEEEDNANTEIDDENWDIDF

2.7.11.12

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I719};

phosphorylation [GO:0016310]; signal transduction [GO:0007165]

cAMP-dependent protein kinase complex [GO:0005952]; endoplasmic reticulum membrane [GO:0005789]

ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]; metal ion binding [GO:0046872]

PF00027;PF00069;

2.60.120.10;1.10.510.10;

Protein kinase superfamily, AGC Ser/Thr protein kinase family, cGMP subfamily

PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8I719}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19779564, ECO:0000269|PubMed:27425827}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8I719}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8I719}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8I719}. Note=Predominantly localizes to the cytoplasm during schizogony. {ECO:0000250|UniProtKB:Q8I719}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12; Evidence={ECO:0000250|UniProtKB:Q8I719}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.12; Evidence={ECO:0000250|UniProtKB:Q8I719};

FUNCTION: Serine/threonine protein kinase which acts as a downstream effector of the second messenger cGMP (By similarity). Controls the release of Ca(2+) from intracellular stores by regulating phosphoinositide biosynthesis (PubMed:24594931). Ca(2+) signals are essential for merozoite and sporozoite invasion and egress from host hepatocytes and erythrocytes, and, in the mosquito vector, for gametocyte activation, and ookinete and sporozoite motility (PubMed:24594931). During the host liver stage, regulates the initial invasion of host hepatocytes by sporozoites by regulating sporozoite motility and microneme exocytosis (PubMed:27425827). Following parasite development in the hepatocytes, required for the release of merosomes, a vesicle containing the mature merozoites (PubMed:19940133, PubMed:27425827). During the asexual blood stage, required for the progression from schizont to the ring stage following merozoite invasion of host erythrocytes and for merozoite egress (By similarity). Regulates merozoite egress by promoting the release of exonemes and micronemes which contain proteins essential for egress (By similarity). Phosphorylates CDPK1 predominantly at the late schizont stage; phosphorylation at 'Ser-64' regulates CDPK1 protein-protein interaction and phosphorylation at 'Thr-231' may regulate CDPK1 kinase activity (By similarity). In the mosquito vector, required for the initiation of gametogenesis induced by xanthurenic acid, specifically the gametocyte differentiation from the crescent-shaped form to the spherical form (PubMed:24594931). Required for the gliding motility of ookinetes to reach and penetrate the midgut epithelium by promoting Ca(2+)-mediated activation of CDPK1 and CDPK4 (PubMed:19779564, PubMed:24594931, PubMed:30315162). Also required for microneme secretion in ookinete by promoting Ca(2+)-mediated activation of CDPK3 (PubMed:30315162). {ECO:0000250|UniProtKB:Q8I719, ECO:0000269|PubMed:19779564, ECO:0000269|PubMed:19940133, ECO:0000269|PubMed:24594931, ECO:0000269|PubMed:27425827, ECO:0000269|PubMed:30315162}.

Plasmodium berghei (strain Anka)

A0A509ALD0

ADA_PLABA

MEIPNEEIKFLKKEDIKNINLNGMNKKERYEIWKKIPKVELHCHLDLTFSGKFFLKWVRKYNLQPNMTDDQVLDHYLFTKEGKSLAEFIRKAISVSDIYRDYDILEDLAKWAVIEKYKEGVVLMEFRYSPTFVSSSHGLDIELIHKAFVKGIKNATEMLNNKIYVALICISDTGHSAASIKHSGDFAIKHKHDFVGFDHGGREIDLKDHKDVYHSVRNHGLHLTVHAGEDATLPNLNTLYTAINILNVERIGHGIRVSESEELIELVKKNNILLEVCPISNLLLNNVKSMDTHPIRKLFDAGVKVSVNSDDPGMFLTDINDNYEKLYIHLNFTLEEFMTMNNWALEKSFVNDDIKSKLKTMYF

3.5.4.31; 3.5.4.4

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:A5KE01}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01};

adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166]

cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]

2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872]

PF00962;

3.20.20.140;

Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family

CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000269|PubMed:19728741};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=57 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=4.4 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 4.7 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.35 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741). {ECO:0000269|PubMed:19728741};

PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000305|PubMed:19728741}.

FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (Probable). {ECO:0000269|PubMed:19728741, ECO:0000305|PubMed:19728741}.

Plasmodium berghei (strain Anka)

A0A509AMC3

PK4_PLABA

MYNKGINICLNEDNKCIILLHIIFNKCIVSFVASHILVEGKICFLNRIKNSKIFRRFGNINNHRRNNVKEYYKFVGRINKGKEKRNKCRIKLHRFYEYAKSYILKQIKWVLNKSKYIYFNIIYHLKTICYLKNAFFLQYTQRKYFSQNIENYIINSLPKHIQSFNPIKWSYYNNNEYASNYIIINNLNFIKYKNKYEKQYDIEMEEDINCKGANDIFYNSYNYCNNNNSNSKCDEKIEKNIVDKNIENKYNIKEYDKTNKSILFPIEEEFKKIIQIENNIERNYMVPNESNKNILYNIKNILEKIRNIEAISNINNYIDMKNTIESYKLNPDKCKEILHKDKDFRNKSKLCLSCFHNIIHKIIYYSKMENISFSDMYKQLLTNYNNTSCEYCNLINNSINSNNDFLSLYNDKNMYNWKNCEKNKFETLENEISCWNFNSSYGNHFQHIQKNSKIYRRILNEENEKAFNNIVGRNEMENDELYKRIHTENNYANQFTENNVDFGVYSDLREYNNGNEKYMLDENEMDQIIDEEVKKQEKNQNLNNMDFNNVNKKYNQLKDDNIIIFNKNNMHNNLYSNGLNDSNLEKNNILFPYEKYNNLDKNEMNLTKYSQNKQFYGQYKYDEAIYKYDLIVLDTSGYIYKVSTDGTYHWKYRIVKNIQYYINYEEENKIENYYNAFKKNNGKINMTHKDILRKNDYEQYHKLKLRAMKKLQYNNFIDVFNSNYKKNYPTYLNEQITEKDDIYKKKNYNYEKSKKKSKNKNAMKKLLSDYSGDLFYVDENNEAIPININIKDVVNNSPFKSTLFPNILFIGSRQSSIVNLDFDTGYVIKKYEENYDDLVKEKQKALPNKYEKFINKNSNVLHDKLEKYLDHSIDINDKNYYVNEEKDDLDKDYTIIDGKVAENNQQLDNIDLYNNEIETENNNGINHLLLIDGKGQIEEQSPNNGNKIIKGDVSNMTDECGTENCLSKHSKEEIEIANNKFNKNNKDKLLIQRTKIKNKKHFLMGKWYMNISNNNLLNINSSVLGINKKKRNSKKGENRNKKRKTQKRQLQISLVKWVIKAVDETSLKQKWITSWVDVGSIFITDSHKQDLSFINSLIDIDGNKLILRTLENNKVNKPYNNTISKNIEDAERNELEFASENYKNDIPNEIDEHNNKMGRNMNKLNSNIKSKIFIFSKEISSVFALQYKSKTNIFTLDTILKQNEKLFPEYDNIKPYSYNLLNLKNNSNALLLPFSSSNDYLKNNDKKNLPWNFNYDENGTNANNSIAFQNYNNFIVQRLNNISINITSIEKDLRYLLLSIIFVFDKHKKIPMNYIFQMKTLLHEYQKTKQKFMICLRGLNHNKNINIFSNHNDIRDTDIKHYGYNDYDYINKEMDAIDEPIHICEYTNKFIDLSFEGKEKCIDYCSMLNIWDKIFNNYTNHDDCLLLSNLYRILNSTYPLTNKDFNRIIDGIFLKNNESMLIKRRRKPNEGSRNHDLTEFSSQKHKKSWYWNIFYAITLVIVIPFIFIYRLFKKQTNNKNNNKIIMRKKKITDYDEDSNDTYDDELLNIDKVLLKRNKRKLANILKENGISSLNKTELEKYMKKSLKKAQDIEQLTLVDILARHARDSDSDSNFYDIHDGKYNLYPYYYSGQESKYSLPNMHYIDLSKSNSGETNKYDLNGNNLFYMHRRRAASQDVTYKQSFIVKKRVRSNYKLGNKYNKRNYTDYEKDKKNSSIKERNINEKAFDKSDFINFLKNFNKKFMKKNPFVDHLMKNNKTDSNNEFNNDNKEKSKYLYNEKYNLNSADEENKSPYAKKYSDEKKNRSKSSKYIENTQSNNNDNTNGNMNVGNHINNDKMNNKGSSARNLSIIQTSHIPYDAPLADFLENGRFTRTFQNISLIGQGGFGSVYKVSHRLEPGSPTYAVKFIYLKVSSLDNVNSRRYFREIAANRDIYSKHVVRYYTWWCEEPQFLPMDIIPKEIQNTLKKNKDPFKKVCNKNKKDNDYSSDCTVSSGENNKFDLKNYKKVITKKNSPKLKFYSDNDTPYNKRKNINQKNSFLNDKNLSDNIYIIENNKKKKKKKKKKKKIIYKEKKKGNIGINEDNKYSTFYEQNNPNNFSSTLQEYDPFGYGYLSENERDLIVFADNDESNGSGHSKKNDNDERKSLNNQNGIYNTGGDISKNGNVIHDDSNMLACQQSDKNSMTIKNTQGTSINGTINRNTISDETGTQGTNNNPKYSIDYHIDAIVKPKGESFTWVEKSPSNKYKKDSLDIINRNRKLIEEKNKKEKGQEKEKYKLKMNGELEKKENANKIKYYKKKNVGPEFSIVLLLQMEFCKGFTLRRWLDRSSRSDKPLYFTYGDKNTNHPLEFDLFKQLIKGLKDIHSTCFIHRDLKPENIFVDLDTYILKIGDLGLVRFIEEKKRENDLNNIDNFKDNIYTEINHNTITSQISLKGQMIGTPGYTAPEGGALCDEKADIYSAALILLELLCPRFNTIMERYKTLNDFRNYYTVPDYVKIHLNPWYILMLQMSKPNPADRPSAADLYNKIKVLLDPHLTDFTFSFNDINNDDLEYTGNRNVINSTNPNGDIKENVNQNNLVDDKGNNNIINGNEVDH

2.7.11.1

negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]

cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]

ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]

PF00069;

1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29241041}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:29241041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:29241041}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:29241041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:29241041};

FUNCTION: During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition (PubMed:29241041). Plays a role in trophozoite differentiation into schizonts (PubMed:29241041). {ECO:0000269|PubMed:29241041}.

Plasmodium berghei (strain Anka)

A0A509APX1

GCYB_PLABA

MKETDKIKSEVLNLMQLDGKREHINKNNKLYRKVIINPTSEDDLQKFCKNYFRIYQFSLYNFIRRLISLDAVIVYTLFMTVYIFSEISQGITKKYLFVDTAISLFLNIGILVVIESLFELKLLKDIKNANSQHYLRIVPKMSYFEKVMTKDIKVGNIIRVFQGEEFPADVVILYSKKNTNAVVDSFKIDGLYNKSIKYPVEKYKIDRDYLKMLSEINGVIKCELPNKNVFCFQGTYKLDKHPRSLHLSYENFALQSSILKGAEYIDGVVVYTGADTKKNLNIPRKIEENMTFCIKMNNVVYYLIFMYILFVLLSIIIKAIFYRKGKLLENSNDTFFTVLEDFIGLYILVLPVMLYSEKSLIYIIQSLKIERDTRMNKDENSNNTKVFNKNKNDALGTVDIIATARNGVLVNKKEILVSCTINNVLYSKKKFIISDEFLKLPSLNILDAERTNVSELLNLDERIFKDPENIFFPSRDFNNFLKILGNNTNPIYDPINGDFSKILKEIYRNYLNEEFLYKKIKLSSSVKSLLDNGYNQFLEDCESSYDCKEIIEDGLKNNEQSEKIEEFILGICACNRIIIYNEKFGDIEMKDNINEKSTSEHMNYDKDREVENIESENKYAVDSDGEENMNTIEHEDICLFNTSKNIGFHIYCYKKCLFFYNLKNICKEYYIICFHDFLRSNNYTMCILKNKKELDKGILYIRGYDFNILPYLCKNKNDINKIKKTIKIHTANYLKVILICKKNITNEDIAKYIYLKSVRSKFSFKFFDIIKTFFLYDLECIGIIGLKNDLNDGVVETFNDINNFDIRSWIFTNDSSKNTYLTALQCNLITPNSNLFIINFLNPDHSDEETVANYLFNNFLFSMENMKSRSYAIAINEMSLKNIMRSRYALKVFLCIIMRATVVLFCKLNNETKGKIISKFLSYTTPKLTVLGVGSTLNDAYLLKNTTISVCLTLNKQVNALYSISDYAMEEFKYVGELLILGRLNRFSLCRAFLWIIYLKVMIGSFYFFHNFDNFFSGSSISSILYSQTAFAIFHYSLIVAFASYEIDIPYKFIRNFPYIYQLARRKYFLNNTIIFLNIVESIFSSFISYYILRGNLFNLITHRKFTFHIFVLNFFLISEKILLFSKTWHIFFFIMTIIIVSILFIYINIYTLVDCLITGKCEFSLFDPEDSYFWISLLPILYINFIIDKFMKFVKNKIYPDITYHLSNTLKIETQEKFATNNKREEVITDKNIEKLAPVPKSYIIKEDNAYYGKSKKNKYIFDTLRKIIDIKIKYRNQQLNLEYKTYEKRNKLKLRIIILLLFIIFLITFTIQIIISKFIEKKLHSLSYLTVIYYIVAVLYLIKILIRNKTNYTYFYIIGKLLLVIGYLLEISENSVNNIINMLVTYSFTVCYIFFISFKILEGLVMCIIILSIAIWVYYHKNNNLNAMCTDFCDNPYTSLDNLEYINISCICKQQIFTFLICTLSFTLICLFMKYYEIYYLKKKFLTRYKQKVNLGKQIEILHTMLPSFLVEYLLVSDPKADGIMVGKNISGEDRGIISVIFCDIDDFQTMVSTLEPHTLVQTLDNLYLYFDKCIKYFNCIKIETVFESYLAASGLSEKKNNCVHKIKYDTKCAIKMAIAQLSAKYYISYKVLDTLSNNKDSNSIFPIESKYIYKNISLRIGIHTGKAISGVIGSVKPQYSLFGDTVNTASRMKSTSLKDHIHVSYDTYKYLKDDKTLVWKERSIFIKGKGEMKTYLLVDILDNSKKDHTKALEESTSSIFRSNDEIVNKSELITKEKEFDKIEMPDKSEIIDETKKIFKKSEKPSTKKKKIKKENAKEKNINIKMKEMGEILNNYDKEKVYNCNKSDDGSNSIGQNDFLYSTKNYNYKKSKYLDLERLSTNKSFRRNVLAYNFESPINLPPKIGDNTKRNYDSDNFFTSPYIIDKNEKDEIRDTTNKALYIKKSKNIINRMREDSIDFKDEFSKENDKIKEYIKERITYRQKVTPNYFNFNNMSKYSNAFKKKKKKKKDIQKKYTYRQKTSFYNFLNKNDIINYNYSSEFEYFIDPKMKNKKPINFNNLFAKIYKKKLSLLNIKNEPINIKKKNIKNKSRDRIIFSSRRDEEHDDNQKMNKKLFSRTYAQKAEQTSHENIFTEMINDNFLKKEDKEQCEIRNENRCPTVFLIKRNKTTININKNRVLKRIFKDIITRKKIKRNRILKNKKLNYVNKNDNLGKKYEILNNICLVHKRAMTFVQYNTEDEEKKRTKRFHKNDEIFGSDMNISRNLNGSNSNIQNINRRSKNKAEDDLFIRNKVNLNNIKNNINLRKNIYKTDERGMQYNDLKGYDKKKNTEENNEDKEKKIEYDSNENIKNGFPKNEDKMIMKKRMISKRISFYSLKEYEKGDSFKSYDNSSCGIKSKKTNSIISDEEMNEYFNYNTEFNSNRNKNKQNKEFSLASKVNNIFKNIFKKNYISDKLKSGKYNTMSNSKSGQTNITTDNKKSQIKKNGDVNKANTNVSNKNSDFVTNFDNYNKNILKKLTSTLQINRKTSYFNRFYYKFKDEELEEEYTREYYQEIINIDLTKKLIIIFVISELILSLCNVIELSYYENKETPNDFIVIIWLIRSIYLFTITFIWLLLKTKLKEYKDNSSKMMWTTFILNIFLSSWGIIMIDLACIHYSNLVGNSRERSIFFMKDATELIISMQLIFVKNMLFKHKFFFFVFFFVFLMYSFFKLFVIHVCELRICCSILLILSINILYFWYSEYLDRTQYIIKRKRNRMERTSHDFLTRILPRQVLEEYQNDNLQLTYKHEKIAFLFADIVGFTKWSKTAAPKNVLKLLQKLISKIDKDTIKLGLYKLFTIGDAYVATSQPNASITDQTEAADGIISIFKLAKLILHNINTIKIQFNKHDFNMRIGLHYGSCVGGIIGSVRIRYDMWGLDVLIANHIESNGIPGEIVCSEQFKNFFLENEPHAKLNFWHYKTISINDKDIKIYVVEDKNYEEDYDPKIINYETLLKLREQNKVKG

4.6.1.2

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IDA0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8IDA0}; Note=Binds 2 magnesium ions per subunit (By similarity). Is also active with manganese (in vitro) (By similarity). {ECO:0000250|UniProtKB:P30803, ECO:0000250|UniProtKB:Q8IDA0};

intracellular signal transduction [GO:0035556]; phospholipid translocation [GO:0045332]; positive regulation of cell motility [GO:2000147]

plasma membrane [GO:0005886]

ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; guanylate cyclase activity [GO:0004383]; metal ion binding [GO:0046872]

PF00211;PF16212;

2.70.150.10;3.40.50.1000;3.30.70.1230;

Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily; Adenylyl cyclase class-4/guanylyl cyclase family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q8IDA0};

FUNCTION: Catalyzes the synthesis of the second messenger cGMP from GTP (By similarity). Probably by regulating cGMP production, required for ookinete gliding motility, which is necessary for the ookinete to traverse the midgut epithelium of the mosquito (PubMed:17030505, PubMed:19779564). {ECO:0000250|UniProtKB:Q8IDA0, ECO:0000269|PubMed:17030505, ECO:0000269|PubMed:19779564}.

Plasmodium berghei (strain Anka)

A0A509AQ68

ENO_PLABA

MAHVITRINAREILDSRGNPTVEVDLETTLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQQAIKNINEIIAPKLIGLDCREQKKIDNMMVQELDGSKTEWGWSKSKLGANAILAISMAICRAGAAANKTSLYKYLAQLAGKNTEKMILPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEAMRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNAHEALDLLVASIKKAGYENKVKIAMDVAASEFYNIETKTYDLDFKTPNNDKSLVKTGQELVDLYIELVKKYPIISIEDPFDQDDWENYAKLTEAIGKDVQIVGDDLLVTNPTRIEKALEKKACNALLLKVNQIGSITEAIEACLLSQKNNWGVMVSHRSGETEDVFIADLVVALRTGQIKTGAPCRSERNAKYNQLFRIEESLGANGSFAGDKFRLQLN

4.2.1.11

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IJN7}; Note=Binds 2 Mg(2+) ions per subunit (By similarity). Mg(2+) is required for catalysis and for stabilizing the dimer (By similarity). Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form an active closed conformation (By similarity). Inhibited by high levels of Mg(2+) (By similarity). {ECO:0000250|UniProtKB:Q8IJN7, ECO:0000250|UniProtKB:W7JLR6};

glycolytic process [GO:0006096]

cell surface [GO:0009986]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]; vacuole [GO:0005773]

magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]

PF00113;PF03952;

3.20.20.120;3.30.390.10;

Enolase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21949403}. Nucleus {ECO:0000269|PubMed:21949403}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:W7JLR6}. Cell surface {ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}. Cell membrane {ECO:0000250|UniProtKB:Q7RA60}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7RA60}. Vacuole {ECO:0000250|UniProtKB:Q8IJN7}. Note=Partially localizes to the nucleus in rings and trophozoites. Localization to the nucleus and food vacuole is higher in early and mid-stage trophozoites compared to the late-stage trophozoites and schizonts (By similarity). In the nucleus, localizes to heterochromatin region (By similarity). In rings, nuclear localization is dependent on the actin cytoskeleton (By similarity). Localizes to the cell surface of merozoites (By similarity). In gametocytes, predominantly localizes to the actin cytoskeleton (By similarity). In the trophozoite food vacuole, colocalizes with hemozoin, a product of heme detoxification (By similarity). In sporozoites, localizes to punctate structures beneath the cell membrane (By similarity). Localizes to the cell surface of ookinetes, especially on the apical pellicle complex that is involved in invasion (PubMed:21949403, PubMed:24474798). When phosphorylated at Thr-339, localizes to the cytoskeleton (By similarity). When phosphorylated at Ser-42, localizes to the cytoplasm (By similarity). When ubiquitinated at Lys-138, acetylated at Lys-133 and Lys-375 and phosphorylated at Tyr-139, localizes to the food vacuole (By similarity). When triubiquitinated at Lys-138, appears to colocalize with hemozoin in the food vacuole (By similarity). {ECO:0000250|UniProtKB:Q7RA60, ECO:0000250|UniProtKB:Q8IJN7, ECO:0000250|UniProtKB:W7JLR6, ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.

CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000250|UniProtKB:W7JLR6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000250|UniProtKB:W7JLR6}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10166; Evidence={ECO:0000250|UniProtKB:W7JLR6};

PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:Q8IJN7}.

FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (By similarity). In addition to glycolysis, involved in various processes such as parasite development and invasion (PubMed:21949403, PubMed:24474798). Plays an essential role during ookinete invasion of the mosquito vector midgut by mediating the interaction of the ookinete with the midgut epithelium and, further, by binding to mammalian host plasminogen in the blood meal, whose conversion to active plasmin promotes the invasion process (PubMed:21949403, PubMed:24474798). {ECO:0000250|UniProtKB:W7JLR6, ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.

Plasmodium berghei (strain Anka)

A0A509AQE6

CDPK5_PLABA

MCEHKANNKNDGEFVNLKEKNENNHCGNTKSTIADCDDDYSIITLCTKCLSTKTEVNKNKIILDSKALKDSRTKRRSSVNINIDILNNNLNLSPYFDRSQIVQETILMNNDDLEKLYELDKYKLGKGSYGNVVKAINKKTGQAKAIKIIDKKRINNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCTGGELFDKIVKHGSFSEYETYKIMKQIFSALAYCHSKNIIHRDLKPENILYVDSSDDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILKGKYDKKCDIWSSGVIMYILLCGYPPFNGKNNDDILKKVKKGEFVFDSNYWSKISLDAKELICECLNYNYKERIDVHKIVNHKWFIKFKNYNHITINKHLSKELIEKFKKFHKLCKIKKLAITCIAYQLNKKKFGKMKKTFEAFDHNGDGVLTISEIFQCLKVGDNEIDRDLYYLLKQLDTDGNGLIDYTEFLAACLDHSILEQDAVCRNAFKIFDANGDGIITKDELLNVLSFSNDQMPFSKEIIENVIKEVDANNDGYIDYDEFYKMMSGRQS

2.7.11.1

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A5K1K8H0};

intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell motility [GO:2000147]

cytoplasmic vesicle [GO:0031410]; microneme membrane [GO:0033163]; nucleus [GO:0005634]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]

PF13499;PF00069;

1.10.238.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily

PTM: May be palmitoylated. {ECO:0000250|UniProtKB:A0A5K1K8H0}.; PTM: Autophosphorylated in vitro. {ECO:0000250|UniProtKB:A0A5K1K8H0}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000250|UniProtKB:A0A5K1K8H0}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A5K1K8H0}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cell membrane {ECO:0000250|UniProtKB:A0A5K1K8H0}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A5K1K8H0}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A5K1K8H0}. Note=During the late stages of schizogony, localizes to the cytoplasm in immature daughter merozoites, co-localizes with AMA1 to a subset of micronemes and to the apical region in maturing daughter merozoites, and near the plasma membrane in mature daughter and free merozoites. {ECO:0000250|UniProtKB:A0A5K1K8H0}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A0A5K1K8H0}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A0A5K1K8H0};

FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). Plays a central role in host erythrocytes and hepatocytes infection cycles (PubMed:32866196). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK4 (PubMed:32866196). Involved in merosome egress from host hepatocytes, probably together with CDPK4 (PubMed:32866196). Required for the release of hepatic merozoites from merosomes in the host blood stream (PubMed:32866196). During the asexual blood stage, required for merozoite egress from host erythrocytes by triggering microneme secretion (By similarity). Phosphorylates transporter NPT1 at late schizont stage (By similarity). {ECO:0000250|UniProtKB:A0A5K1K8H0, ECO:0000269|PubMed:32866196}.

Plasmodium berghei (strain Anka)

A0A517FNB9

C9B52_PARPY

MEGLLLLLPTAIIALYLYISLIRRSRKKHNLPPGSDGWPFLGETFSYLKPHSAISIGRFMEDHISRYGKIYRSNLFGEPTIVSADAELNRFVLQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRMISLNFMSAARLRTRLMPEVERQTLLVLRSWREGSTFSAQEEAKKFTFNLMAKHIMSMDPGEPETEMLRREYITFMKGVVSAPLNFPGTPYWKALKSRSSILAVIERKMEERIGRRDRGDGGVEDDDLLGWAMNQSNLLKEQILDLLLSLLFAGHETSSMALALAIYFLESCPEAVRDLRDEHLAISMSGKEGECGLSWDQYKQMEFTHCVINESLRLGNVVRFVHRKAIQDVQYKGYDIPCGWKVLPVFAAVHLDSTLYSDPHRFNPWRWQSSSSKTTAANFMPYGGGLRLCTGSELAKLEMAVFLHHLVLNYQWKLAEPEQAFAYPFLDFPKGLQIKVRAIT

1.14.14.-

brassinosteroid biosynthetic process [GO:0016132]; cholesterol metabolic process [GO:0008203]; steroid biosynthetic process [GO:0006694]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69839, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:31324795}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69840; Evidence={ECO:0000269|PubMed:31324795};

PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:31324795}.

FUNCTION: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation. {ECO:0000269|PubMed:31324795}.

Paris polyphylla (Daiswa polyphylla)

A0A517FNC5

C90G4_PARPY

MAPVVILFFLFPTLLVLVVAVLGLRGGDDSWKKRGLKVPPGSMGWPLLGETIAFRRLHPCTSLGEYMEEHVNKYGKIYRSNLFGAPTIVSADAELNRFVLMNDERLFEPCFPKSVADILGHTSMLVLTGEMHRYMKSLSVNFMGIARLRNNFLGDSELYITQNFNRWKENIPFPAKEEACKVTFNLMVKNILSLNPGEPESEHLRKLYMSFMKGVVAIPLNLPGTAYKKAIQSRATILKMIEKLMEERIRNKKAGTDKIGEADLLGFILEQSNLDAEQFGDLLLGLLFGGHETSATAITLVIYFLYDCPKAVDHLREEHLGIVRAKKARGEPPALTWDDYKQMEFSQCVVSETLRLGNIIKFVHRKAKTDVQFKGYDIPKGWSVIPVFAAAHLDPSVYENPQKFDPWRWQTISTGTARIDNYMPFGQGLRNCAGLELAKMEIVVFLHHLTLNFDWEMAEPDHPLAYAFPDFPKGLPIKVRRLALK

1.14.14.-

cholesterol metabolic process [GO:0008203]; saponin biosynthetic process [GO:0016135]; steroid biosynthetic process [GO:0006694]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=cholesterol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (16S,22S)-dihydroxycholesterol + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:72191, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:191938; Evidence={ECO:0000269|PubMed:31324795}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72192; Evidence={ECO:0000269|PubMed:31324795};

PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:31324795}.

FUNCTION: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones (PubMed:31324795). During the 5,6-spiroketalization of cholesterol, catalyzes the hydroxylation of cholesterol to form 16S,22S-dihydroxycholesterol and, possibly, the subsequent conversion of 16S,22S-dihydroxycholesterol into 16-oxo-22-hydroxy-cholesterol and 16-hydroxy-22-oxo-cholesterol (PubMed:31324795). 16-hydroxy-22-oxo-cholesterol submit a spontaneous reaction leading to the production of furostanol-type steroid diastereomers, precursors of diosgenin (PubMed:31324795). {ECO:0000269|PubMed:31324795}.

Paris polyphylla (Daiswa polyphylla)

A0A517FNC6

C9B51_TRIFG

MSDSDITFYCLSSILSVLLIFIFILIKRKQAKPKLNLPPGKMGWPFLGETIGYLKPYSATTLGEFMDQHIARYGKIYKSKLFGEPAIVSADAGLNRFILQNEGKLFECSYPRSIGGILGKWSMLVLVGDMHRDMRLISLNFLSHARLRTHLLKEVEKHTRLVISSWKENSTFAAQDEAKKFTFNLMAEHIMSLQPGKIETEKLKKEYVTFMKGVVSAPLNFPGTAYWKALKSRGTILKFIEGKMEERIKRMKEGNENLEEDDLLNWVLKHSNLSTEQILDLILSLLFAGHETSSVSIALAIYFLPGCPQAILQLREEHKEIARAKKQAGETELTWEDYKKMEFTHCVVNETLRLGNVVRFLHRKALKDVRYKGYDIPCGWKVLPVIAAVHLDPLLFDQPQHFNPWRWQNNGNCPNFSGASSNSNNIFLPFGGGPRLCAGSELAKLEMAVFIHHLILNYHWELTDNNDQAFAYPFVDFPKGLQIRVQSHSLI

1.14.14.-

brassinosteroid biosynthetic process [GO:0016132]; cholesterol metabolic process [GO:0008203]; steroid biosynthetic process [GO:0006694]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69839, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:31324795}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69840; Evidence={ECO:0000269|PubMed:31324795};

PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:31324795}.

FUNCTION: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation. {ECO:0000269|PubMed:31324795}.

Trigonella foenum-graecum (Fenugreek)

A0A5B8NIM2

CMU_ERYQU

MDAAVDLLDPSKALNLKHIRQQLIRMEDTITFQLIERVQFPLNRTVYEPGAVKIPNSNLSFLDWTLREREKTDSLIRRYQSPDEHPFFPDALLKPILQPLIYPKILHRNNINLNDKIKKYFTDQVLPSICHDFGREDRGEQAENYGSTVTADIQCLQTLSRRIHFGKWVAESKYIDDPQGFAKLIKAGDRQAIGKAITKPAVELQVLERIRLKSRTYSTDPCESDDPEPKINVDAVVAMYRDCVIPLTKEVEIDYLMQRLSD

5.4.99.5

chorismate metabolic process [GO:0046417]; effector-mediated suppression of host salicylic acid-mediated innate immune signaling [GO:0140502]; L-phenylalanine biosynthetic process [GO:0009094]; tyrosine biosynthetic process [GO:0006571]

cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]

chorismate mutase activity [GO:0004106]

1.10.590.10;

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:33010586}. Secreted {ECO:0000305|PubMed:33010586}. Host cytoplasm {ECO:0000305|PubMed:33010586}. Note=Appears to be secreted despite an apparent lack of a secretory signal. {ECO:0000305|PubMed:33010586}.

CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:33010586}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000269|PubMed:33010586};

PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:33010586}.

FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:33010586). May function both as an effector during plant infection and in the fungal tyrosine and phenylalanine biosynthesis pathways (PubMed:33010586). During infection it channels chorismate into the phenylpropanoid pathway, thereby decreasing the synthesis of the plant immune signal salicylic acid (Probable). Within fungal cells, it acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (Probable). {ECO:0000269|PubMed:33010586, ECO:0000305|PubMed:33010586}.

Erysiphe quercicola (Hevea powdery mildew)

A0A5B9

TRBC2_HUMAN

DLKNVFPPKVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG

adaptive immune response [GO:0002250]; alpha-beta T cell activation [GO:0046631]; antibacterial humoral response [GO:0019731]; complement activation, classical pathway [GO:0006958]; T cell receptor signaling pathway [GO:0050852]

alpha-beta T cell receptor complex [GO:0042105]; blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]

antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]

PF07654;

2.60.40.10;

SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20452950}.

FUNCTION: Constant region of T cell receptor (TR) beta chain (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). {ECO:0000303|PubMed:15040585, ECO:0000303|PubMed:23524462, ECO:0000303|PubMed:24600447, ECO:0000303|PubMed:25493333}.

Homo sapiens (Human)

A0A5C2A2T2

COP1_CONPU

MKLLAPVLWAMAALGVTWLVAVDSKESCTKHSNGCSTPLRLPCQEYFRPACDIHDNCYHCGTIFGISRKECDDAFLKDMNTLCKKLGSNSATCPARGKREVTSHRATSIAHSRLWKTALDQKSFLNRKARQAILLTPNSCLYWANNFYMAVHVFGARSYSRTTDPKDCQGLKHCLPNH

3.1.1.4

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:30765458};

arachidonic acid secretion [GO:0050482]; phospholipid metabolic process [GO:0006644]

extracellular region [GO:0005576]

phospholipase A2 activity [GO:0004623]; toxin activity [GO:0090729]

1.20.90.10;

Phospholipase A2 family, Group IX subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30765458}.

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:30765458};

FUNCTION: Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:30765458}.

Conus purpurascens (Purple cone)

A0A5E4M3Q4

SYD9_CAEEL

MSVCVSPLVQATILMTEESLTCPQCPKSFSSTKLLQQHQQMFHTDKSVLLSLKSTDAPVGMDRAFICETCGKAFRFRSNLAEHRSVHTALKPYVCKFCGKSSRLKGNLTKHILKHHKKEQNEAIAKDDIIVKKAPKIVTKDNGPTTNGSTPTTSTATPSVITVSSALASSNGHNNNNNNHAVNNNLRTIKMELEDPDYNLIAKSAPTPVVSKIVATHTVTPRSRPTPKDIKEILETIAPSVGVSETPEEMCLLPKDASSESDRSVLISLGFDFGSTLSLNHQQLQQVVRELKGELSISPDTVQSDHSDDFEQDSPPPMAIANISTVGGEATLAAMIVAATNASGQRGDGTPDSTDTQKGCSPQRELSPESDPSTSSGDSCPSPPKMLHCKECGTLVRKSSHLPIHMTMSHGYPPPLVAAPVEEKPAPEQPVNASSLHNELRVISNAICELKAQQAATPRVEQALTYIDSRVGKLERSLETALNSIYTLVQLQTGMTSSVNRLREDSTKNFSDLKTRMEMSLSPIKPFQQRFSRERSSSSSVERSPSRERSRSPL

regulation of transcription by RNA polymerase II [GO:0006357]

nuclear speck [GO:0016607]; nucleus [GO:0005634]

DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]

PF00096;

3.30.160.60;

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16803962}. Nucleus speckle {ECO:0000269|PubMed:16803962}.

FUNCTION: Plays a role in regulating synaptic function, probably by modulation of endocytosis (PubMed:16803962). May be dispensable in muscle for normal locomotion (PubMed:16803962). May be involved in post-transcriptional mRNA processing, in parallel with unc-75 (PubMed:16803962). {ECO:0000269|PubMed:16803962, ECO:0000303|PubMed:16803962}.

Caenorhabditis elegans

A0A5F8MPU3

CTSRT_MOUSE

MELPPPGNRRVSINNPQETSGRVPTTSAGFPTQSSKISLKRSTYAYRPSMMSNRSSGGQSLLPSSILQKTSLNPPGSLQSKPSNLSSVHYADEEGKPLTDKNKDKDKGRGKGKGTGTRLLTMLRKTLQGSQSDEMAIANQTPNLIPFGDVVGCLAIHIKSCRQFSQRFLGQQRFNLFMRVSINNIVKCTKIRHLKAVNNEKNLVLRFGEMKYFSVQVPRRQDDERNFIYLELMHDGGDPESPPIPLGGAESHLYEVIQKGCFTEVMHLMHKNSSICRVEVEFMFSYGNFGYGFSHQLKPLQKAIEPSMFMNIAPPPERTDPVTNVITPQRVEYPAFLSPEFNVSIGVPEASHATVVQLEKLREKPRERLERMKEEYKNMSTWIEKADYLRNLINPKMTKRDNKGSSIPSESNSSALEELERTTYDIHHRKYEAISNEYGDKEGRVIPVLKVLDQNYSEVFLPKSSDSTPLEDVLLPPIHSLQIVEENEMPHLPKTSEPEDRPHEERKSIVFSSDEELMPKHPSILKISSSQQENRRKMEKSPHFSDVLIIPDKPFEDLNTNKKGRPPIELRKSWERHPTDVACSLRKVAFAQKDYTIPVCKAETTEFKPKHQFQKLSKSGLDPFLRNINSKMSFRKKKDHDDGYRNLSTSSAEILEHEDQDPPYPGHSGSAGSDATWAENPSPVTVQMVNRDSLPPDLITATIVISDRKNKLSLDSVFNSANSLNTKSIFASDNPVVSLTKLSDSDNKLITDSSFNTTKPSNRRLSKDSNFNTTKPSDRKLSSDPSSNTTKPSDTKLFSDPSSNKLSQGPSSNASQLSGSNRLSHNPSINGNKSSYTSDLNKVSRDPSIVSTISSDPNKLSRDPSFVLAKSSDPNKLSHYPSIISAKSSDPNKLSHDPSFVSARSSDPNKLSHDPSIISARSSDPIKLSRDPSFVSARSSDPNKLSHDPSIISARSSDPNKLSRDPSINSTKLSDPSKLSRDPSIFSTKSSDPNKLYRVPSIISGMSSNPKLSRDPSIISGMSSDPKLSRDPSIISAKSSDPNKLSHDPSIISGMSSNPNKLSHDPSIISMKLSDMSKLSRESSINASKSSDTNQLSYDPNIISAKSLDSNNSSASSSPTVNSDTTTNAAEPSGTKNMLDPVVSTIDSSDKQSKLEWLPNVQGASSVTENINTHRSSNSVNFTSDIDILKQSIVLKSILSKNLQDLSDELFSKSELYTNDEGYSPPPSVHSRPSDSTDDRVLGKVQDLNSWRSSKDLLNSQVLLSPVVKNSPQDLLPEGEPGKSSDIEDYVSEKLLEAAGRNFPMNRKSSFKKKHLVSEESSSEHVLSGSIYEYVIKQIFTAPIFSQLGIGIKSSSEARMDSQNQLLTPWERSVTSHIINYEEKDSDVNLSQSKSIISQIIQSFPVNTLLESGVIKVIELDKEHQNSLLDSQTTSSTEQYSDSRSQIKLLSRQNTSSINPLDSSVSGAEYTEDCQSISTQESKYPVRDTKSDSPNDTEEMELDSNLESSSSSLDKVKDTDTAKLKNILKNIFSIFFKYNQSERRQQPEKDSESLIKHSSSSGSEHLEKTQENFNKADKKVDRKPILNPKLRMFLEKLSETEVKNLKSELSKHIQHYLVERLTESGHITKEDLPTIYHKLYLMNEKVELKEQTPFQEKYSETVKEIMSFVNNFNHHFIDKHLETKLRGFLSEILQNYFLKNLSVSNLFNETDAMALHASMSPVRSKSELGQDIADGNFGSSLKINMQYPVTKSLQHYLQDLSENELLSLKTDLSKYLQVLFIEKLYKSGLVSERQLKGISQEIISLHSPSIPLKHIKTNLPFRNESYFMREDSEEQMKYLKNGQNAALHVLLKDKCGETELSRKKERESSFSQILKENLPAIWEQKNIYTREEETLNLIQMQSFLNKNNQANPLTRSPERPSDISLKKQKKDHGFMQFTQVEGSVYKTEIQDPYSWDSRSKTIQSKPCLEKTLKMKLLDKRENNNFYKLTAQEKLDTEFSSYLKLPNCKIPKEKEPISRLSFPTWKTNTFIHVKPEIGEQSKLDHYYQRLKGNNNNNKKHLVTFAQFKNEMETLYRNPYEACNEKRAKISESQSFKYKEKEKSSRPFFFPEVLKRENTKSKRKERDHATKPKKSFHKIVRLLPATLPTTRPHLRKSAPRNLLHWTARRTIHDCLDRFDDLHAPTVKCPKKSKSGARLLGKSPEDSHNQAKHCARPYTAPEPNKRRESAAWKFASPRMVSAGLLHLYVTPAYGIRKVRSKRKLKEDIEKRPLISEIIQMLDNAE

flagellated sperm motility [GO:0030317]; sperm capacitation [GO:0048240]; spermatogenesis [GO:0007283]; vesicle-mediated transport to the plasma membrane [GO:0098876]

CatSper complex [GO:0036128]; sperm principal piece [GO:0097228]

PF15729;

SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:34998468}. Note=Specifically located in the principal piece of the sperm tail. {ECO:0000269|PubMed:34998468}.

FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CatSper complex targeting and trafficking into the quadrilinear nanodomains. Targets the preassembled CatSper complexes to elongating flagella, where it links the channel-carrying vesicles and motor proteins. {ECO:0000269|PubMed:34998468}.

Mus musculus (Mouse)

A0A5K1K8H0

CDPK5_PLAF7

MKETEVEDMDTNRKDGKIKKKEKIVNMKNEEVKSTTKSTLADSDEDYSIITLCTKCLSKKLEDNKNRIILDSKAFKDNRLKGRCSVSSNEDPLDNKLNLSPYFDRSQIIQEIILMNNDELSDVYEIDRYKLGKGSYGNVVKAVSKRTGQQRAIKIIEKKKIHNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCDGGELFDKIVKYGSFSEYEAYKIMKQIFSALYYCHSKNIMHRDLKPENILYVDNTEDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILRGKYDKRCDIWSSGVIMYILLCGYPPFNGKNNDEILKKVEKGEFVFDSNYWARVSDDAKDLICQCLNYNYKERIDVEQVLKHRWFKKFKSNNLIINKTLNKTLIEKFKEFHKLCKIKKLAVTCIAYQLNEKDIGKLKKTFEAFDHNGDGVLTISEIFQCLKVNDNEFDRELYFLLKQLDTDGNGLIDYTEFLAACLDHSIFQQDVICRNAFNVFDLDGDGVITKDELFKILSFSAVQVSFSKEIIENLIKEVDSNNDGFIDYDEFYKMMTGVKE

2.7.11.1

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20466936};

intracellular signal transduction [GO:0035556]; positive regulation of regulated secretory pathway [GO:1903307]; protein phosphorylation [GO:0006468]

cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; extrinsic component of membrane [GO:0019898]; microneme membrane [GO:0033163]; nucleus [GO:0005634]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]; protein serine kinase activity [GO:0106310]

PF13499;PF00069;

1.10.238.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily

PTM: May be palmitoylated. {ECO:0000303|PubMed:12368867}.; PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:20466936}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29487234}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:29487234}; Peripheral membrane protein {ECO:0000269|PubMed:29487234}; Cytoplasmic side {ECO:0000269|PubMed:29487234}. Cell membrane {ECO:0000269|PubMed:20466936, ECO:0000269|PubMed:29487234, ECO:0000269|PubMed:31915223}; Peripheral membrane protein {ECO:0000303|PubMed:20466936}; Cytoplasmic side {ECO:0000305}. Note=During the late stages of schizogony, localizes to the cytoplasm in immature daughter merozoites, co-localizes with AMA1 to a subset of micronemes and to the apical region in maturing daughter merozoites, and near the plasma membrane in mature daughter and free merozoites. {ECO:0000269|PubMed:29487234}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20466936, ECO:0000269|PubMed:31915223}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20466936, ECO:0000269|PubMed:31915223};

FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (PubMed:20466936, PubMed:31915223). Plays a central role in host erythrocytes and hepatocytes infection cycles (PubMed:20466936, PubMed:29487234). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK4 (By similarity). Involved in merosome egress from host hepatocytes, probably together with CDPK4 (By similarity). Required for the release of hepatic merozoites from merosomes in the host blood stream (By similarity). During the asexual blood stage, required for merozoite egress from host erythrocytes by triggering microneme secretion (PubMed:20466936, PubMed:29487234). Phosphorylates transporter NPT1 at late schizont stage (PubMed:31915223). {ECO:0000250|UniProtKB:A0A509AQE6, ECO:0000269|PubMed:20466936, ECO:0000269|PubMed:29487234, ECO:0000269|PubMed:31915223}.

Plasmodium falciparum (isolate 3D7)

A0A5K7RLP0

MEIOS_MOUSE

MLGSDKFSCFSDQHRARSPSPTDRKDKKNHTNKLRELALLIPVTMKTRDKKYTKKEILLRVLHYIQYLQRNIDMTKALLKLHSSNGKGRFVGPGLNPSAGQTQQQHSTPSSSQKPSLWSTSSKPRKKKFTRVSEHPSWPYNPRRSLALDQAENPNTIHPGLKEENEECATYPGVLSPSTYPTTEPSVSEGDGQGAQLVFLDMAQNIFAYDILSDHAVEVQGGEPNADIKVQRSFFLTRAQPCVSSCRQKLFLCTSSEADKEAPDSDPWLPVWTSEDSPNGSPLALGSSQINTWHVADYLNEILGVSSSLFSSPSKILPDHVLEDGTYFLTEGLLESSPATCEVESPQEKEVSSEGPTGPPNFQSSVSLDHCYLSLSENVKVLSNCGSSSESTDTESLWGQEEVRGVATYPRRTGVFSLAQPSVLQQANPEGLQTSSDEDRDYTWTPTGQSSGLPVASKKIKKVQASQGPVKPKDSRKACPGQVKKKCVNGFIMFCRMNRKQYIRACPGTASTAATKDLAQLWRGMTLEEKKPYCTKARRFSRQNNRIVKQENSSSEDDDGETPKPFYQLLAEKAQVSLGLTSLPTPNCQ

activation of meiosis [GO:0090427]; cellular response to retinoic acid [GO:0071300]; meiotic cell cycle [GO:0051321]; oogenesis [GO:0048477]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]

nucleus [GO:0005634]

DNA binding [GO:0003677]; protein dimerization activity [GO:0046983]

PF00505;

1.10.30.10;

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32032549}.

FUNCTION: Gatekeeper of meiotic initiation in both male and female germ cells (PubMed:32032549). In complex with STRA8, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis. Temporal expression of MEIOSIN is required for meiotic entry decision (PubMed:32032549). {ECO:0000269|PubMed:32032549}.

Mus musculus (Mouse)

A0A5P3XKQ1

PMP1_PARBF

MLQIRVFNYNDPIDGENIVELRYHNRSPVKAFQIVDGIWIIPERYNFTNDTKKVPDDRALTILEDEVFAVRENDYLTTDVNEKNSFLNNITKLFKRINSSNIGNQLLNYISTSVPYPVVSTNSIKARDYNTIKFDSIDGRRITKSANVLIYGPSMKNLLDKQTRAINGEEAKNGIGCLSDIIFSPNYLSVQTVSSSRFVEDPASSLTHELIHALHNLYGIQYPGEEKFKFGGFIDKLLGTRECIDYEEVLTYGGKDSEIIRKKIDKSLYPDDFVNKYGEMYKRIKGSNPYYPDEKKLKQSFLNRMNPFDQNGTFDTKEFKNHLMDLWFGLNESEFAKEKKILVRKHYITKQINPKYTELTNDVYTEDKGFVNGQSIDNQNFKIIDDLISKKVKLCSITSKNRVNICIDVNKEDLYFISDKEGFENIDFSEPEIRYDSNVTTATTSSFTDHFLVNRTFNDSDRFPPVELEYAIEPAEIVDNTIMPDIDQKSEISLDNLTTFHYLNAQKMDLGFDSSKEQLKMVTSIEESLLDSKKVYTPFTRTAHSVNERISGIAESYLFYQWLKTVINDFTDELNQKSNTDKVADISWIIPYVGPALNIGLDLSHGDFTKAFEDLGVSILFAIAPEFATISLVALSIYENIEEDSQKEKVINKVENTLARRIEKWHQVYAFMVAQWWGMVHTQIDTRIHQMYESLSHQIIAIKANMEYQLSHYKGPDNDKLLLKDYIYEAEIALNTSANRAMKNIERFMIESSISYLKNNLIPSVVENLKKFDADTKKNLDQFIDKNSSVLGSDLHILKSQVDLELNPTTKVAFNIQSIPDFDINALIDRLGIQLKDNLVFSLGVESDKIKDLSGNNTNLEVKTGVQIVDGRDSKTIRLNSNENSSIIVQKNESINFSYFSDFTISFWIRVPRLNKNDFIDLGIEYDLVNNMDNQGWKISLKDGNLVWRMKDRFGKIIDIITSLTFSNSFIDKYISSNIWRHITITVNQLKDCTLYINGDKIDSKSINELRGIDNNSPIIFKLEGNRNKNQFIRLDQFNIYQRALNESEVEMLFNSYFNSNILRDFWGEPLEYNKSYYMINQAILGGPLRSTYKSWYGEYYPYISRMRTFNVSSFILIPYLYHKGSDVEKVKIINKNNVDKYVRKNDVADVKFENYGNLILTLPMYSKIKERYMVLNEGRNGDLKLIQLQSNDKYYCQIRIFEMYRNGLLSIADDENWLYSSGWYLYSSGWYLDNYKTLDLKKHTKTNWYFVSEDEGWKE

3.4.24.69

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P0DPI0};

proteolysis [GO:0006508]

extracellular region [GO:0005576]

metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270]

PF01742;PF07953;PF07952;

2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10;

Peptidase M27 family

CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000269|PubMed:31253776};

FUNCTION: [Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice. {ECO:0000269|PubMed:31253776}.; FUNCTION: [Paraclostridial mosquitocidal protein 1 light chain]: Neurotoxin that cleaves A.gambiae syntaxin 1a, probably hydrolyzing the '240-Glu-|-His-241' bond. Does not cleave A.gambiae n-synaptobrevin or SNAP-25, nor human syntaxin 1A. {ECO:0000269|PubMed:31253776}.; FUNCTION: [Paraclostridial mosquitocidal protein 1 heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of PMP1 light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD), called HCN and HCC. {ECO:0000250|UniProtKB:P0DPI0}.

Paraclostridium bifermentans (Clostridium bifermentans)

A0A5R8T042

BLC15_ECO25

MVKKSLRQFTLMATATVTLLLGSVPLYAQTADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAAAAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAALQYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDPRDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPASWVVGDKTGSGGYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVLASAAKIVTDGL

3.5.2.6

beta-lactam antibiotic catabolic process [GO:0030655]; response to antibiotic [GO:0046677]

beta-lactamase activity [GO:0008800]

PF13354;

3.40.710.10;

Class-A beta-lactamase family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34310213}. Note=Type I secretion system (T1SS) probably involved in secretion process. {ECO:0000269|PubMed:34310213}.

CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:28069651, ECO:0000269|PubMed:29941650, ECO:0000269|PubMed:35515906, ECO:0000269|PubMed:35563620};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42 uM for amoxicillin (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:29941650}; KM=19 uM for amoxicillin (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:28069651}; KM=197 uM for ampicillin (at pH 7.4) {ECO:0000269|PubMed:35563620}; KM=141 uM for desfuroylceftiofur (at pH 7.4) {ECO:0000269|PubMed:35563620}; KM=77 uM for cefalotin (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:29941650}; KM=200 uM for ceftazidime (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:29941650}; KM=600 uM for ceftazidime (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:28069651}; KM=24 uM for cefotaxime (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:29941650}; KM=324 uM for cefotaxime (at pH 7.4) {ECO:0000269|PubMed:35515906}; KM=66 uM for nitrocefin (at pH 7.4) {ECO:0000269|PubMed:35515906}; KM=47 uM for nitrocefin (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:28069651}; KM=1047 uM for nitrocefin (at pH 7.4) {ECO:0000269|PubMed:35563620}; KM=51 uM for ceftaroline(at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:28069651}; KM=150 uM for aztreonam (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:28069651}; KM=330 uM for ceftiofur (at pH 7.4) {ECO:0000269|PubMed:35563620}; Note=kcat is 47 sec(-1) with amoxicillin as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:29941650). kcat is 40 sec(-1) with amoxicillin as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:28069651). kcat is 101 sec(-1) with ampicillin as substrate (at pH 7.4) (PubMed:35563620). kcat is 2200 sec(-1) with cefalotin as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:29941650). kcat is 1.8 sec(-1) with ceftazidime as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:29941650). kcat is 1.4 sec(-1) with ceftazidime as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:28069651). kcat is 110 sec(-1) with cefotaxime as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:29941650). kcat is 12,820 sec(-1) with cefotaxime as substrate (at pH 7.4) (PubMed:35515906). kcat is 6,172 sec(-1) with nitrocefin as substrate (at pH 7.4) (PubMed:35515906). kcat is 338.3 sec(-1) with nitrocefin as substrate (at pH 7.4) (PubMed:35563620). kcat is 90 sec(-1) with ceftaroline as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:28069651). kcat is 1.2 sec(-1) with ceftaroline as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:28069651). kcat is 313.7 sec(-1) with ceftiofur as substrate (at pH 7.4) (PubMed:35563620). kcat is 489.8 sec(-1) with desfuroylceftiofur as substrate (at pH 7.4) (PubMed:35563620). {ECO:0000269|PubMed:28069651, ECO:0000269|PubMed:29941650, ECO:0000269|PubMed:35515906, ECO:0000269|PubMed:35563620};

FUNCTION: Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, third and fourth-generation cephalosporins (PubMed:11470367, PubMed:28069651, PubMed:29941650, PubMed:34310213, PubMed:35515906, PubMed:35563620). Has cefotaxime- and ceftazidime-hydrolyzing activity (PubMed:28069651, PubMed:29941650, PubMed:35515906). Inactive against the carbapenem antibiotics, imipenem, meropenem and ertapenem (PubMed:11470367, PubMed:29941650). {ECO:0000269|PubMed:11470367, ECO:0000269|PubMed:28069651, ECO:0000269|PubMed:29941650, ECO:0000269|PubMed:34310213, ECO:0000269|PubMed:35515906, ECO:0000269|PubMed:35563620}.

Escherichia coli O25b:H4

A0A5S9I252

TATC6_HYPAT

MGQPTTTSLFMRDVMFHRMTGTSQAVNDVATLSGERREIIRRALNKKILVPNILELMPAWPSEFQPNIDEVNVEIDEWLKTVNVAKEKKLKHRARGNYTLLAGIYYPHCRKEKMLALSQFLYWIFFWDDEIDTGGELTEDREGTILCCAETNKCINDCLGPEPNYTPPPGSRGTVEMLYPILRDLRAGLSPVSTMRLKQELHDYVNGVKNQQKVRQEDHLPNPWDHFQMRVDDVGVIPSITQNEYAMDFTLPDWIRRHEAMEEIVLQCTKLTILLNEILSLQKEFRVSQLENLCLLFMNTYDMSIEQSIHKVLGLLKDHYKICIEAEARLPWSTTDEKLNNNIREYIRGCQRLATGTACWSYNCERYFKLSQLNDQQELLLDLSRT

4.2.3.-; 4.2.3.104; 4.2.3.137; 4.2.3.157; 4.2.3.182; 4.2.3.57

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UR08}; Note=Binds 3 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:Q9UR08};

(-)-E-beta-caryophyllene synthase activity [GO:0080016]; alpha-humulene synthase activity [GO:0080017]; metal ion binding [GO:0046872]

PF19086;

1.10.600.10;

Terpene synthase family

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + trichobrasilenol; Xref=Rhea:RHEA:66644, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:167379, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66645; Evidence={ECO:0000269|PubMed:31418991}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence={ECO:0000269|PubMed:31418991}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|PubMed:31418991}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-2-epi-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:34703, ChEBI:CHEBI:33019, ChEBI:CHEBI:68667, ChEBI:CHEBI:175763; EC=4.2.3.137; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34704; Evidence={ECO:0000269|PubMed:31418991}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-isoafricanol + diphosphate; Xref=Rhea:RHEA:53616, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:137522, ChEBI:CHEBI:175763; EC=4.2.3.157; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53617; Evidence={ECO:0000269|PubMed:31418991}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-(2S,3R,9R)-pristinol + diphosphate; Xref=Rhea:RHEA:54372, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:138165, ChEBI:CHEBI:175763; EC=4.2.3.182; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54373; Evidence={ECO:0000269|PubMed:31418991}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = african-3-ene + diphosphate; Xref=Rhea:RHEA:66648, ChEBI:CHEBI:33019, ChEBI:CHEBI:167380, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66649; Evidence={ECO:0000269|PubMed:31418991}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = african-1-ene + diphosphate; Xref=Rhea:RHEA:66652, ChEBI:CHEBI:33019, ChEBI:CHEBI:167381, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66653; Evidence={ECO:0000269|PubMed:31418991};

PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:31418991}.

FUNCTION: Terpene cyclase that is able to convert FPP into a mixture of sesquiterpene hydrocarbons and alcohols (PubMed:31418991). The main product is trichobrasilenol (PubMed:31418991). Additionally, side products include alpha-humulene, caryophyllene, 2-epi-caryophyllene, african-3-ene, african-1-ene, isoafricanol and pristinol (PubMed:31418991). Does not accept GPP, GGPP, and GFPP as substrates (PubMed:31418991). {ECO:0000269|PubMed:31418991}.

Hypocrea atroviridis (Trichoderma atroviride)

A0A5S9MMK5

FPEB1_CAEEL

MMTTTVQKNCWRLDQTMLGLEKPGSSDISSSSTDTSAISPISVSSMPLSPDKEKKKISFVRYNPDIPQIVTSFKGYQKLMYQGYRYNIYQIAPERNFKSWRCVCAKKMHDGQWCKCRAETTMDNKNACTKGSHNHPPRHHVAEIEFIKSQLYSAALENPDHDAGDLVNQASMYLSDGVMFDNKESIKKSLVVARNKDGKPKKPRSKRMMKFEVDDDDENEYKMPKLETDISCFLPFINNMVKVEPPFSHTPTIQIPQPIPTPIQHQQQEQSNLLQPATLNGMNNPWMGMEDHLAMIWAANAMLNPGLDVLSTIAALSKHQQHVQGPSPQQAATAPTTASLSSNLSVSSFTPQMPKEASIAIPAPLQVLNLKDLKPLPPLANIQTSPVIQAANLLLPVAALKKDSSTQTTEEIKVSQCLTSGCGCRVIRICCCDEGVCRRTAAC

negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]

nucleus [GO:0005634]

metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]

PF04500;

2.20.25.240;

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11203704, ECO:0000269|PubMed:15165844}. Note=Localization to nucleus dependent, in part, on FLYWCH-type domain. {ECO:0000269|PubMed:15165844}.

FUNCTION: Putative transcription factor (PubMed:11203704). Binds to specific sequence motif 5'-[TC][AGT]TGCC[GA][AT]-3' in regulatory elements of target genes such as myosin myo-2 (PubMed:11203704, PubMed:15165844). May modulate gene expression, perhaps acting in opposition to transcription factor pha-4 (PubMed:11203704, PubMed:12095247). Involved in morphogenesis, perhaps especially in formation of the pharynx (PubMed:11203704, PubMed:15581870). Plays roles in molting, feeding and morphology (PubMed:15581870). {ECO:0000269|PubMed:11203704, ECO:0000269|PubMed:12095247, ECO:0000269|PubMed:15165844, ECO:0000269|PubMed:15581870}.

Caenorhabditis elegans

A0A644F0Y1

TBG_GIAIC

MPREVITIQCGQCGNQIGEVFWNRLCTEHGINPDGTLRPEAYTFNDRKDVFFYQSDDEHYVPRAILLDTEPGVISHIRNGPIKELINPENVYIDSTGGGAGNIWTKGFQCGEAGFEKIVEIIDREADGADSLAGFSLTHSIAGGTGSGMGSFLLDRLSDRYPKALLQTYSVFPNTTADIIVQPYNSILTLQRLALCADAVVVLDNTALDRIITNHIPNELLTNPFEHVNSLVSTVMAASTSTLRLPGFMSNDLLSLVSSLVPTPRLHFLMSSYTPITSSSLNVKEHTKDQEAGSGAVAGAAAGATRRQVHTDSIVQLVKRLLHPTNGMVSCGRDGKYISLLNIVQGEAESNQLYKSLQQIKEGRDVKFIDWGPSNMQMALSKRSPFTNEAHKVSGLMLANHTAIRKIFDNINNTFTQLFSKRAYLQNYIDSMVTGGEPEILEQFTDAQAVCTSLSKEYEAAESKDYLEYIGM

cytoplasmic microtubule organization [GO:0031122]; meiotic spindle organization [GO:0000212]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle organization [GO:0007052]

centrosome [GO:0005813]; cytoplasm [GO:0005737]; gamma-tubulin complex [GO:0000930]; microtubule [GO:0005874]; motile cilium [GO:0031514]; nucleus [GO:0005634]; spindle [GO:0005819]

GTP binding [GO:0005525]; structural constituent of cytoskeleton [GO:0005200]

PF00091;PF03953;

1.10.287.600;3.30.1330.20;3.40.50.1440;

Tubulin family

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:30318753}. Note=Localizes mainly to basal bodies of trophozoites during interface (PubMed:30318753). Localizes as four dots at the basis of posterolateral and ventral flagellar pairs in interphase (PubMed:10928459). Localizes also to axonemes and median body in over half of the interphase cells (PubMed:30318753). Colocalizes with microtubules in the median bodies of the interphase cells (PubMed:30318753). Localizes to basal bodies and median bodies in dividing stages of the trophozoites (PubMed:30318753). The four dots are absent in late prophase and early metaphase, but reappear as tiny dots at the perikinetosomal areas of the separated parent flagella in anaphase (PubMed:10928459). Localizes transiently to the centers of the mitotic spindles in anaphase (PubMed:30318753). The four dots localize at the basal body regions of each daughter karyomastigont in telophase (PubMed:10928459). Colocalizes with centrin outside the two nuclei in telophase (PubMed:30318753). Localizes to basal bodies and axonemes of the two daughter cells during cytokinesis (PubMed:30318753). Does not localize at the spindle poles of the dividing nuclei (PubMed:10928459). {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}.

FUNCTION: Tubulin is the major constituent of microtubules (Potential). The gamma chain is found at microtubule organizing centers (MTOC) such as the centrosome (PubMed:30318753). Component of the gamma-tubulin small complex (gamma-TuSC) involved in microtubule nucleation for the formation of median bodies and in the biogenesis of flagella (PubMed:30318753). Gamma-TuSC may be required for the correct positioning of EB1 within the trophozoites (PubMed:30318753). {ECO:0000255|RuleBase:RU000352, ECO:0000269|PubMed:30318753}.

Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)

A0A644F649

IFT88_GIAIC

MTQNWRPQSRLQTMTFAGTARPMTSMTAAGFTKNPLATAGVASIFDKLPPEPPKDSPEQKADQMEINIFKLLRDGMSAASCKDYVTALGRIREAIKLEQKVSQHRTMNGLADSINLDLRTCIWMHWAQIQALGGQPEMALSTYEKIVKTAEGATLAQIRFNMGNINHNLGKYNEALKNFRMAIDQASPSLPRFRQKIASHMAQSCIKLHRWQDAVDRIEEYLIKQYTLASSVGTDVERQNFYAMTTRFDPLYTVLIGYYALGVPEKMIDAYSRLIDSSILISDHPDSLEIDDHHNGISSKQIAMADAELCNMSNDDELDDLSRYNATLRHEHTNKLLISARLLAPAIAWEESQGYAKLSDILREKGHHGISLQVQMSMALTLLKRNEFEKATDIMLRIDREGLESALALGINVPLSILQKTRNLSLTAAATAVTNQESDLHLLGIDPSVLANQQSVVDRDAVASRGAPEVDMLKTDDDNGTKKQPYAAFVPRGVHTNIAFIYYLKGDYEASARHAQIALEIDPYDSFAHINLGCTYSKTNQWELSLREFLKAQEINMESVQATYNAGLVYFKQQEYKTAYSCFQKVASKLPSYGDAIYMSADCLARMSQIDEAIQMLSNLVTMFSAVKAYDPSIYIRLGELYSIAGDEGQAAHYFKEAHRLVPFSLAVINWLGSHYIKNELYEQARVCFEKASRVDTTTPKWSLAVAACLRKSKQYRDAIYEYKHILKRFPTNTTAMTHLISSLNNIGQHKEADEWAEKLTKLTNNKVPEVTEDRELDEFVKQERRNSVAAVGPGSRAGQDRFEASNNRVSSNTGDLFGDVDIAEELLTEN

cilium assembly [GO:0060271]; inner ear receptor cell stereocilium organization [GO:0060122]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; kidney development [GO:0001822]; non-motile cilium assembly [GO:1905515]

9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; intraciliary transport particle B [GO:0030992]; non-motile cilium [GO:0097730]

kinesin binding [GO:0019894]

PF13174;PF13181;

1.25.40.10;

SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips. Localizes to the basal bodies. {ECO:0000269|PubMed:31855176}.

FUNCTION: Component of the intraflagellar transport complex B (IFT-B) involved in flagellar assembly (Probable). {ECO:0000305|PubMed:31855176}.

Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)