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Synthyra 5

P37458

MSLMQFSGLLVVWLLSTLFIATLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSVLVFRFDVGVAPPEILLQALLSAACFYGVYYVTYKTRLRKRVVDVPRKPLFTMNRVETHLTWVILMGIALVSVAIFFMHNGFLLFRLHSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISLWMLAAAGVLGIVGMFWLALKRYGLNVSGDEAFYTFLYLTRDTFSPWENLALLLQNYHNIEFQGLAPIVRDFYVFIPTWLWPGRPSIVLNSANYFTWEVLNNHSGLAISPTLIGSLVVMGGALFIPLGAIVVGLIIKWFDWLYELGNREPNRYKAAILHSFCFGAIFNMIVLAREGLDSFVSRVVFFLVVFGASLLVAKLLFWLFDSAGLIHKRTTSLPQAQVEGKL

Function: Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 51647 Sequence Length: 452 Pathway: Bacterial outer membrane biogenesis; enterobacterial common antigen biosynthesis. Subcellular Location: Cell inner membrane

Q46800

MFDFASYHRAATLADAINLLADNPQAKLLAGGTDVLIQLHHHNDRYRHIVDIHNLAELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPRGVRFVPINGFHTGPGKVSLEHDEILVAFHFPPQPKEHAGSAHFKYAMRDAMDISTIGCAAHCRLDNGNFSELRLAFGVAAPTPIRCQHAEQTAQNAPLNLQTLEAISESVLQDVAPRSSWRASKEFRLHLIQTMTKKVISEAVAAAGGKLQ

Function: Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate Sequence Mass (Da): 31557 Sequence Length: 292 Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2. EC: 1.17.1.4

O32145

MNGQVTKARMNIQLWRPAALDEAYSLLEKLAPDVCAASGSTLLQLQWDKGTLPKQHLVSLEGIDEMRGISTSDTHVSIGGLTSLNECRKNPLIKRALSCFSDAASAVAAPGIRSRATIGGNIASKIGDFIPLLLVLGAELIVYQKELIRLPLGAWLSEEDFRTAIVTRVIIPRAEGERVFYHKLGRRQAFTGAAAVAAGRFLKDGSIRLAAGHADITPRRLLDSEAKWMAPGWDPHELYKTLIHELPFSSDVFMSAAYRKKAAANVIMAELMAEGGE

Function: Oxidizes hypoxanthine and xanthine to uric acid. Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate Sequence Mass (Da): 30119 Sequence Length: 277 Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2. EC: 1.17.1.4

Q46801

MNHSETITIECTINGMPFQLHAAPGTPLSELLREQGLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREKPLTITEIRRGLAGNLCRCTGYQMIVNTVLDCEKTK

Cofactor: Binds 2 [2Fe-2S] clusters. Function: Iron-sulfur subunit of the xanthine dehydrogenase complex. Sequence Mass (Da): 16922 Sequence Length: 159 Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2.

O32144

MIINKPSRVRPDGRGKVTGELKYMTDLSFPGMLYGKVLRSAYPHAEIVSVCTIKAEKMEGVQAVVTHKDVPGLNRFGIVIPDQPVLCEDRVRYVGDAIAAVAAETEEIAEAALELIQVEYKELEVMDSPEKALRPNAQRLHEDGNILHRAFFSNGDVEEGFQASDTVFEETYELPRQMHTYMETEGGVAVPEDDGGFTMYAGTQHGYKDRFQLARIFDIPEEKIRIVSSPMGGSFGGKDELNIQPYAALLALKSGRPVKIHQTRKESVRSGIKRHPMKITIKTGADHSGNLLAHDVKIVADTGAYATLGPAVLDFSVEHAAGPYRIPNIRTEGISVFTNNGVAGEFRGFGGNQITFALETHLDRLSGMLGIDPLELRRKNIRKPHDLGPLEHRIAPTDGAAQVLNAISKSPILKKTSRNCGYLQRGTGAAITMHGGGLGFGRMDAAGGRLSLSSEGKITASFGFEECGQGILAAIEQIVMEELGCAAEDISIVIGDTAKVPKSGSSTASRGTSMVWHAIQRLKKPFLAQLKKRAAEWSGCSAENLIPGAAGLRDKNTKALVVTYKELAEKGPLAEETAFDFPTTPDPVVGGHFLYSFGAAAVEVEVDLLTGDVKLIDCEHAIAAGPVVSPQGYRGQIEGGAAMALGYTLMEEAKMTDGRYAAENLDHYLIPGIKDVPDMKLIAIEDLMKGDVYGPRGVGEIGTIAITPAIVKAVHDAVGCWINKLPISREELLEAIDRKGLKQWT

Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Function: Oxidizes hypoxanthine and xanthine to uric acid. Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate Sequence Mass (Da): 80434 Sequence Length: 745 Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2. EC: 1.17.1.4

Q46814

MIIHFTLNGAPQELTVNPGENVQKLLFNMGMHSVRNSDDGFGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIELAVARKNNPQATIDIAPTFRDDLEVIGKHYPKTDAAKMVQAKPCYVEDRVTADACVIKMLRSPHAHALITHLDVSKAEALPGVVHVITHLNCPDIYYTPGGQSAPEPSPLDRRMFGKKMRHVGDRVAAVVAESEEIALEALKLIDVEYEVLKPVMSIDEAMAEDAPVVHDEPVVYVAGAPDTLEDDNSHAAQRGEHMIINFPIGSRPRKNIAASIHGHIGDMDKGFADADVIIERTYNSTQAQQCPTETHICFTRMDGDRLVIHASTQVPWHLRRQVARLVGMKQHKVHVIKERVGGGFGSKQDILLEEVCAWATCVTGRPVLFRYTREEEFIANTSRHVAKVTVKLGAKKDGRLTAVKMDFRANTGPYGNHSLTVPCNGPALSLPLYPCDNVDFQVTTYYSNICPNGAYQGYGAPKGNFAITMALAELAEQLQIDQLEIIERNRVHEGQELKILGAIGEGKAPTSVPSAASCALEEILRQGREMIQWSSPKPQNGDWHIGRGVAIIMQKSGIPDIDQANCMIKLESDGTFIVHSGGADIGTGLDTVVTKLAAEVLHCPPQDVHVISGDTDHALFDKGAYASSGTCFSGNAARLAAENLREKILFHGAQMLGEPVADVQLATPGVVRGKKGEVSFGDIAHKGETGTGFGSLVGTGSYITPDFAFPYGANFAEVAVNTRTGEIRLDKFYALLDCGTPVNPELALGQIYGATLRAIGHSMSEEIIYDAEGHPLTRDLRSYGAPKIGDIPRDFRAVLVPSDDKVGPFGAKSISEIGVNGAAPAIATAIHDACGIWLREWHFTPEKILTALEKI

Cofactor: Binds 2 [2Fe-2S] centers. Function: Probably has no xanthine dehydrogenase activity; however deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage. Sequence Mass (Da): 103519 Sequence Length: 956 EC: 1.-.-.-

O32143

MDIKEAGPFPVKKEQFRMTVNGQAWEVAAVPTTHLSDLLRKEFQLTGTKVSCGIGRCGACSILIDGKLANACMTMAYQADGHSITTIEGLQKEELDMCQTAFLEEGGFQCGYCTPGMIIALKALFRETPQPSDKDIEEGLAGNLCRCTGYGGIMRSACRIRRELNGGRRESGF

Cofactor: Binds 2 [2Fe-2S] clusters. Function: Oxidizes hypoxanthine and xanthine to uric acid. Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate Sequence Mass (Da): 18838 Sequence Length: 173 Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2. EC: 1.17.1.4

Q9A9Z0

MSSAIYPSLKGKRVVITGGGSGIGAGLTAGFARQGAEVIFLDIADEDSRALEAELAGSPIPPVYKRCDLMNLEAIKAVFAEIGDVDVLVNNAGNDDRHKLADVTGAYWDERINVNLRHMLFCTQAVAPGMKKRGGGAVINFGSISWHLGLEDLVLYETAKAGIEGMTRALARELGPDDIRVTCVVPGNVKTKRQEKWYTPEGEAQIVAAQCLKGRIVPENVAALVLFLASDDASLCTGHEYWIDAGWR

Function: Involved in the degradation of D-xylose . Catalyzes the initial reaction in the xylose utilization pathway by oxydizing D-xylose into D-xylonolactone . Shows some activity with L-arabinose and D-lyxose, but D-xylose is clearly the best substrate . Has no activity with D-ribose, D-glucose, D-galactose or D-mannose . Catalytic Activity: D-xylose + NAD(+) = D-xylono-1,5-lactone + H(+) + NADH Sequence Mass (Da): 26641 Sequence Length: 248 EC: 1.1.1.175

Q9AEM9

MTNPVIGTPWQKLDRPVSEEAIEGMDKYWRVANYMSIGQIYLRSNPLMKEPFTRDDVKHRLVGHWGTTPGLNFLLAHINRLIADHQQNTVFIMGPGHGGPAGTAQSYIDGTYTEYYPNITKDEAGLQKFFRQFSYPGGIPSHFAPETPGSIHEGGELGYALSHAYGAIMDNPSLFVPCIIGDGEAETGPLATGWQSNKLVNPRTDGIVLPILHLNGYKIANPTILARISDEELHDFFRGMGYHPYEFVAGFDNEDHLSIHRRFAELFETIFDEICDIKAAAQTDDMTRPFYPMLIFRTPKGWTCPKFIDGKKTEGSWRAHQVPLASARDTEAHFEVLKGWMESYKPEELFNADGSIKEDVTAFMPKGELRIGANPNANGGRIREDLKLPELDQYEITGVKEYGHGWGQVEAPRSLGAYCRDIIKNNPDSFRVFGPDETASNRLNATYEVTKKQWDNGYLSALVDENMAVTGQVVEQLSEHQCEGFLEAYLLTGRHGIWSSYESFVHVIDSMLNQHAKWLEATVREIPWRKPISSVNLLVSSHVWRQDHNGFSHQDPGVTSVLLNKTFNNDHVTNIYFATDANMLLAIAEKCFKSTNKINAIFAGKQPAATWITLDEVRAELEAGAAEWKWASNAKSNDEVQVVLAAAGDVPTQEIMAASDALNKMGIKFKVVNVVDLIKLQSSKENDEAMSDEDFADLFTADKPVLFAYHSYAQDVRGLIYDRPNHDNFTVVGYKEQGSTTTPFDMVRVNDMDRYALQAKALELIDADKYADKINELNEFRKTAFQFAVDNGYDIPEFTDWVYPDVKVDETSMLSATAATAGDNE

Function: Phosphoketolase using both fructose 6-phosphate and xylulose 5-phosphate as substrate. Catalytic Activity: D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O Sequence Mass (Da): 92530 Sequence Length: 825 EC: 4.1.2.22

Q8VXZ5

MVEGWRNGFRDATNSKPLFVTIYATVIIGVLVSSFYVFSAIYSPTNGSSSFLSFPPLSTSGRIHSLPQENATLELPVAPPPPPQALPPPVLEEAQGNSLGKIWVSPPRDKKMPPLETFKLTKELFGERVKDNVIIVTFGNYAFMDFILTWVKHLTDLDLSNILVGAMDTKLLEALYWKGVPVFDMGSHMSTVDVGWGSPTFHKMGREKVILIDSVLPFGYELLMCDTDMVWLKNPMPYLARFPDADVLTSSDQVVPTVIDDSLDIWQQVGAAYNIGIFHWRPTESAKKLAKEWKEILLADDKVWDQNGFNEIVRRQLGPSVEGDSGLFYAYDGNLKVGILPASIFCSGHTYFVQAMYQQLRLEPYAVHTTFQYAGTEGKRHRLREGMVFYDPPEYYDSPGGFIAFKPSIPKSLLLDGKHTIESHFILVNHQMKQIRSALAIASLLNRTLVMPPIWCRLDRLWFGHPGTLQGSMTRQPFICPLDHVFEVNIMLKELPEEEFGPGIGIREYSFLDNPLLPKQVKESWLDVQLCQEGKEGCEASNNTSPSRVLKFPKRSNEDTFKAIFSSFDDVKVIKFSSIEDAFIGFSDKEREERFRRRVKRYVGIWCCEENKTPGHIYYDMYWDEKPGWKPVPPQTPEEDHPPL

Function: Plays a role in the arabinosylation of cell wall components. Involved in the arabinosylation of extensin proteins in root hair cells . Extensins are structural glycoproteins present in cell walls and its arabinosylation is important for cell elongation, root hair cell development, lateral root development and root hair tip growth . Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 73213 Sequence Length: 644 Domain: The conserved DXD motif is involved in enzyme activity. Subcellular Location: Golgi apparatus membrane EC: 2.4.2.-

Q7Z9M8

MKVSRVLALVLGAVIPAHAAFSWKNVKLGGGGGFVPGIIFHPKTKGVAYARTDIGGLYRLNADDSWTAVTDGIADNAGWHNWGIDAVALDPQDDQKVYAAVGMYTNSWDPSNGAIIRSSDRGATWSFTNLPFKVGGNMPGRGAGERLAVDPANSNIIYFGARSGNGLWKSTDGGVTFSKVSSFTATGTYIPDPSDSNGYNSDKQGLMWVTFDSTSSTTGGATSRIFVGTADNITASVYVSTNAGSTWSAVPGQPGKYFPHKAKLQPAEKALYLTYSDGTGPYDGTLGSVWRYDIAGGTWKDITPVSGSDLYFGFGGLGLDLQKPGTLVVASLNSWWPDAQLFRSTDSGTTWSPIWAWASYPTETYYYSISTPKAPWIKNNFIDVTSESPSDGLIKRLGWMIESLEIDPTDSNHWLYGTGMTIFGGHDLTNWDTRHNVSIQSLADGIEEFSVQDLASAPGGSELLAAVGDDNGFTFASRNDLGTSPQTVWATPTWATSTSVDYAGNSVKSVVRVGNTAGTQQVAISSDGGATWSIDYAADTSMNGGTVAYSADGDTILWSTASSGVQRSQFQGSFASVSSLPAGAVIASDKKTNSVFYAGSGSTFYVSKDTGSSFTRGPKLGSAGTIRDIAAHPTTAGTLYVSTDVGIFRSTDSGTTFGQVSTALTNTYQIALGVGSGSNWNLYAFGTGPSGARLYASGDSGASWTDIQGSQGFGSIDSTKVAGSGSTAGQVYVGTNGRGVFYAQGTVGGGTGGTSSSTKQSSSSTSSASSSTTLRSSVVSTTRASTVTSSRTSSAAGPTGSGVAGHYAQCGGIGWTGPTQCVAPYVCQKQNDYYYQCV

Function: Hydrolyzes the glucosidic bonds of unbranched Glc residues in tamarind seed xyloglucan, producing XXXG, XLXG, XXLG and XLLG. Has a low activity against beta-glucan and carboxymethylcellulose. Not active against Avicel, laminarin, xylan, galactomannan, linear and branched arabinans, galactan, polygalacturonic acid, starch, beta-D-Glcp, beta-D-cellobiose, beta-D-Galp, beta-D-Xylp, alpha-D-Xylp, alpha-L-Araf and alpha-L-Arap. Catalytic Activity: Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the newly-formed chain end after endo-initiation on a polymer molecule. Sequence Mass (Da): 87133 Sequence Length: 838 EC: 3.2.1.155

B9HJR7

MGSPFKDHHHHHHPFSLAKKLIPWTFYAMIPLVLFRLYFYPYPLHNITTPILTSSSSSVSSSTPFVAEETSCDYTTGKWVRDKRGPLYNGSACGTIKEGQNCIAHGRPDMGYLYWRWKPKHCKLPRFEPNTFLQLLRNKHLAFVGDSMARNQLESLLCMLSSASAPNLVYRDGDDNKFRRWYFESHNINISVYWSPFLVKGVEKSNTGPNHNQLYLDHVDERWAADMNGIDMIVLSIGHWFLHPAVYYEGDQVLGCHYCPGLNHTEIGFYDVLRKAIKTTLKALIDRKGANSNGINAFVTTFSPAHFEGDWDKLGACPKTKPYKEGDKALEGMDADMRQIEVEEVEAAKMNSTQLEKFRLEALDVTSLSLMRPDGHPGPYMHPFPFANGVTERVQNDCVHWCLPGPIDTWNEILLEVIKKWDYESRREE

Function: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains . Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers . Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 49207 Sequence Length: 429 Subcellular Location: Golgi apparatus membrane EC: 2.3.1.-

B9HVC2

MGSPFKDHHTLHPSLVRKLIPWTFYAMVPLVLFRVYLYPYPLHHTTTTILTSSPVSPPPALLEDETSCDYTDGNWVPDRRDPLYNGSTCGTIKEGQSCIAHGRPDMGYLYWRWKPKQCKLPRFEPNTFLQLLRNKHLAFVGDSMARNQLESLLCMLSSVSPPNLVYRDGEENKFRRWYFESHNFSISVYWSPFLVRGVEKSNTGLNHNQLFLDHVDERWAADMNGIDMVVLSIGHWFLHPAVYYEGDQVLGCHYCPDLNHTEIGFYDILRKAIKTTLKALVDRKGPNDNGFDALVTTFSPAHFEGDWDKLGACPKTEPCKEGEKTLEGMDAEMRQVEVEEVEAAKMNSVQLEKFRLEALDVSKLSLMRPDGHPGPYMHPFPFAYGVAERVQNDCVHWCLPGPIDTWNEILLEVIKKWEYASRREQ

Function: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains . Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers . Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 48943 Sequence Length: 425 Subcellular Location: Golgi apparatus membrane EC: 2.3.1.-

A0A2K1YKA4

MNRFFYTVGLIFLFSFFILYSPKTSDLSNNVDLHQQLLISLQKEEERCDLFSGYWVQDLRGSQYTNVSCSSIPESKNCFMQGRPDAGFSQWRWKPDGCELPRFDPGTFFEIVRGKTMAFIGDSVARNHVESLLCLLSSEEMPLGIYKDTEDRTRTWYFPHSNFTLMVIWTRFLVLDEERVINGSVTGVFDLHLDKMDKNWANKLPEIDYAILSDAHWFFRKNYLYEKGKNIGCIFCGEPGIKSLDIDSALQMVIKVVLNYINNCKKCRNILTVLRTFSPAHFADGAWDTGGSCNRTHPLGEKEIDLASLDWKIRSIQVEEIKRVRPVARRRKKFEVLDVTKAMLMRPDGHPNSYWGNKWMKGYNDCVHWCMPGPIDAWNDFLIALLRRHAFTDFTWS

Function: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains . Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers . Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 46209 Sequence Length: 397 Subcellular Location: Golgi apparatus membrane EC: 2.3.1.-

Q94AA9

MAAPRSRRCSLSLLTLFSITLILISVSLFVSTKPANKPFLDYRNQFSISISISSPLEQNTTNTSFVSASPPLSPLGQSNTTNTILASSSSSSSFSDHQNQNKSPSPTSKKIVIRKRSGLDKIESDLAKARAAIKKAASTQNYVSSLYKNPAAFHQSHTEMMNRFKVWTYTEGEVPLFHDGPVNDIYGIEGQFMDEMCVDGPKSRSRFRADRPENAHVFFIPFSVAKVIHFVYKPITSVEGFSRARLHRLIEDYVDVVATKHPYWNRSQGGDHFMVSCHDWAPDVIDGNPKLFEKFIRGLCNANTSEGFRPNVDVSIPEIYLPKGKLGPSFLGKSPRVRSILAFFAGRSHGEIRKILFQHWKEMDNEVQVYDRLPPGKDYTKTMGMSKFCLCPSGWEVASPREVEAIYAGCVPVIISDNYSLPFSDVLNWDSFSIQIPVSRIKEIKTILQSVSLVRYLKMYKRVLEVKQHFVLNRPAKPYDVMHMMLHSIWLRRLNLRLGT

Function: Involved in pectin biosynthesis. Catalyzes the transfer of xylose from UDP-xylose onto oligogalacturonides and endogenous acceptors. Catalytic Activity: Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a beta-1,3-D-xylosyl-D-galactose linkage. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 56600 Sequence Length: 500 Subcellular Location: Golgi apparatus membrane EC: 2.4.2.41

O94218

MKLSLLSLATLASAASLQRRSDFCGQWDTATAGDFTLYNDLWGESAGTGSQCTGVDSYSGDTIAWHTSWSWSGGSSSVKSYVNAALTFTPTQLNCISSIPTTWKWSYSGSSIVADVAYDTFLAETASGSSKYEIMVWLAALGGAGPISSTGSTIATPTIAGVNWKLYSGPNGDTTVYSFVADSTTESFSGDLNDFFTYLVDNEGVSDELYLTTLEAGTEPFTGSNAKLTVSEYSISIE

Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components. Catalytic Activity: xyloglucan + H2O = xyloglucan oligosaccharides. Sequence Mass (Da): 25159 Sequence Length: 238 Subcellular Location: Secreted EC: 3.2.1.151

A1CRJ0

MKFNLALALSLTVATAEAATELCKQWDSIIEGNFIVYNNLWGQGNADDGGHQCTTVKSISGDTVVWSTEWAWSGGPGQVKSYANAALQFTPTTLSSVSSIDSTWKWRDSYTGSDIVANVAYDMFLSSSATGSEEYEIMVWLAALGGAGPISSTGSPIATPTINGVQWDLYLGPNGAMQVYSFVAPSSTENFAGDMKGFIDYLTSEQGLSKDLYLLDVQAGTEPFSGSDAVLTVSEYSVNLA

Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components (By similarity). Catalytic Activity: xyloglucan + H2O = xyloglucan oligosaccharides. Sequence Mass (Da): 25618 Sequence Length: 241 Subcellular Location: Secreted EC: 3.2.1.151

Q8L794

MLILRQFQISSFELFQSPKQTGFYSSSRSVPLPRTRFYSDFRVMSGNKGTNYEKLYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEESMGWASSWKATLFSLLEDIPVTVRSLVSSISLDGTSATTLILNSESGEVLCQPYLYNQSCPDALPEVKSIAPANHTVCSGTSTLCKLVSWWNTEVPNRESAVLLHQADWLLWLLHGRLGVSDYNNALKVGYDPESESYPSWLLGQPYSQLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYSHRLDDKWLVGGASNTGGAILRQLFSDEQLERLSQEINPMVGSPLDYYPLQSSGERFPIADPNLAPRLLPRPESDVEFLHGILESIARIEGKGYKLLKELGATEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEASYGASLLALKGAKQNSGL

Function: Exhibits ATP hydrolysis without substrate. Can phosphorylate D-ribulose with low efficiency. Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+) Sequence Mass (Da): 52468 Sequence Length: 478 Subcellular Location: Plastid EC: 2.7.1.47

Q949W8

MADLSLPPDSLFLGFDSSTQSMKATVLDSNLNIIKTELVHFDSDLPQYKTKDGVYRDTTVNGRIVSPTLMWVEAFDLILQKLSNANFDFAKVIAVSGSGQQHGSVYWSKGSSEVLRSLDSKRSLKEQLENAFSVKESPIWMDSSTTLQCKEIENAVGGAMELSKITGSRAYERFTGPQIRKLFMTQGEVYKSTERISLVSSFMASLLVGDYACIDETDAAGMNLMDIEKRCWSKAALEATATGLEEKLGKLAPAYATAGSISQYFVQRFGFEKNCVVVQWSGDNPNSLAGLTLSTPGDLAISLGTSDTVFGITKELQPSLEGHVLPNPVDPESYMVMLVYKNASLTREEIRDRCAEGSWDVFNKYLQQTQPLNNGKLGFYYTENEILPPLPVGSHRYILENFSGESLEGVKEQEVGEFDPPSEVRALIEGQFLSKRAHTERFGMPSPPLRIIATGGASANENILSLISAIFGCDVYTVQRPDSASLGAALRAAHGWLCNKKGSFVPISNLYEGKLETTSLNCKLKVKAGDANIASTYGLLMKKRMEIENKLVEKLGHF

Function: Mediates 1-deoxy-D-xylulose (DX) phosphorylation in the cytoplasm prior to the translocation of 1-deoxy-D-xylulose 5-phosphate into plastids. Can also phosphorylate D-xylulose (Xyl). Uses preferentially ATP as cosubstrate. Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+) Sequence Mass (Da): 61295 Sequence Length: 558 Pathway: Isoprenoid biosynthesis; carotenoid biosynthesis. Subcellular Location: Cytoplasm EC: 2.7.1.17

Q8EGP9

MNKFLIIDGLNLVRRIYAAIPDENDMESLTERVSVACTKLLRIHHPTHVAVVWDGDEISWRKQLYPDYKKGRKPMPEPLAAGLIALQEHLQNLQIQSIYAAAEADDVIATLATKTAKAQGEALIVSTDKGFSQLNHPRISQWDHFNQQYLNIAELEQKLGVDRSQFLDLMALAGDSGNKIPGIPGIGPKSAAELLRTFRTLATLFSSLPNLGAKQAKKLAEGRDMARLSYKLVQLQTDLPLNINLRDFRVNSPTKASSNNL

Cofactor: Binds 2 Mg(2+) per subunit. Only one magnesium ion has a direct interaction with the protein, the other interactions are indirect. Function: Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Sequence Mass (Da): 29005 Sequence Length: 261 EC: 3.1.-.-

Q54G06

MQRVLNKIISKDTINTMGKVAISKKVEKLRTFMKDQSLSAYIVPSEDAHQSEYICVKDKRREYISGFSGSAGCVVITLDNQLLWTDGRYWLQAEKELESNWKIMKDRVVGEPTIQDWLLSNLNKENKVGIDSRLISKGYYDSMKLVLKEKSIDIKFDEDGENLIDKVRESFKDEEEIPEYPKNSIFFLEDKFTGKQSNEKLKEIREEMKKQSADLMVVSALDEIAWLLNLRGSDISFNPVFLSYVVVEHEKVTLFVDESKLNDKTKSQLPSGIAISPYSSVFEYLRNSDKQGKKIWIDPRSSVALYNCVSISNLLEKINPILLSKAIKNETEIQGMKNAHIRDAVALIQFLAWMEEEIVEKSDETSHTEYSVCEKLEGFRRQQTDFVSLSFDTISSINANGAIIHYKPDETTSATIVKGMYLVDSGAQYLDGTTDVTRTLHYGKPTQHEIDCYTRVLRGHVGLSLLKFPNRVNGRDIDCVARTHLWSVGLDYAHGTGHGVGSFLNVHEGPQGISYRAIANPTNLQAGMTLTNEPGYYESGNFGIRIENVMIVAPVTTQFNNGKFIGFDNITLVPYERKLINLEMLTKDEINFINDYYKEIGEKILPLIEKTNNQKSINWLKNQIKPL

Cofactor: Binds 2 manganese ions per subunit. Function: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Sequence Mass (Da): 71393 Sequence Length: 627 Subcellular Location: Cytoplasm EC: 3.4.11.9

Q9NQW7

MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQKQGRQEALEWLIRETQPISKQH

Cofactor: Binds 2 manganese ions per subunit. Function: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro . Contributes to the degradation of bradykinin . Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Sequence Mass (Da): 69918 Sequence Length: 623 Subcellular Location: Cytoplasm EC: 3.4.11.9

O43895

MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDVRIWIGTSYTMYGIYEMIPKEKLVTDTYSPVMMTKAVKNSKEQALLKASHVRDAVAVIRYLVWLEKNVPKGTVDEFSGAEIVDKFRGEEQFSSGPSFETISASGLNAALAHYSPTKELNRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLIFPAATSGRMVEAFARRALWDAGLNYGHGTGHGIGNFLCVHEWPVGFQSNNIAMAKGMFTSIEPGYYKDGEFGIRLEDVALVVEAKTKYPGSYLTFEVVSFVPYDRNLIDVSLLSPEHLQYLNRYYQTIREKVGPELQRRQLLEEFEWLQQHTEPLAARAPDTASWASVLVVSTLAILGWSV

Function: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin. PTM: N-glycosylated. Location Topology: Lipid-anchor Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Sequence Mass (Da): 75625 Sequence Length: 674 Subcellular Location: Cell membrane EC: 3.4.11.9

B8YG19

MRLGVALSTIAVLLTATSARNLDKRQWGWPNFGGGNGGNGGNGGKTINDYKREQGAGRDIHVYAPSNLAPNSPLLLSLHGMDQDPNYQQSNTHWETLADSEGFVVVYPRGGTGMSTWDIQGTKDTQWVSQIIDQMKKEYNIDTKRVYLSGFSMGGMFTYHAMSQIANKIAAFAPCSGPNVFGASKAQRPVPIFHVHGTNDDVLNYQQVEGFLKNYRDQFHCPSQADTKTNYPNRENPNATLYTWGPCDKGVYIKHLKLQGRGHSPSSADIQDIWDFVSQWTVDGPVSASGNGGGNTTPTNPSTGGNGNGNGGGNTTPTNPSTGGNGNGNGGSTDKCSSNITKQGYKCCASNCEVVYTDSDGDWGVENDQWCGCGNRVTVGSGTCSAKILQQGYKCCPSGCIIYYTDEDGTWGVNGEEWCGCGSGSSSTGGGNDAPSSGSGYQGANGTNFCNNAKHSGESVTVTSNKVGDINGIGYELWADSGNNSATFYDDGSFSCSFQRAKDYLCRSGLSFDSTKTHKQIGHIYAEFKLVKQNIQNVDYSYVGIYGWTRNPLVEFYVVDNWLSQWRPGDWVGNKKHGDFTIGGAQYTVYENTRYGPSIDGDTNFKQYFSIRQQPRDCGTIDITAHFEQWEKLGMTMGKMHEAKVLGEAGSNNGGTSGTADFPFAKVYVKN

Function: Bifunctional acetylxylan esterase/xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades xylan from acetylxylan, beechwood, birchwood, and oat spelt, and releases acetate from 4-methylumbelliferyl acetate and beta-D-xylose tetraacetate. No activity is observed against carboxy methyl cellulose, beta-glucan, p-nitrophenol acetate, p-nitrophenol laurate, p-nitrophenol myristate, p-nitrophenol, palmitate, or beta-naphthol acetate. Catalytic Activity: Deacetylation of xylans and xylo-oligosaccharides. Sequence Mass (Da): 72469 Sequence Length: 671 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted

Q84H44

MANDTRQVVQGVQEMTPSEAFVETMVANGVTEIFGIMGSAFMDAMDIFAPAGIKLIPVVHEQGAAHMADGFARVSGRTGVVIGQNGPGISNCVTAIAAAYWAHTPVVIVTPEAGTTGIGLGGFQEARQLPMFQEFTKYQGHVTHPARMAEYTARCFARARDEMGPAQLNIPRDYFYGKIKCEIPLPQPLDRGPGGAQSLDAAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDSFPASHPLWCGPLGYQGSKAAMKLLADADVVLALGTRLGPFGTLPQHGLDYWPKNARIIQVDADSKMLGLVKKITVGVCGDAKASAAEISRRIDGMKLACDANKAERAARIQAEKDAWEQELTDWTHERDPFSLDMIEEQSKEEGNWLHPRQVLRELEKAMPEDVMVSTDIGNINSVANSYLRFEKPRSFFAAMSWGNCGYAFPTIIGAKVAAPHRPAVSYAGDGAWGMSMSEIMTCVRHDIPVTAVVFHNRQWGAEKKNQVDFYNRRFVAGELESESFAGIARAMGAEGVVVDRIEDVGPALKKAIDAQMNDRKTTVIEIMCTRELGDPFRRDALSKPVRLLEKYRDYT

Catalytic Activity: acetyl phosphate + H(+) + sulfite = phosphate + sulfoacetaldehyde Sequence Mass (Da): 65108 Sequence Length: 598 Pathway: Organosulfur degradation; taurine degradation via aerobic pathway; acetyl phosphate and sulfite from taurine: step 2/2. Subcellular Location: Cytoplasm EC: 2.3.3.15

Q93PS3

MAKVKMTPSEAMTEVLVNEGVTHVTGILGSAFMDMLDLWPTAGIEFIAVRHEQTAGHMQDAYCRITGKASVCIGQNGPGVTNLVTCVAAANQAHTPMVVLGPSAGTPTVGWDGFQECDQVSIFRSITKQVLQVPHPSRAGDVLRTAFRIAYAERGPVYVDIPRNYFYGEVYEEILRPDQYRAMNVRGAGDATELARATEILAAAKNPVIISGRGVVDADAFAEVKEIAHMLTAPVAMSYLHNDTYPADDELWVGPIGYMGAKSAMYSLQDADVILAIGSRLSVFGTLPQYDINYFPENAKIIQIEVNPKQIGRRHPVTVPIIGDAKLATAELIKLLKAKGDVKPNAERLAKIQERRNDWFKEIEEMAMMPGNPINPRRVLFEVAKLMPEDAILTTDIGNVASTANSYFKFTKPKKHIAALTFGNTGFAYQAGLGAQMAEPDSPVVAIVGDGAWGQSLHEISTAVQYKLPVIACVFRNMAWCAEKKNQIDFYNNRFVGTEIPNPISFIPAAEAFGAKGIRVEKPEDIADAFKQGLAWRAEGHPVVLEFVVDGTILAPPFRKDALALPTRYLPKYEHLDAKYFPKN

Catalytic Activity: acetyl phosphate + H(+) + sulfite = phosphate + sulfoacetaldehyde Sequence Mass (Da): 63939 Sequence Length: 584 Pathway: Organosulfur degradation; taurine degradation via aerobic pathway; acetyl phosphate and sulfite from taurine: step 2/2. Subcellular Location: Cytoplasm EC: 2.3.3.15

A3SR25

MLFRASQPEDKPMKMTTEEAFVKTLQMHGIQHAFGIIGSAMMPISDIFGKAGITFWDCAHEGSGGMMADGYTRATGKMSMMIAQNGPGITNFVTAVKTAYWNHTPLLLVTPQAANKTMGQGGFQEVEQMAAFKDMVCYQEEVRDPTRMAEVLNRVILNAKRYSAPAQINVPRDYFTQVIDIELPKIVDFERPSGGEEALDEAAKLLSEAKFPVILNGAGVILAGAIPATAELAERLDAPVCCGYQHNDAFPGSHPLHAGPLGYNGSKAGMELISKADVVLALGTRLNPFSTLPGYGIDYWPKDAKIIQVDVKPERIGLTKPVAVGIVGDAKKVAKTILAKLSDTAGDADREERKATIAKTKSAWAQELSSMDHEQDDPGTTWNERARGAKPDWMSPRMAWRAIQAALPKEAIISSDIGNNCAIGNAYPSFEEGRKYLAPGLFGPCGYGLPAVVGAKIGCPDTPVVGFSGDGAFGIAVNELTAIGRGEWPAVTHVVFRNYQWGAEKRNSTLWFDDNFVGTELDEQVSYAGIAKACGLKGVVARTMDELTDALDQAIKDQKAGTTTLIEAMINQELGEPFRRDAMKKPVAVAGIDPADMREQQVD

Function: Catalyzes the degradation of sulfoacetaldehyde into sulfite and acetyl phosphate. Involved in sulfolactate degradation. Catalytic Activity: acetyl phosphate + H(+) + sulfite = phosphate + sulfoacetaldehyde Sequence Mass (Da): 65061 Sequence Length: 603 EC: 2.3.3.15

Q8PEW5

MSNTVYIGAKEYFPGIGKIGFEGRDSDNPLAFKVYDANKTIGDKTMAEHLRFAVAYWHSFCGNGADPFGPGTRAYPWDVGDTALNRAEAKADAAFEFFTKLGVPYYCFHDIDLSPDADDITEYESNLKHMVGVAKQRQADTGIKLLWGTANLFSHPRYMNGASTNPDFNVVARAAVQVKAAIDATVALGGENYVFWGGREGYACLHNTQMKREQDNMARFLTLARDYGRSIGFKGNFLIEPKPMEPMKHQYDFDSATVIGFLRQHGLDQDFKLNIEANHATLSGHSFEHDLQVASDAGLLGSIDANRGNPQNGWDTDQFPTDLYDTVGAMLVVLRQGGLAPGGLNFDAKVRRESSDPQDLFLAHIGGMDAFARGLEVANALLTASPLEQWRAERYASFDSGAGADFAAGKTTLADLAKHAAGNAPQQISGRQEAYENLINQYLTR

Cofactor: Binds 2 magnesium ions per subunit. Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose Sequence Mass (Da): 48766 Sequence Length: 445 Subcellular Location: Cytoplasm EC: 5.3.1.5

Q9FKK7

MKKVEFFMLLLCFIAASSLVSADPPTCPADLGGKCSDSDDWQGDFFPEIPKIKYEGPSSKNPLAYRWYNAEEEILGKKMKDWFRFSVAFWHTFRGTGGDPFGAATKYWPWEDGTNSVSMAKRRMRANFEFLKKLGVDWWCFHDRDIAPDGTTLEESNKNLDEVIELAKELQKGSKIKPLWGTAQLFLHPRYMHGGATSSEVGVYAYAAAQVKKAMEVTHYLGGENYVFWGGREGYQTLLNTDMGRELDHLARFFEAAVAYKKKIGFKGTLLIEPKPQEPTKHQYDWDAATAANFLRKYGLIDEFKLNIECNHATLSGHTCHHELETARINGLLGNIDANTGDAQTGWDTDQFLTDVGEATMVMMSVIKNGGIAPGGFNFDAKLRRESTDVEDLFIAHISGMDTMARGLRNAVKILEEGSLSELVRKRYATWDSELGKQIEEGKADFEYLEKKAKEFGEPKVSSAKQELAEMIFQSAM

Cofactor: Binds 2 manganese ions per subunit. Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose Sequence Mass (Da): 53720 Sequence Length: 477 EC: 5.3.1.5

A2QTU5

MYFSSFLALGALVQAAAATYFAPNSTGLRIQHGFETILIQPFGYDGFRVRAWPFRPPSGNEISFIYDPPIEGYEDTAHGMSYDTATTGTEPRTLRNGNIILRTTGWGGTTAGYRLSFYRVNDDGSETLLTNEYAPLKSLNPRYYYWPGPGAEFSAEFSFSATPDEQIYGTGTQQDHMINKKGSVIDMVNFNSYIPTPVFMSNKGYAFIWNMPAEGRMEFGTLRTRFTAASTTLVDYVIVAAQPGDYDTLQQRISALTGRAPAPPDFSLGYIQSKLRYENQTEVELLAQNFHDRNIPVSMIVIDYQSWAHQGDWALDPRLWPNVAQMSARVKNLTGAEMMASLWPSVADDSVNYAALQANGLLSATRDGPGTTDSWNGSYIRNYDSTNPSARKFLWSMLKKNYYDKGIKNFWIDQADGGALGEAYENNGQSTYIESIPFTLPNVNYAAGTQLSVGKLYPWAHQQAIEEGFRNATDTKEGSACDHVSLSRSGYIGSQRFCSMIWSGDTTSVWDTLAVQVASGLSAAATGWGWWTVDAGGFEVDSTVWWSGNIDTPEYRELYVRWLAWTTFLPFMRTHGSRTCYFQDAYTCANEPWSYGASNTPIIVSYIHLRYQLGAYLKSIFNQFHLTGRSIMRPLYMDFEKTDPKISQLVSSNSNYTTQQYMFGPRLLVSPVTLPNVTEWPVYLPQTGQNNTKPWTYWWTNETYAGGQVVKVPAPLQHIPVFHLGSREELLSGNVF

Function: Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides. Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose. Sequence Mass (Da): 82593 Sequence Length: 736 Subcellular Location: Secreted EC: 3.2.1.177

P19148

MNKYFENVSKIKYEGPKSNNPYSFKFYNPEEVIDGKTMEEHLRFSIAYWHTFTADGTDQFGKATMQRPWNHYTDPMDIAKARVEAAFEFFDKINAPYFCFHDRDIAPEGDTLRETNKNLDTIVAMIKDYLKTSKTKVLWGTANLFSNPRFVHGASTSCNADVFAYSAAQVKKALEITKELGGENYVFWGGREGYETLLNTDMEFELDNFARFLHMAVDYAKEIGFEGQFLIEPKPKEPTKHQYDFDVANVLAFLRKYDLDKYFKVNIEANHATLAFHDFQHELRYARINGVLGSIDANTGDMLLGWDTDQFPTDIRMTTLAMYEVIKMGGFDKGGLNFDAKVRRASFEPEDLFLGHIAGMDAFAKGFKVAYKLVKDRVFDKFIEERYASYKDGIGADIVSGKADFRSLEKYALERSQIVNKSGRQELLESILNQYLFAE

Cofactor: Binds 2 cobalt ions per subunit. Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose Sequence Mass (Da): 50475 Sequence Length: 439 Subcellular Location: Cytoplasm EC: 5.3.1.5

P46364

SELKDIIAAVTPCKGADFELQALKIRQPQGDEVLVKXXATGM

Cofactor: Binds 2 Zn(2+) ions per subunit. Function: Oxidizes primary alcohols with an aromatic or cyclohex-1-ene ring. It is highly specific for benzyl alcohol. Catalytic Activity: an aromatic primary alcohol + NAD(+) = an aromatic aldehyde + H(+) + NADH Sequence Mass (Da): 4508 Sequence Length: 42 EC: 1.1.1.90

P12867

MALVAGIDSSTQSCKVVIRDAETGALVRQGRASHPDGTEVHPDAWWSALQSAIEEAGGLDDVAAASVAGQQHGMVALDENGEVVRPALLWNDTRSAGAAADLIAELGGGEKWAEAVGIVPVASFTLTKLRWLARNEPANAAKVAAVCLPHDWLTWKLSGSTDIADIKTDRSDASGTLYWSAKTNEYRRDLLELGFGRDLVLPEVLGPTGIAGHLPNGAPLGPGAGDNAAAALGTGALPGDVIVSIGTSGTVFVSSDVAPVDGRGTVAGFADTTGRFLPIVVTLNAARVLDAAAKLLGVDHDELSRLALSAPAGADGMVLVPYLEGERTPNRPDATGAIHGLTLKTSDPAHLARAAVEGMLCALADGLDALVAHGAEANRIVLVGGGARSEAVRRIAPALFGKPVLVPPPGEYVADGAARQAAWVARGGDTPPAWSAASPEVYEDDPVPLIREQYAAAQNAVIDRTR

Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+) Sequence Mass (Da): 47866 Sequence Length: 466 EC: 2.7.1.17

P54271

MALVAGIGQLDAVVQGGHSATPRPATGPAGPAAHSGRHQYDPDAWWARATGDSREAGGLGRTLAAASVAGQQQRHGALLESAVTVVRPALLWNDTRRPGAAADLIQELGGADKWAEAVGIVPVASLTLTNSGWLARHEPANAAKVAAICLPHDWLTWKLSGS

Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+) Sequence Mass (Da): 16671 Sequence Length: 162 EC: 2.7.1.17

F4JG10

MEKNTNTNHTSDDNNDKNHTNEEQEKIILNPNFEDGLNNWTGRACKIVLHESMDSGKIVPLSGKVFAAATQRKDTWNGIQQEISGRFRRKRVYEVTAVVRIFGNNVTSATVQATLWVLNANKREQYIVIANVQATDKNWVELKGKFVIHGSPSRVILYLEGPPPRADILLNSLVVQHAKRNRPSPPPFYENPGFGVNIVENSEVLDGGTKPWFTLGNCKLSVGQGAPRTLPPMARDTLGPHKPLGGNYIVVTNRTQTWMGPAQMITDKIKLFLTYQISAWVKLGVGVSGSSMSPQNVNIALSVDNQWVNGGQVEVTVGDTWHEIAGSFRLEKQPQNVMVYVQGPGAGIDLMIAALQIFPVDRRERVRCLKRQVDEVRKRDIVLKFSGLNDDESFDLFPYIVKVKQTYNSFPVGTCINRTDIDNEDFVDFFTKNFNWAVFGNELKWYATEAERGKVNYQDADDMLDLCIGNNINVRGHCIFWEVESTVQPWVRQLNKTDLMNAVQKRLTDLLTRYKGKFKHYDVNNEMLHGSFYQDRLGKGVRALMFNIAHKLDPSPLLFVNDYHVEDGDDPRSSPEKYIKLVLDLEAQGATVGGIGIQGHIDSPVGAIVCSALDMLSVLGRPIWFTELDVSSSNEYVRGEDLEVMLWEAFAHPSVEGIMLWGFWELSMSRENANLVEGEGEVNEAGKRFLEVKQEWLSHAYGIINDESEFTFRGYHGTYAVEICTPAGIVLKTFVVEKGDTPLVISIDLSSL

Function: Binds to and hydrolyzes insoluble and soluble xylan substrates. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 84552 Sequence Length: 752 Domain: The GH10 domain binds to xylan. Pathway: Glycan degradation; xylan degradation. EC: 3.2.1.8

P23557

MKQQYLLDYEATKASKNGMPVCKFDSCIPALQFCKENGIKMRGHVLVWHNQTPEWFFHKDYDVSKPLVDAATMERRLESYIKQVIEFCQKNYPGVVYCWDVVNEAILDDGSWREINNNWYTIMKEKYVEKAFYYARKYAKKDVALFYNDYNVFLPAKREAIYNLAQKLKEKGLIDGLGLQPTVGLNYPELDSDDIDSFKTTLETFAKLGLQIHITELNFEIKGDESNRTPENLKKQADRYYEMMKLLLKEDTDNGGPCNITCVTVFGICDDYPLYKNFKQCMYLWDKNCNPKPCFYSFLQAGLDWKASLLSK

Function: Could be a xylanase. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 36494 Sequence Length: 312 Pathway: Glycan degradation; xylan degradation. EC: 3.2.1.8

G4NA54

MVSFTTILVAATAALVAANPVPPSIDEMREIYVKSRDLHARGGTPSSTGTHDGFYYSWWTDNGAQATYTNNAGGSYSITWSGNGNLVGGKGWNPGSARNVTYSANYRPNGNSYLSVYGWTRNPLVEYYVVENFGTYDPSSQASRKGTINVDGATYQVAQSTRTNQPSIDGTRTFQQYWSVRQQKRSSGTVDMKKHFDAWASMGMKLGTHDYQIVATEGYFSSGSSTVTIQR

Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 25305 Sequence Length: 231 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.8

Q84WT5

MNSIKNGFFLCMIFLLWCHVDSGVSIDPFSHSHSLNTECVMKPPRSSETKGLLQFSRSLEDDSDEEWKIDGNGFIREMAQRIQLHQGNIYSFSAWVKLREGNDKKVGVVFRTENGRLVHGGEVRANQECWTLLKGGIVPDFSGPVDIFFESENRGAKISAHNVLLKQFSKEEWKLKQDQLIEKIRKSKVRFEVTYENKTAVKGVVISLKQTKSSFLLGCGMNFRILQSQGYRKWFASRFKITSFTNEMKWYATEKARGQENYTVADSMLKFAEDNGILVRGHTVLWDNPKMQPSWVKNIKDPNDVMNVTLNRINSVMKRYKGKLTGWDVVNENLHWDYFEKMLGANASTSFYNLAFKIDPDVRLFVNEYNTIENTKEFTATPIKVKKMMEEILAYPGNKNMKGAIGAQGHFGPTQPNLAYIRSALDTLGSLGLPIWLTEVDMPKCPNQAQYVEDILREAYSHPAVKGIIIFGGPEVSGFDKLTLADKDFNNTQTGDVIDKLLKEWQQKSSEIQTNFTADSDNEEEEVSLLHGHYNVNVSHPWIANLSTSFSLEVTKEMDQDQVIRVVISA

Function: Binds to and hydrolyzes insoluble and soluble xylan substrates. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 64941 Sequence Length: 570 Domain: The GH10 domain binds to xylan. Pathway: Glycan degradation; xylan degradation. EC: 3.2.1.8

A0A1P8B8F8

MKNINNGFFLCMLLLLWCFVHSGISIDPFSPSDSLKTECVMKPPRSSETKGLLQFSRSVEDDSDEEWKIDGSGSIREMTQRIQLHEGNIYSFSAWVKLREGNNKKVGVVFRTENGRFVHGGEVRAKKRCWTLLKGGIVPDVSGSVDIFFESDDKEAKISASDVSLKQFSKQEWKLKQDQLIEKIRKSKVRFEVTYQNKTAVKGAVISIEQTKPSFLLGCAMNFRILQSEGYRNWFASRFKITSFTNEMKWYTTEKERGHENYTAADSMLKFAEENGILVRGHTVLWDDPLMQPTWVPKIEDPNDLMNVTLNRINSVMTRYKGKLTGWDVVNENVHWDYFEKMLGANASSSFYNLAFKLDPDVTMFVNEYNTIENRVEVTATPVKVKEKMEEILAYPGNMNIKGAIGAQGHFRPTQPNLAYMRSALDTLGSLGLPIWLTEVDMPKCPNQEVYIEEILREAYSHPAVKGIIIFAGPEVSGFDKLTLADKYFNNTATGDVIDKLLKEWQQSSEIPKIFMTDSENDEEEVSLLHGHYNVNVSHPWMKNMSTSFSLEVTKEMGQRQVVRVVINA

Function: Binds to and hydrolyzes insoluble and soluble xylan substrates. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 64947 Sequence Length: 569 Domain: The GH10 domain binds to xylan. Pathway: Glycan degradation; xylan degradation. EC: 3.2.1.8

G4MLU0

MTRLATLITLAGLLAVSPGAYAQRNRNDTGGSTGAEGLNSLAVKAGLLYFGTASDTRNFADEPYMSVVNNTNEFGMIVPENSMKWEATEKEPGRFSFANADRVRALTKANGQMLRCHALTWHSQLPNFVKTTAWTRDTLTAAIESHISNEVGHFAGDCYAWDVVNEAVNENGSFRDSPFHRTLGTDFLAISFRAAAAADPNAKLYYNDFNIETPGPKANAAMGIVRLLKEQGVRIDGVGFQGHLTVGSTPSRAQLASQLQRFADLGVEVTYTELDIRHKSLPVSSRAAQDQARDYVSVIGSCLDVTACVGVMVWQPTDKYSWIPETFPGTGDACLFDANMNPKPAYTSVSSLLAAAAATAPASVVPPASVTTSKTPIQAGAGRETVSIAGLTLALSSLAFGMFML

Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Location Topology: Lipid-anchor Sequence Mass (Da): 43247 Sequence Length: 405 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Cell membrane EC: 3.2.1.8

I1S3C6

MHFLGLVVAFAPAALAQSAIWGQCGGTGWSGSTTCQSGLKCEKINDFYYQCIPGSDNGGGTTPDPGTPSPGNGNADATGLDAKIRAKGKIYFGTEIDHYHLSNNPLINIVKKDFGQVTNENSMKWDAIEPSRGQFTFSNADKVVDFAQANGKKIRGHTLLWYSQLPQWVKNIRDRATMTSVIENHVKTVVTRYKGKILHWDVVNEIFAEDGNMRNSEFYQVLGEDFVGIAFRAARAADPAAKLYINDYNLDIANYAKVTRGMVDHVNKWVSQGIPIDGIGSQAHLAKPGGWNPASGFPAALKVLAGANVKEVAITELDIDGAAANDYVTVVNSCLTTPKCVGITVWGVSDKDSWRSESNPLLFDRNYQPKAAYTAVSNALN

Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Plays an important role in causing fusarium head blight (FHB) on cereal crops. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 41327 Sequence Length: 381 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.8

P45796

MIRKCLVLFLSFALLLSVFPMLNVDAANRPLAKIPGNSNPLMDHKLGADPYSLVYDGRVYIFMSSDTYVYNKDGSIKENDFSALDRIQVISSTDMVNWTDHGTIPVAGANNKNSGRGIAKWASNSWAPAVAHKKINGRDKFFLYFANGGAGIGVLTADTPIGPWTDPLGKALVTHSTPGMAGVTWLFDPAVLVDDDGTGYLYSGGGIPNESDPASIANPKTARVIKLGADMTSVIGSATTIDAPYLFEDSGIHKYNGKYYYSYCINFAGTHPQQYPAGEIGYMVSDNPMGPFTYKGHFLKNPYTFFGVGGNNHHAVFNFKNEWYVVYHAQTVSKAQIGAGKGYRSPHINKLVHKEDGSISEVQGNMTGIAQLSNMNPYTRVEAETIAWQAGVTTEPTQASGGPISNLNVTNIHNGDWIAVGKADFGSAGAKTFKANVATNVGGNIEVRLDSETGPLVGSLKVPSTGGMQTWREVETTINNATGVHNIYLVFTGSGSGNLLNLDAWQFTPNTGGNTITKVEAENMKIGGTYAGKISAPFDGVALYANADYVSYSQYFANSTHNISVRGASSNAGTAKVDLVIGGVTVGSFNFTGKTPTVQTLSNITHATGDQEIKLALTSDDGTWDAYVDFIEFSL

Function: Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation (By similarity). Preferres wheat flour xylan over oat spelt xylan as substrate. Does not display endoxylanase activity. Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Sequence Mass (Da): 67914 Sequence Length: 635 Domain: The C-terminal CBM6 domain shows calcium-dependent xylo-oligosaccharide and xylan binding. It binds, next to the structural calcium ion, a second calcium ion that, in addition to its coordination sites on the protein, completes its heptacoordination through coordination to the bound xylose moiety. Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.55

Q53317

MKKSIFKRYAAAVGLMASVLMFTAVPTTSNAADDQKTGKVGGFDWEMWNQNYTGTVSMNPGAGSFTCSWSGIENFLARMGKNYDDQKKNYKAFGDIVLTYDVEYTPRGNSYMCIYGWTRNPLMEYYIVEGWGDWEPPGNDGVDNFGTTTIDGKTYKIRKSMRYNQPSIEGTKTFPQYWSVRTTSGSRNNTTNYMKDQVSVTKHFDAWSKAGLDMSGTLYEVSLNIEGYRSNGSANVKSISFDGGIDIPDPEPIKPDENGYYLKENFESGEGNWSGRGSAKVKSSSGYDGTKGIFVSGREDTWNGASINLDELTFKAGETYSLGTAVMQDFESSVDFKLTLQYTDADGKENYDEVKTVTAAKGQWVDLSNSSYTIPSGATGLVLYVEVPESKTDFYMDGAYAGVKGTKPLISISSQSVDPPVTEPTNPTNPTGPSVTKWGDANCDGGVDLSDAIFIMQFLANPNKYGLTGTETNHMTNQGKVNGDVCEHGSGLTEDDAVSIQKYLIRAISELPESYLEGHDPSKTTTTTTRITTTTTTTTTTTTSKTTTTTTTTSPAMHGGYRDLGTPMNTSATMISDFRTGKAGDFFASDGWTNGKPFDCWWYKRNAVINDGCLQLSIDQKWTNDKNPDWDPRYSGGEFRTNNFYHYGYYECSMQAMKNDGVVSSFFTYTGPSDDNPWDEIDIEILGKNTTQVQFNYYTNGQGKHEKLYDLGFDSSEAYHTYGFDWQPNYIAWYVDGREVYRATQDIPKTPGKIMMNAWPGLTVDDWLKAFNGRTPLTAHYQWVTYNKNGVQHSSQGQNPWG

Function: Contains two catalytic domains with xylanase and endo-beta-1,3-1,4 glucanase activities. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 89091 Sequence Length: 802 Pathway: Glycan degradation; xylan degradation.

Q5ZNB1

MTLVKSILLALAAGHVAQAQLNTAAKAAGLLYFGTAVDNPDLSDSKYLVNLETADFGQITPANAMKWQPTEPSQGSYTFTQGDQIASLAKSNNDYLRCHNLVWYNQLPSYITSGSWTNATLIAALKEHINGVVTHYKGQCYAWDVVNEALNEDGTYRQNVFYQHIGEAYIPIAFAAAAAADPNAKLYYNDYNIEYAGAKATGAQGIVKLIQAAGGRIDGVGLQSHFIVGQTPSLATQKANMAAFTALGVDVAITELDIRMTLPDTSALQTQQSTDYQTTTTACVQTKGCVGITLWDYTDKYSWVPGTFSGQGDACPWDSNYNKKPAYYGILAGLQSGSGSSSSTSSTTLITTTTPTASSSTTSATTTSATSGAAHWGQCGGIGWSGPTICVSPYTCQVLNPYYSQCL

Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Shows an endo-mode of action on xylan forming mainly xylobiose and short-chain xylooligosaccharides (XOS). Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 43235 Sequence Length: 407 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.8

O94163

MVHLKALASGTLFASLASSAVISRQAAASINDAFVAHGKKYFGTCSDQALLQNSQNEAIVRADFGQLTPENSMKWDALEPSQGSFSFAGADFLADYAKTNNKLVRGHTLVWHSQLPSWVQGITDKDTLTEVIKNHITTIMQRYKGQIYAWDVVNEIFDEDGTLRDSVFSQVLGEDFVRIAFETAREADPNAKLYINDYNLDSADYAKTKGMVSYVKKWLDAGVPIDGIGSQSHYSANGFPVSGAKGALTALASTGVSEVAVTELDIEGASSESYLEVVNACLDVSSCVGITVWGVSDKDSWRSSTSPLLFDSNYQAKDAYNAIIDAL

Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 35402 Sequence Length: 327 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.8

Q96VB6

MVHLKSLAGILLYTSLCIASSQQAPASINNAFVAKGKKYFGTCADQGTLSDGTNSGIIKADFGQLTPENSMKWDATEPSQGKFSFSGADYLVNYAATNNKLIRGHTLVWHSQLPSWVQGITDKNTLTSVLKNHITTVMNRYKGKVYAWDVVNEIFNEDGTLRSSVFYNVLGEDFVRIAFETARAADPQAKLYINDYNLDSANYGKTTGLANHVKKWIAQGIPIDGIGSQTHLSAGGSSGVKGALNTLAASGVSEVAITELDIAGASSNDYVNVVEACLEVSKCVGITVWGVSDKNSWRSAESPLLFDGNYQPKSAYNAILNAL

Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 34696 Sequence Length: 323 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.8

Q6PRW6

MIPNITQLKTAALVMLFAGQALSGPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKVYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGALNALASAGTEEVAVTELDIAGASSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNVSQLLSRQHAFDLYLKLGNLLLSRLHSD

Function: Cold active endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 38165 Sequence Length: 353 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.8

O97402

MQFLIPVVILCVSLVDSQKVLYNNEIGFNNGFYYAFWKDSGSATFTLESGGRYAGNWTTSTNNWVGGKGWNPGNSWRTVNYSGYYGINEYANSYLSLYGWTTNPLIEYYVVESYGSYSPLNCPGGTDEGSFTSGGATYQVRKCRRTNAPSIIGTQSFDQYFSVRTPKKGFGQVSGSVNFADHVQYWASKGLPLGTHAHQIFATEGYQSSGFADITVS

Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Sequence Mass (Da): 23942 Sequence Length: 217 Pathway: Glycan degradation; xylan degradation. Subcellular Location: Secreted EC: 3.2.1.8

Q9ZBU1

MSDITVTNWAGNITYTAKELLRPHSLDALRALVADSARVRVLGSGHSFNEIAEPGDGGVLLSLAGLPSVVDVDTAARTVRVGGGVRYAELARVVHARGLALPNMASLPHISVAGSVATGTHGSGVGNGSLASVVREVELVTADGSTVVIARGDERFGGAVTSLGALGVVTSLTLDLEPAYEMEQHVFTELPLAGLDPATFETVMAAAYSVSLFTDWRAPGFRQVWLKRRTDRPLDGFPYAAPAAEKMHPVPGMPAVNCTEQFGVPGPWHERLPHFRAEFTPSSGAELQSEYLMPREHALAALHAMDAIRETLAPVLQTCEIRTVAADAQWLSPAYGRDTVAAHFTWVEDTAAVLPVVRRLEEALVPFAARPHWGKVFTVPAGELRALYPRLADFGALAGALDPAGKFTNAFVRGVLAG

Cofactor: Binds 1 FAD covalently per subunit. Function: Oxidase that performs selective oxidation of the terminal primary hydroxyl group of several alditols, with a reduction of O2 to H2O2. Shows highest activity on xylitol and D-sorbitol, and a poor efficiency with D-mannitol and L-threitol. Catalytic Activity: an alditol + O2 = an aldose + H2O2 Sequence Mass (Da): 44347 Sequence Length: 418 EC: 1.1.3.41

Q6YRJ4

MPKPLIIFKDFSFQYYSQQTPTLNQINLTIYEGQKVLIVGKNGSGKSTFLKCINGLIPHSYQGKITGTAIIKDKVLTQTNIFDLSLDVGTIMQDTDNQFVGLTVAEDIAFALENDDLPQSEIYQKVNMWAQDLGLQSFLDYKPQELSEGHKQLASMAGVLIYNPSILLFDESLSNLDPVSRAKMTALIKTIHQKYHSTILVIEHYLEDILDDSFDRVIVFEDEKIIYDNSPQKLILENILTKQGIQEPTYISALKKVGINLGSLPYLLNLPALQSLDFVQYFSNQLTNLKKCAISQNDPTQLLPFFPKQFAPFCPILQLQNISYHYESKQPNILNDISLDLFPGKMISIVGKNGSGKSTLAKVICGFSNPQTGTILLNNQDLTHLSLQQRSEKIGFVMQNPHHMISQKTVFEEVALGLLGKQLSLTEIKTKVHAILKTCNLDCFVNRPISALSFGQKKRLTIASILVMQPQILILDEPTIGQDLKHHTQIMTFLQKLNNKGITIIIITHDMSLMLNYTQRTLVLEQGKIIANTTPLKIFTDMSLMQKTSLNPISLIVLINKLPFTSEQKNVLLTQMLAFLKEDCCYGK

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 66174 Sequence Length: 588 Subcellular Location: Cell membrane EC: 7.-.-.-

Q9RVK3

MIDPRYPLGPMPQPRDLSDDERQEARAALRALPGELRAAVAGLSEPQLDTPYREGGWTVRQVVHHVADRHLNAYVHTARVLSGGEALAQPAHEEAWAALPASSFATELSLLLLERLHIHWDEVLADVTDWQQAGLRPDGSEWTLDGLLGQAAWHGRHHTAHITRLREREGW

Cofactor: Binds 1 zinc ion per subunit. Function: Possible metal-dependent hydrolase. Sequence Mass (Da): 19138 Sequence Length: 171 Subcellular Location: Cytoplasm EC: 3.-.-.-

Q9RVK2

MEHDERTHVPVELRAAGVVLLNERGDILLVQEKGIPGHPEKAGLWHIPSGAVEDGENPQDAAVREACEETGLRVRPVKFLGAYLGRFPDGVLILRHVWLAEPEPGQTLAPAFTDEIAEASFVSREDFAQLYAAGQIRMYQTKLFYADALREKGFPALPV

Cofactor: Binds 3 Mg(2+) ions per subunit. Function: Hydrolase that can act as a nucleoside triphosphatase and a dinucleoside polyphosphate pyrophosphatase. The best substrates are 8-oxo-dGTP and 8-oxo-GTP. Other substrates include Ap4A, dGTP and GTP. May be involved in protection from damage caused by radiation. Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGDP + H(+) + phosphate Sequence Mass (Da): 17569 Sequence Length: 159 EC: 3.6.1.61

Q57571

MREIMKILIITGKLAERKVKDAVKKYDFIDVHVANISVAAFLTPNLIIKEIKKLENKLGKKLKDIYDFVLVTGLIRHDLKNVEEETGIKCFKSTREASDIPILIENLDKIKLSTKEYADLQLLEIIRKKCEEEIKKAEEQELGEGDIKIGKLKVGDKFPMRVLGEIVHAPWLKEKELEEKIIYYLESGADMIDLGMVSNENNADKIKDMLKIARDLTDNPISVDTLNTKELIEAINLGADMILSVDAGNLDELIPYLKDSETAVVVLPTNYKTNYVPETIEGKIKSLEENIKKLIDAGIEKIVADPILEPINNAGCSFIESVIACREFKKRNKLPLFFGVGNVTELFDADSNGVNALLAAIGAEIGANILFTPEASAKCKFSIKELKIASKMMFLAKKRNSLPKDIGYNLINYKDKRFEEEITFNSYNIPIIKAEEDERQILDEGSFKIEIDRKNKEIVAIYFNKRREPVLIIRGKKPKEIYETAIRLNLIKKLDHASYFGRELAKAEIALRIGKKYNQDFDLFL

Function: Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4-aminobenzoate to form 7,8-dihydropteroate. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 59645 Sequence Length: 525 Subcellular Location: Cell membrane

Q54F34

MAGSLDDSIYNNGRSGGGGGGFKFSKGFNKDSISKRIIMMLFFSKGIRAWSCIILLYFLQSSISIISASFYMCLFSAIFSVVVEKPWNLLSSLRPSQIKKIIYHSIFNLLIIITWNSSIKFIGPIGSILASDYTFSTYPLIFNSLLQGNFLATDMSRGSIMLMIGYFLIPLFGISNRLDILGYTSSQVFMIGLFSLIVHNVLVLWKKTIVRSWNSGSSGGKNKLSSLGSCVSTIILFVFKLFEGFSSGSSGSDSINQVSYSQLFVIAIITFILYSLNQFIDDVSEKELTFNVLSKVSLTSSVIFGLLAALFIGFKDFFHPILILSFIFIINAIHILYSKSNDIQPMTFSNNMDGGNSSIKTYNSSGGGGGGSIINGNGSGNAIYYFEILKDVLRQIVDKPTSRRIFTFLVINLMFMFVEMAYGIWTNSLGLITDACHMFFDATALFIALVAEVISQWKQNDKYSYGYGRFQVLSGFVNGIFLIFIAVTILMESVERLLEPPEINTDKLLLVSVLGFIINLIGIFSFHGDHGHSHGGGGGHSHGGGEKKEKHHGHSHGGHGDHQQVTPILGEEKKKKRSVNIDGVFLHLLADTLGSVGVIVSSLIIQIWGYTLADPICSLLISILIFLSVLPLIANTAKTLLQCTPEPIQSSLYQINQFILSIDGVHNIISYHFWSHYDDMNIATLKIQLNETASSNSTLDTERIKKSISKYLNKDHNIHKCIIEFIPLLYNNNNQQQGNDVPLINHHIHNDIHHNHSSSSSSSSHHHRHN

Function: May be involved in zinc transport from the cytoplasm to either intracellular organelles or extracellular spaces. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 85330 Sequence Length: 770 Subcellular Location: Membrane

O27262

MVIIHSPSYDLHNHEGHVENSGRTRAILRAIESSDLSPRFVEPGMAGIDDILMVHSSTHVEYLEVFAGRGGGWLDYDTYMTPESFSVARLSAGGAMLAAEEALRDGWSYSLGRPPGHHATYDRSMGFCIFNNIAIAIEHARRNLGVSRPLVLDFDVHHGNGTSSIFYRDRDVMYISIHQDPRTLFPGTGFIDETGSGEGEGFNLNIPMPRGSGNREYLWILGMILPAVLEGFRPDMIFVSAGFDAHRRDPLAEIMVDEEFFSWIGWFIHQTGLPCTAVLEGGYDPEALGRSNIAFMRGLDGEEYEPETAAPGGVSEIFSQLSDRFSAYFNF

Cofactor: Binds 1 zinc ion per subunit. Function: Probable deacetylase. Sequence Mass (Da): 36722 Sequence Length: 331 EC: 3.5.1.-

O58967

MRRISPTRFLLYIVLIFLAAWYLLPIWSAITTSTKTGEQVALTTPVQFVFPPTFDPYREAFRELKRPILNSLIFTTFATIFSTILGSIAGFTIAKLVRGRVSRQLLALISFGIFLPYQSILIPLVKIISSLGLYNRILGLILTHTAYGIPITTLLFTNYYYEIPDELVEAAKIDGADPWKIYTKVILPLSKAPFVVTGIYQFTNIWNDYLFGVVLTRGEEAMPATVKLANLKGSFVANWNIQMAGALIVALPTLLIMIALGKYLIRGYTSGALKG

Function: Probably part of a binding-protein-dependent transport system PH1214/15/16. Probably responsible for the translocation of the substrate across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 30683 Sequence Length: 275 Subcellular Location: Cell membrane

P45114

MKKAIKLNLITLGLINTIGMTITQAQAEETLGQIDVVEKVISNDKKPFTEAKAKSTRENVFKETQTIDQVIRSIPGAFTQQDKGSGVVSVNIRGENGLGRVNTMVDGVTQTFYSTALDSGQSGGSSQFGAAIDPNFIAGVDVNKSNFSGASGINALAGSANFRTLGVNDVITDDKPFGIILKGMTGSNATKSNFMTMAAGRKWLDNGGYVGVVYGYSQREVSQDYRIGGGERLASLGQDILAKEKEAYFRNAGYILNPEGQWTPDLSKKHWSCNKPDYQKNGDCSYYRIGSAAKTRREILQELLTNGKKPKDIEKLQKGNDGIEETDKSFERNKDQYSVAPIEPGSLQSRSRSHLLKFEYGDDHQNLGAQLRTLDNKIGSRKIENRNYQVNYNFNNNSYLDLNLMAAHNIGKTIYPKGGFFAGWQVADKLITKNVANIVDINNSHTFLLPKEIDLKTTLGFNYFTNEYSKNRFPEELSLFYNDASHDQGLYSHSKRGRYSGTKSLLPQRSVILQPSGKQKFKTVYFDTALSKGIYHLNYSVNFTHYAFNGEYVGYENTAGQQINEPILHKSGHKKAFNHSATLSAELSDYFMPFFTYSRTHRMPNIQEMFFSQVSNAGVNTALKPEQSDTYQLGFNTYKKGLFTQDDVLGVKLVGYRSFIKNYIHNVYGVWWRDGMPTWAESNGFKYTIAHQNYKPIVKKSGVELEINYDMGRFFANVSYAYQRTNQPTNYADASPRPNNASQEDILKQGYGLSRVSMLPKDYGRLELGTRWFDQKLTLGLAARYYGKSKRATIEEEYINGSRFKKNTLRRENYYAVKKTEDIKKQPIILDLHVSYEPIKDLIIKAEVQNLLDKRYVDPLDAGNDAASQRYYSSLNNSIECAQDSSACGGSDKTVLYNFARGRTYILSLNYKF

Function: Probable receptor, TonB-dependent. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 102768 Sequence Length: 913 Subcellular Location: Cell outer membrane

Q57251

MLSFILSIFPIVLLIYLMVKRNALPSYVALPWVATLVMGVHLLHFNTDIVTISANVVSAIIAVQTPITVIFGAILFNRFSEISGATNIMRKWLGNINPNPVAQLMIIGWAFAFMIEGASGFGTPAAIAAPILVGLGFHPLKVAMLALIMNSVPVSFGAVGTPTWFGFGALKLSEDMILEIGSITAFIHSIAALIIPLLALRILVNWDDIRKNIVFIYISVLGCVVPYFLIAQVNYEFPSLVGGAIGLFISVWAANRNIGLAKVTNTLDNNAVSAGEVVKALFPTGLLIAFLIVTRIHQLPFKAMMNDATIWFSTTLGSLGLFEISKGLIFSLKNIFGSNVSSSYKLLYVPALIPFVITVLIAIPFFKISSSNVKQILVSSLQQSKNPFIALIGALVMVNLMLVGGEHSMVKIIGRTFAEISGSNWTIFSSFLGAIGSFFSGSNTVSNLTFGSVQLSTAETTGISVALVLALQSVGGAMGNMVCINNIVAVSSVLNISNQEGTIIKKTIIPMIIYGIIAALGALFLVPLFYNL

Function: May play a role in L-lactate transport. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 56885 Sequence Length: 532 Subcellular Location: Cell inner membrane

Q57223

MKVYKSFLIATASLFLFACSSFQNDDYAMNYKGQIGEPIMAIAMLSEQQHEWAGTPYVLGGVSRRGVDCSGFVQKTFFDRFNLRLPRSTVEQANYGKHVRKEDIQTGDLIFFKTGRGPNGYHVGIYVKEDKFLHASTRGGVVYSSMNNPYWSKAFWQVRRI

Location Topology: Lipid-anchor Sequence Mass (Da): 18388 Sequence Length: 161 Subcellular Location: Cell membrane EC: 3.4.-.-

Q58774

MKTLSEIKEILRKHKKILKDKYKVKSIALFGSYARGEQTEESDIDIMVEFDENNYPSFSEYLELIEYLEKILGLKVDLITKKSIHNPYVKKSIEEDLIYV

Cofactor: Binds 2 Mg(2+) ions. Function: Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Neutralizes cognate toxic MJ1380 by di-AMPylation. Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein] Sequence Mass (Da): 11819 Sequence Length: 100 EC: 2.7.7.108

P45268

MEIISQYGSWLVWITAVFGFFMAFGIGANDVSNSMGTSVGSGTITAKQAIIIALIFESAGAYLAGGEVTQTIKSGVIEPIQFVDTPDILALGMLSTLFASGAWLFIATKMGWPVSGTHTIIGAIIGFACITIGPSSVDWSKIGSIVGSWFVTPVIAGILAYAIFASTQKLIFDTEQPLKNAQKYGPYYMGITVFVLCIVTMKKGLKHVGLNLSNSETLIISLAISLIGMFFFHFYFKSKIFTQSANKGTFGAVEKVFSILMLLTACAMAFAHGSNDVANAIGPLSAVVSIVNEGGKIVSGGALTWWILPLGALGIAVGLITMGQKVMATVGSGITDLTPSRGFAAQFATAMTVVVASGTGLPISTTQTLVGAILGIGFARGIAALNLTVIRNIISSWIVTLPAGAFFAIIIFYVLRTIFN

Function: Potential transporter for phosphate. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 44026 Sequence Length: 420 Subcellular Location: Cell inner membrane

Q9HPH7

MIETTTLRFSHGDTTVLDGVDFTAETGDVTVLFGRNGAGKSTLLRHFNGLLEPDAGTVSVGGTPIAYDDDSLTELRLRVGLIFQNPDDQLVAPTVQQDIAFGPRNAGIEDTDRIEDVVSTFDLSEQAERLCNTLSGGEKKRVSLAGVLAMDPEYVLLDEPTAGLDGAGCRTIVEFVSSLAADGITTVIATHDVGFGLTVADTVTVLEDGVIDYRGDTLSQSLAAEYDLRSYVFDDWSDVSVE

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 25844 Sequence Length: 242 Subcellular Location: Cell membrane EC: 7.-.-.-

Q59026

MLNTLMLREWLRSMLRSCISKIFGDLMLISHISLSDKITLLTYGCNFKCKYCFFKPLSCKKYSVDEILNKILEVNENYKLDKILIAGGEPTLQNDLSELTKLLKDEGFYLMLSTNGYYLKDMLDKLEVDEIHIDLKAYDENKHIYLTSCSNKKVLDCISYIGKYRDEFNFKVEIDTVLIPNIVDLDEIEKIAKFLSNWDLPYRITGYVKYNNNLNAEKPDEDKILKAKEIALKYLSNVSCSLDFKRHKKSKKVII

Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Catalytic Activity: glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+) + L-methionine + semiquinone [flavodoxin] Sequence Mass (Da): 29795 Sequence Length: 255 EC: 1.97.1.-

C0LGH8

MRSKYFCSLALVLGLFFVSCDGFASNEVQALRRFKEAIYEDPLLVMSNWNDPNSDPCDWTGIYCSPSKDHVIKINISASSIKGFLAPELGQITYLQELILHGNILIGTIPKEIGNLKNLKILDLGNNHLMGPIPAEIGSLSGIMIINLQSNGLTGKLPAELGNLKYLRELHIDRNRLQGSLLVAGASGYQSKVYSSNSSANIAGLCKSLKVADFSYNFFVGNIPKCLENLPRTSFQGNCMQNKDLKHRSSSQCANAQLVKTHGSPSAAPKHQSAQMVAKHHRASKPKWLLALEIVTGSMVGLLLLVALFSAVHRWNNRSTLIIPWKKSSSEKEKFTVYVDSEMLKDVSRLTRQELEVACEDFSNIIGLSADSQIYKGTLKGGSEIAVISLCVKEEDWTGYLELYFQREVADLARLNHENTAKLLGYCKEISPFTRMLVFEYASNGTLYEHLHYGEAALVSWARRMKIVIGIARGLKYLHMELDPPFTISELSSNAIYLTEDFTPKLVDFECWKTILARSEKNLRNISSQGSICVLPNGMESRYLDVSGNIYAFGILLLEIVSGRPPYCKDKGFLIEWAKEFLEAPEAMSGLVDPELKHFNQEDLETVCEVASQCLNRDPTNNNNNHNKPSVQELCETLESRISLSISAELRSSSLAWAELALDS

Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 73910 Sequence Length: 664 Subcellular Location: Cell membrane EC: 2.7.11.1

Q8XJR2

MYIIFALLAFSALILVHELGHFIVAKLNGIYVEEFAIGMGPKLFGVKVGETEYNLRILPFGGFVKMLGEEDESDDSRSLNAKTPIQRILVMGAGAFMNYVLALIIFIGLAMSSGFAENKVASVVPNSPAQEIGIEQGDEFLKIDGNKIHTTDDFRMGLALAKGNPVELEIKRGNDVLTKTVQPILNESGMYQVGISYALVEKPTLLQGIKQGFNETRSLVSQSFIALKTIVTGEANLKTDVGGPVTIIKMSGQAAKAGANTLLWFMAFLSVQLAVFNLLPFPALDGGRIFIELIQMIIRKEIPAKYIEAVNTVGFMLLMGLMVLVTIKDIIFPIL

Location Topology: Multi-pass membrane protein Sequence Mass (Da): 36491 Sequence Length: 335 Subcellular Location: Cell membrane EC: 3.4.24.-

Q8TYV9

MTHEYPDGTCAVCGLSLRVKEGESVVVLGPNGSGKTTLLHHILGLLTPTKGHIRVLGHDLPDGVREVRKRIGVVFQDVDDQLIMPTVLEDVAFGLVNRGMPREEAFERAREILERLGIEDLEDRPPQFLSGGQKRLVALAGAVAPEPDLLILDEPTSGLDFRATRLFVRLIRELKEELGFTMILTTFDVDIAAALAERVVVIREGKTVAEGSPEDILTDVDLIRESGLKPPEHVELLRRLGIENPPLDISEAEELLVAMLGEESRGNP

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 29422 Sequence Length: 268 Subcellular Location: Cell membrane EC: 7.-.-.-

Q0V7T5

MCLLRHLLPIWVLLGFFFFSTATKSQESSVVYVSGASPEIPISQASPRMGAQSPGPPIVKVVLRQDLNKKILIALIVSSSLLCVTVMFLVYLLLWRYRNMKNSFTGIKRKSDSVKSVTTKPTVHKIDSVRKGTIPVYEYQLLESATNKFSDSNVLSRGGRGCLYRACLDEKSSVTVKKLDGGGETDIEKQFETEVDWLAKIRHQNIVSLLGFCVYRQTSCIVYELMQNGSLESQLHGPSQGSGLTWQLRMKIAVDIARGLEYLHEHCHPPVVHRDLKSSSILLDSDFNAKISDFGFATVLTTQNKNLIHKASEDLLDGKVTDKNDVYSFGVILLELLLGKKSVEKPSSEPESIVTWAVPKLSDRANLPNILDPAIKGTMDLKHLYQVAAVAVLCVQPEPSYRPLITDVLHSLIPLLPVELGGSLRIL

Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 47373 Sequence Length: 427 Subcellular Location: Cell membrane EC: 2.7.11.1

Q86JM5

METIQSVITEWSDSKSWDHLFQHNFKDSNWSELFDPVNFKFKFGTTPFSQFQILPSVISLYLVIIFSIKFLMRNRKPFSLKYVSILHNAILCIWSLVMCVGILYEVIKRITAEGPLFTVCETVSGFDKGPAYYWSYIFYISKFYELLDTVIIVLKKKPLIFLHVYHHCIVVWLCWYFMYSGWNLQLWVVFLNTFVHVFMYYFYFQTGRGKTVWWKKYITMIQIIQFICLGIAGLLHSAAINLNSSPCFTHYPAFISAYLINFSFLFLFSQFFVKSYSNKPTSSSSTTTPTKTKKID

Function: Could be implicated in synthesis of very long chain fatty acids. Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA Location Topology: Multi-pass membrane protein Sequence Mass (Da): 34929 Sequence Length: 296 Subcellular Location: Membrane EC: 2.3.1.199

O22891

MATETNKELFVGGFAKILKEQRQVDVRLKAGDSGDEGASTSAHKLVLSARSEVFKKMLESDEIKASAQLETITLCEMKHEELEAFIEFIYSDGSMLSAKEKQHVRSLYIAGDKYEIPHLRDLCRIELISSLKSSNALDILELAQIPFDKALHDSAFFFFFFFFFG

Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Sequence Mass (Da): 18683 Sequence Length: 165 Domain: The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes. Pathway: Protein modification; protein ubiquitination.

C0LGK4

MVDQRRSALGFVLLLLCLVLFFDCVVVGQTQSRFSEKLILLNLRSSLGLRGTDWPIKGDPCVDWRGIQCENGSIIGINISGFRRTRIGKLNPQFSVDPLRNLTRLSYFNASGLALPGTIPEWFGVSLLALEVLDLSSCSVNGVVPFTLGNLTSLRTLNLSQNSLTSLVPSSLGQLLNLSQLDLSRNSFTGVLPQSFSSLKNLLTLDVSSNYLTGPIPPGLGALSKLIHLNFSSNSFSSPIPSELGDLVNLVDFDLSINSLSGSVPQELRKLSKLQLMAIGDNLLSGTLPVDLFSAESQLQTLVLRENGFSGSLPDVCWSLPKLRILDIAKNNFTGLLPYSSYDSDQIAEMVDISSNTFYGELTPILRRFRIMDLSGNYFEGKLPDYVTGENVSVTSNCLRNERRQKPSAICAAFYKSRGLDFDDFGRPNLTQPTSKNASSGISRRTVIILAAVGGGVAFILLFVILPIILVLCMRHRRRAAQRGNNDRPKPAGEASQQPPKGAQTFDLSRLGNAFSYEQLLQATEEFNDANLIKRGHSGNLFRGFLENGIPVVIKKIDVREGKSEGYISELELFSKAGHQRLVPFLGHCLENESQKFLVYKFMRHGDLASSLFRKSENEGDGLKSLDWITRLKIALGAAEGLSYLHHECSPPLVHRDVQASSILLDDKFEVRLGSLSEAYAQGDAYQSRISRLLRLPQSSEPSSSGVTNAICSYDVYCFGKVLLELVTGKLGISSPDNALAKEYMEEALPYISTNEKELVTKILDPSLMVDEDLLEEVWAMAIIAKSCLNPKPTRRPLMRHIVNALENPLKVVREDTNSGSGSSRLRTNSSRGSWNAAIFGSWRQSASDVTAVQAGATTSGGGGGGGGNGLRNSGSQGSSGRNNNNNGNSSSSRRRQSSEIVPEPAAYGVVEDNL

Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 99704 Sequence Length: 915 Subcellular Location: Membrane EC: 2.7.11.1

C0LGL4

MEGRRQRLLVFIFGALAITHLVQAQPPDQRGFISLDCGLPVNESPYTDPRTGLTFSSDADFILSGLRGEAGDDNTYIYRQYKDLRYFPDGIRNCYNLKVEQGINYLIRAGFGYGNYDGLNVYPKFDLHVGPNMWIAVDLEFGKDREIIYMTTSNLLQICLVKTGSTIPMISTLELRPLRNDSYLTQFGPLDLIYRRAYSSNSTGFIRYPDDIFDRKWDRYNEFETDVNTTLNVRSSSPFQVPEAVSRMGITPENASLPLRFYVSLDDDSDKVNVYFHFAEIQALRGNETREFDIELEEDIIQSAYSPTMLQSDTKYNLSPHKCSSGLCYLKLVRTPRSTLPPLISAIEAFKVVDFPYAETNPNDVAAMKDIEAFYGLKMISWQGDPCVPELLKWEDLKCSYTNKSTPPRIISLDLSSRGLKGVIAPAFQNLTELRKLDLSNNSFTGGVPEFLASMKSLSIINLNWNDLTGPLPKLLLDREKNGLKLTIQGNPKLCNDASCKNNNNQTYIVPVVASVASVLIIIAVLILILVFKKRRPTQVDSLPTVQHGLPNRPSIFTQTKRFTYSEVEALTDNFERVLGEGGFGVVYHGILNGTQPIAVKLLSQSSVQGYKEFKAEVELLLRVHHVNLVSLVGYCDEESNLALLYEYAPNGDLKQHLSGERGGSPLKWSSRLKIVVETAQGLEYLHTGCKPPMVHRDVKTTNILLDEHFQAKLADFGLSRSFPVGGETHVSTAVAGTPGYLDPEYYRTNRLNEKSDVYSFGIVLLEIITSRPVIQQTREKPHIAAWVGYMLTKGDIENVVDPRLNRDYEPTSVWKALEIAMSCVNPSSEKRPTMSQVTNELKQCLTLENSKRGVREDMGSRSSVEMSTSFTTEINPKAR

Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 98965 Sequence Length: 880 Subcellular Location: Membrane EC: 2.7.11.1

Q9KXJ6

MIRFEDVSVTYDGATEPTVRAVDFEVPEGELVLLAGPSGVGKSTVLGAVGGLVPHFTGGTLRGRVTVAGRDTRTHKPRELADVVGTVGQDPLSHFVTDTVEDELAYGMESLGLPPDVMRRRVEETLDLLGLSDLRSRPIATLSGGQQQRVAIGSVLTPHPDVLVLDEPTSALDPAAAEEVLAVLQRLVHDLGTTVLMAEHRLERVIQYADQVVLLPAPGEAPLIGAPAEVMAVSPVYPPVVGLGRLAGWSPLPLTIRNARRRAAPLRERLAGREIPDHTPPPSAPLPAPPAPRPVTSRWRRRGKRPENPSAPTPYAAEVRSLAVRRDRVQALRHVDLTVSPGETVALMGRNGAGKSTLLSALVGLVEPSAGSVRAGDAVPHRTAPRDLVRRVGLVPQEPRDLLYADTVAAECAAADRDADAAPGTCRALLSELLPGITDDIHPRDLSEGQRLTLALSVVLTARPPLLLLDEPTRGLDYAAKARLAGILRGLAAEGHAIVLATHDVELAAELAHRVVLLAEGEVIADGPAADVVVASPSYAPQVAKVLAPRKWLTVAQVREALT

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 59587 Sequence Length: 563 Subcellular Location: Cell membrane EC: 7.-.-.-

O30238

MRRERYLEKIEYIVEALSEIPERVKTPIEVSGVFYNLLTSIESAMDISAMLVKDLGGRVEDDYSNVEMLKELGIIDEELAEGLKKCNGLRNWLVHRYNRVDKELVLSSVEEVKALLLKFIQRVEDVLEKIEP

Function: Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin AF_2432. Neutralization may be due to AMPylation by AF_2432. PTM: Modified by cognate antitoxin AF_2432; probably at least 2 successive AMPylation events occur on Tyr-97. Sequence Mass (Da): 15298 Sequence Length: 132 EC: 3.1.-.-

Q7A342

MTEPIISFKDFSFQYHSQATPTLQNINVDIYPGEKVLVVGASGSGKSTFANCINGLIPFKTKGNITGELYINNQDATVSCLHDRSNVVGTVLQDTDGQFIGLTAAEDMAFLLENNCVEQDDMKKNVSYWAEKVGMIEHLNHRPQDLSGGQKQRVSLGGILIHRTPILILDEPLANLDPATGHETLRLLNNIHEETKSTMIIVEHRLEESLDDTFDRVLLFKDGKIIANTTPSDLLKSSKLKEAGIREPLYCTALKYAEVDVESIDNLANLRDVCMSEHVKFKVKKWIDETSANNDNKYKSEPLLELNEVCVQYSDYSNSVLNNVQLNVYRREMLSIVGHNGAGKSTLAKAICGFLDITGNIQFCNRGFNQLSISERSEFVGYVMQNPNHMISEKMIYDEVALGLRARGMKESDIKIRVENVLKICGLYAFRNWPIAALSYGQKKRVTIASVLVLNPEIIILDEPTAGQDFYHYNEIMSFLIELNRQGKTIIMITHDMHLLSEYSSRTVVLSKGQVVADTTPVLILNDKKICEIASLRQTSLFEMAEYIGISEPQKLVQLFINHDRKVRRQ

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 64158 Sequence Length: 570 Subcellular Location: Cell membrane EC: 7.-.-.-

P9WL78

MRWARQAVAVNGMPVDDGALPGLQRIGLVRSVRAPQFDGITFHEVLCKSALNKVPNAAALPFRYTVNGYRGCSHACRYCFARPTHEYLDFNPGTDFDTQVVVKTNVAAVLRHELRRPSWRRETVALGTNTDPYQRAEGRYALMPGIIGALAASGTPLSILTKGTLLRRDLPLIAEAAQQVPVSVAVSLAVGDPELHRDVESGTPTPQARLALITAIRAAGLDCHVMVAPVLPQLTDSGEHLDQLLGQIAAAGATGVTVFGLHLRGSTRGWFMCWLARAHPELVSRYRELYRRGPYLPPSYREMLRERVAPLIAKYRLAGDHRPAPPETEAALVPVQATLF

Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 37176 Sequence Length: 340 Subcellular Location: Cell membrane

O82343

MRGSNNTDLFDPKTEMDSNFSRHGSSSEGDFGFAFNDSNFSDRLLRIEILGGPSDSRSDAEGCTSIADWARHRKRRREDNKKDNGVAISDIVACAEEQILTDNNQPDMDDAPGGDNLDDEGEAMVEEALSGDDDASSEPNWGIDCSTVVRVKELHISSPILAAKSPFFYKLFSNGMRESEQRHVTLRISAQEEGALMELLNFMYSNSLSVTTAPALLDVLMAADKFEVASCMRYCSRLLRNMPMTPDSALLYLELPSSVLMAEAVQPLTDAAKQFLASRYKDITKFHDEVMALPLAGIEAILSSDDLQIASEDAVYDFVLKWARGQYSSLEDRREILGSRLALYIRFPYMTCRKLKKVLTCSDFEHEVASKQVLEALFFKAEAPHRQRILAAEGSDSMNRRFIERAYKYRPVKVVEFELPRPQCVVYLDLKREECAGLFPSGRVYSQAFHLGGQGFFLSAHCNMDQQSSFHCFGLFLGMQEKGAVSFGVDYEFAARDKSTKEEYVSKYKGNYTFTGGKAVGYRNLFGIPWTSFIAEDSQHFINGILHLRAELTIKRSSDLH

Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Sequence Mass (Da): 63037 Sequence Length: 561 Domain: The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes. Pathway: Protein modification; protein ubiquitination.

P77868

MLDLTPQSKKISIQIGGMTCQSCANRIEKVLNKKPFVQQAGVNFAAEEAQVVFDATQASEAQIIEIIHKTGFSAHIKQANELPIEENTSIPWRLIVLWIINIPFLIGMLGMIGGSHNLMLPPIWQFALASIVQLWLAIPFYRGAIGSIRGGLTNMDVLVSTGTLTIYLYSAFMLFYHANHAMGHVYFEASVMVIGFVSLGKFLEDRTKKHSLNSLSMLLQLTPKKVTVLRNEKWIEIALDQVNIGEIIRANQGERIAADGVIESGNGWCDESHLTGESRPEEKQKGGKVLAGAMVTEGSIIYRANQLGSQTLLGDMMNALSDAQGSKAPIARFADKVTSVFVPVVLVISLVTFALTYILTNDSVSSLIHAVSVLVIACPCALGLATPAAIMVGLGKAVNAGVWFKDAAAMEETAHVDTVVLDKTGTLTKGELEISALWQPQSAVYSEDDLYRFAAAVERQANHPIAKAIVQAAEXKMLEIPTALFSKMEVGQGIQAELEQVGTIKVGKPDYCGLILPKNLEDIWQIASIVAVSINDEPIGAFALTDTLKNDSLHAIQRLQQQNIDVVIMSGDQQSVVDYIAKQLGIKKAFGKLTPRDKAEQIQKLKDLGHIVAMVGDGINDAPALASANVSFAMKSSSDIAEQTASATLMQHSVNQLVDALFIARATLKNIKQNLFFALIYNILGIPLAAFGFLSPIIAGAAMALSSISVLMNALRLKKVRF

Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Location Topology: Multi-pass membrane protein Sequence Mass (Da): 78072 Sequence Length: 722 Subcellular Location: Cell membrane EC: 7.2.2.-

P9WKA9

MAQLTALDAGFLKSRDPERHPGLAIGAVAVVNGAAPSYDQLKTVLTERIKSIPRCTQVLATEWIDYPGFDLTQHVRRVALPRPGDEAELFRAIALALERPLDPDRPLWECWIIEGLNGNRWAILIKIHHCMAGAMSAAHLLARLCDDADGSAFANNVDIKQIPPYGDARSWAETLWRMSVSIAGAVCTAAARAVSWPAVTSPAGPVTTRRRYQAVRVPRDAVDAVCHKFGVTANDVALAAITEGFRTVLLHRGQQPRADSLRTLEKTDGSSAMLPYLPVEYDDPVRRLRTVHNRSQQSGRRQPDSLSDYTPLMLCAKMIHALARLPQQGIVTLATSAPRPRHQLRLMGQKMDQVLPIPPTALQLSTGIAVLSYGDELVFGITADYDAASEMQQLVNGIELGVARLVALSDDSVLLFTKDRRKRSSRALPSAARRGRPSVPTARARH

Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis. Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA Sequence Mass (Da): 48847 Sequence Length: 446 Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis. EC: 2.3.1.20

Q576D9

MNARLTGLGLNLLSFAVGIGGWYLLTATGAVVLPGPVDVLERAVTLLLNGQLVGDIFASLRRVLSGFVLGVALAIPVGFLMGWYRIARSLIEPWVQFFRMIPPLAVIPLAIVTLGIDESPKIFVIFLASFLSSVVATYQGVISVDRTLINAARVLGAKDATIFARVIVPASVPFILVGVRIGLGSAWATVVAAELIAAQSGLGYRMQQAQLYYDLPTIFVSLVTIGILGLFMDRLLQAADRRLTQWQERA

Function: Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (Probable). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 26895 Sequence Length: 250 Subcellular Location: Cell inner membrane

Q9FYC8

MSPVAKVSEFHREGNDWFCKTGLSSDITVVVDDVKFHLHKFPLVSKCGKLARMYEDSKSTDKQSLWTTVLEEFPGGADNFLIVARFCYGARVDITSKNLVSIHCAAEYLEMTNEYGEDNLISQVETFLHKHVLRNWKDCILALQSSSPVLKSAEKLQMIPKLMNAVSTMVCTDPSLFGWPMMMYGTLQSPGGSILWNGINTGARMRSSGSDWWYEDISYLSVDLFKRLIKTMETKGIRAESLAGAMMYYARKYLPGLGRWQSGTSDSSKSRRRVVSFNLAKASSPSSMPPLDQIALLETILSLLPEKRGRSFCKFLLGLLRVAFILGVDGNCVKKLEKRIGMQLELATLDNLLILNYSDSETLYNVDCVERIVRHFVSSLSSSSSQLPEFSPPSLDPVTSPSPAPLKKVANLVDSYMAEVASDVNLKPDKMRSLAAALPESSRPLYDGLYRAFDIYFKEHPWLSDRDKEQLCNIMDYQRLSIDACAHASHNDRLPLRVVLQVLFFEQMHLRTALAGGLNVANTETAHAVTIPGGRTGQEIVQRDGWVTVVRQNQVLKVDMQKMRSRVGELEEEFQSIKQEMKKRVSKSSSSMSSPRLVKLGCKFLLPRASDAKNDTVQNSVSSTPRSATADHTLPRSSRHSKHRKSFSFFG

Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Sequence Mass (Da): 72965 Sequence Length: 651 Domain: The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes. Pathway: Protein modification; protein ubiquitination.

Q54QU8

MENFKNNELESSPIINKNNSSHSINNEDNNYYSHNLEHNDNNNNDNNNTITNSHINNHDHKHNHEHEHKHKHNHDHNHDHDHNHEEEYGHGNELEHNNDQEHNVGNKNLLTNNNNQSKKKKHGHSHGGGEDGSSSGGGGGRHGHGHSHGGGSGSDHNHGSSDEDDEESKPLNQLRNLDSKKKARYSLILALTLTTIFMVGEIVGGYFANSLAIMTDAAHLLTDIGAMFLSLFAMWISQHPPTSSMSFGFHRAEILGALVSVLMIWALTGVLVYEAIQRILYPPDAVDGKIMFIIASCGLFINIIDAIILHWGSGGHGHSHGGGHGHSHGIGGGTQKKKSKKNRLLNNQGQDIEDLGGENGKNKKGVRNINVHSAYIHVLGDCFQSIGVMVASCIIWVHPHWKIADPITTLIFSVIVLGTTIKLLRESLGVLMEGVPPEIDVSEVKGDLSEIEGVTEVHDLHIWSITLGRPALSVHLTILPTIDPEEILSIANKILLEDYEINHTTIQIEKPLVKDKCKDHSCPPPKPKKKKIKNDNLSSPPNQ

Function: May be involved in zinc transport from the cytoplasm to either intracellular organelles or extracellular spaces. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 59836 Sequence Length: 543 Subcellular Location: Membrane

Q9T020

MEIRKKPNIFTVLVIDFSSKPSMALLLAILLFLSGPSASAVAAAAVGPATGFKPADDILIDCGSKSSSKTPDGRVFKSDQETIQYIEAKEDIQVSAPPSDKVASPIYLTARIFREEATYKFHLTRPGWHWVRLHFLAFPNDKFDLQQATFSVLTEKYVLLHNFKISNNNNDSQAAVQKEYLVNMTDAQFALRFRPMKSSAAFINAIEVVSAPDELISDSGTALFPVIGFSGLSDYAYQSVYRVNVGGPLIMPQNDTLGRTWIPDKEFLKDENLAKDVKTTPSAIKYPPEVTPLIAPQTVYATAVEMANSLTIDPNFNVSWNFPSNPSFNYLIRLHFCDIVSKSLNDLYFNVYINGKTAISGLDLSTVAGNLAAPYYKDIVVNATLMGPELQVQIGPMGEDTGTKNAILNGVEVLKMSNSVNSLDGEFGVDGRTTGMGKHGMVATAGFVMMFGAFIGLGAMVYKWKKRPQDWQKRNSFSSWLLPIHAGDSTFMTSKGGSQKSNFYNSTLGLGRYFSLSELQEATKNFEASQIIGVGGFGNVYIGTLDDGTKVAVKRGNPQSEQGITEFQTEIQMLSKLRHRHLVSLIGYCDENSEMILVYEFMSNGPFRDHLYGKNLAPLTWKQRLEICIGSARGLHYLHTGTAQGIIHRDVKSTNILLDEALVAKVADFGLSKDVAFGQNHVSTAVKGSFGYLDPEYFRRQQLTDKSDVYSFGVVLLEALCARPAINPQLPREQVNLAEWAMQWKRKGLLEKIIDPHLAGTINPESMKKFAEAAEKCLEDYGVDRPTMGDVLWNLEYALQLQEAFTQGKAEETENAKPDVVTPGSVPVSDPSPITPSVTTNEAATVPVPAKVEENSGTAVDEHSGTAMFTQFANLNGR

Location Topology: Single-pass membrane protein Sequence Mass (Da): 96505 Sequence Length: 878 Subcellular Location: Membrane EC: 2.7.11.-

Q97SA3

MKEAIIEWKDFSFRYETQQEPTLQGIDLTIYKGEKVLIVGPSGSGKSTLGQCLNGIIPNIYKGQTYGEFLIKGQVAFDMSIYDKSHLVSTVLQDTDGQFIGLSVAEDLAFALENDVTALDEMKGRVYKWAEKLDLLPLLDQRPQDLSGGQKQRVSLAGVLIDESPILLFDEPLANLDPKSGQDIIELIDQIHKEEGTTTLIIEHRLEDVLHRPVDRIVLINDGRILFNGSPDQLLATDLLTQNGIREPLYLTTLRQLGVDLVKEEQLANLDNLSISKGQVQLQNELAKETPALQSLFRLEEVSFSYDDRPILKSLHLDIKKGEKIAIVGKNGAGKSTLAKAISSFIQTEGRYLWEKQDIKGDSVAERAERVGYVLQNPNQMISTNMIFDEVALGLRLRGVDEKEIETRVYETLKICGLYEFRNWPISALSFGQKKRVTIASILVLGAEIILLDEPTAGQDQKNYTEIMEFLEELHQKGHTIVMITHDMQLMLDYSDRVLVMVDGELIADTVPASLLSDPELLVKANLKETSIFNLAKKLDVDPLDLTAFYKERREGCKLN

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 62873 Sequence Length: 560 Subcellular Location: Cell membrane EC: 7.-.-.-

Q92IC3

MSKSKAIENNGISNTNSPNGKYMAPRPEGVKPTCVVITYSVSKDIKAVREVLDERGASVHYIIDKDGTQKEYHNDLTDQAFYAGKSSWKGEVGVNKFGIGVMLINDAKSDFPAEQIGKLKEFLKDVTERYPNLDLKHDLVGLGEVTVNREGNAHIAPGSKFPWKELAEAGFGRYFETTQEQKSKLLLSLDSTGEKVNTLQENLKEYGYGVESTSTFDQFTQQAVRVFNDRYGTGLPNEEPPVSWTEAGQDVLSQLLGQTVLEQTENA

Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Sequence Mass (Da): 29592 Sequence Length: 267 Subcellular Location: Secreted EC: 3.5.1.28

P55569

MTKTIIDQAGATPGAIRTREGLVSAYRTELAIAGAIVLLVLAVGTQVPQAMSWGNFANITQAGAPLIIMSLGVLLVVITGGIDLSVGSVFSLTGMVTAQAMASGLDVSAALIGLGVGLVFGSINGFLVTVAGLAPFVVTLITFAVAGSLAFIVTNGRSMPIGDPDFWLLNSGSLIPGVPNYILFCIVLLVVIEIFLKKMVAGRWFYAVGSSAAAARLLGIPVKRTQFFAYVASSLLASFSGLLTISYILNAESTAGSSLMLQAIAAVVIGGASLLGGTGTAVGAVLGALMITVIQNGVNLIGINSFWQGSVTGLAILIAVLIDRFSKSRRGAV

Function: Probably part of the binding-protein-dependent transport system y4mIJK. This system probably transports a sugar. Probably responsible for the translocation of the substrate across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 33907 Sequence Length: 333 Subcellular Location: Cell inner membrane

P55570

MTDASKDIVSVRSLTKSYGATVVLKGVDFSVARGEIHALLGGNGAGKSTLIRVITGTAAKDGGELVFRDMAGNILTEADGRRKVAVVHQELALLPHLTVAESIALPHFRKGSRVYDGRTAGSQAYAALSMIDRDFAGTALNRLVGDLSLHEGQMVEIARALSSGAELILLDEPTANLTAAETERLFGVLRKLTRGNGLSVVFVSHRMKEIRQIAHVCSIIRDGRTVVGNVPTAELSDLAIIEHMGQAQATAVAHSARPAPVASLSDEPLTIAETGFSVTLQPGTILGVAGAPAGPETLIAALIGAAHERRWTVTRAGWPDRFRSPREAARLGAGFVTGDRSHRGILHSLPIIDNVLASRRATRGSLFATKREEVECLDLMQALKVKAGSLWHLPNTLSGGTQQKLLLARWLNVPSRLLVLEEPTRGVDIGTKREIYQLIRDMATTGTAIVWWSTENAELLEICDQVLAFDTEGRSSGVIERDELSEDKLATLTGMAA

Function: Probably part of the binding-protein-dependent transport system y4mIJK. This system probably transports a sugar. Probably responsible for energy coupling to the transport system. Location Topology: Peripheral membrane protein Sequence Mass (Da): 53193 Sequence Length: 497 Subcellular Location: Cell membrane

P55572

MTKTVTRAGGASGPQQFQSGGETMKYEITRRRFLAASSAVLAAPAIVTMVRPARAGTTLTLGHGAAPGNPRTVAAAKFAELVAEKTAGRVTINVAGAETLGSDAAMLTSLRTGALDVTANSQGATSALVPELAALGLPFLFENTAKAMQVLGGPVGAELVKRFEAVGVVPLDWWDNGIRHLTNSKRKVAAPAEVSGMKIRTPADPMTMDIFQALGAATEQIAFGELYVALQQGVVDGQENPLANIDSSKLYEVNKYISLTGHKWESTPFLMSQIAQARLGGDLEAVKAAAKEAGELQRKLSADKDAEVLAAFRRISAIEVTEVDREGFAKATASVVESRRSPSGISSPRSNRQPKAEALSAREHPMKSLSNLVELTARAIVWFARQVVIFSGIALMVFMTANVAARYVLAGGGFSFAQELPVLIFPWFILGGIVLAAHSGGHMAVEWIYDKLRDGARSTAFVAANLVSAGAFLMLGYQAYLVGEIAGIEHSPVLQLPNSVGYFALAVGSVLVAIVTLAVALRVLRLGWDHRTNTESGEVAL

PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 57124 Sequence Length: 541 Subcellular Location: Cell membrane

P55574

MAQIGHNISLPERARRIRRHALRMGEVQGQGYIAQALGIADVLAVAYFHATTYRPDDPEWEGRDRFLLSIGHYAIALYAALIEAKIIPEDELETYGADDSRLPMSGMAAYTPGMEITGGSLGHGLGIAVGMSLALKRKGSRSFVYNLFSDGELDEGSTWEAAMSAGSYKLDNLIGIVDVNQMQADGPSLGVLNFEPLGPKFEAFGWYVQRIDGNDIDALVDAFDNARQHRHPQPRIIICDTKMAKGVPFLEARERNHFLRVEPQEWAEAIRIIDAGVTA

Cofactor: Binds 1 thiamine pyrophosphate per subunit. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 30743 Sequence Length: 279 Subcellular Location: Cell membrane

Q87G35

MTIEFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGETSGTLTIYGQDTAPFDMHQYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLTSNIDMYPLVKATAKMVDLEQMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAALDPKTGKKTIEIIDDLHRETGKTIVIIEHRLEDVLHRSVDRIILMESGEIIADTTPDEILASPLLEDYGIREPLYISALKEAGCAIEGDAKPSSLTTLPLEQYKPTVQAWFDGSTAQPPKTPAETLLEVRGLTYSYDGEKNALEDVSFDIKRGEFVSVLGKNGSGKSTITKLIMGVIEADSGSMSMNGQDLNELTIFERSQKVGVVMQNPNHMISHHMIFDEVAFGLRNRGIKEKQIEAKVLEVLELCGLSKYRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLSFIEKLNRELGVTVMIISHDMHLVLEYTTRSIVIADSKLVADAPMTQVFSSPELLDQANLTTTSLFDLATKVGIEDTNGFMQHFINVEKAHRQQKSGEVNQPEKAVA

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 64053 Sequence Length: 579 Subcellular Location: Cell inner membrane EC: 7.-.-.-

C0LGV0

MLFWVLLSSFCVFCFSSPDGFLSLSCGGSSYTAAYNISWVSDNDYIETGNTTTVTYAEGNSTSSVPIRLFPDPQGRQCYKLPVRKDLSSVLIRATFVYRNYDSQNSPPAFHVSLGRRITSTVDLRTNDPWIEELVWPVNNDSLLLCLLAVKGRGIPVISSLEVRPLPLGSYKYSLEGSPDIILRRSYRINSGYTNGTIRYPSDPFDRIWDPDQSYSPFHASWSFNGLTKLNSFNITENPPASVLKTARILARKESLSYTLSLHTPGDYYIILYFAGILSLSPSFSVTINDEVKQSDYTVTSSEAGTLYFTQKGISKLNITLRKIKFNPQVSALEVYEILQIPPEASSTTVSALKVIEQFTGQDLGWQDDPCTPLPWNHIECEGNRVTSLFLSKINLRSISPTFGDLLDLKTLDLHNTSLTGAIQNVGSLKDLQKLNLSFNQLESFGSELEDLVNLEVLDLQNNSLQGSVPETLGKLKKLRLLNLENNNLVGPLPQSLNITGLEVRITGNPCLSFSSISCNNVSSTIDTPQVTIPINKKQRKQNRIAILLGVSGGALFATFLVFVFMSIFTRRQRNKERDITRAQLKMQNWNASRIFSHKEIKSATRNFKEVIGRGSFGAVYRGKLPDGKQVAVKVRFDRTQLGADSFINEVHLLSQIRHQNLVSFEGFCYEPKRQILVYEYLSGGSLADHLYGPRSKRHSLNWVSRLKVAVDAAKGLDYLHNGSEPRIIHRDVKSSNILLDKDMNAKVSDFGLSKQFTKADASHITTVVKGTAGYLDPEYYSTLQLTEKSDVYSFGVVLLELICGREPLSHSGSPDSFNLVLWARPNLQAGAFEIVDDILKETFDPASMKKAASIAIRCVGRDASGRPSIAEVLTKLKEAYSLQLSYLAASAHTD

Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 99613 Sequence Length: 895 Subcellular Location: Membrane EC: 2.7.11.1

R8NBR0

MLEKQNSEENIELLRAMRYCYNKSKIFYAVRISISILIPILSISIYLFNRGSTGTSNTGVWFSVIGSIWLLIAYQIEKLEGGYIEKGAKIQEKFDINLFNIRWNNVLVGNQISPEDIRDFSSKFKGDEEKLKNWYGGLSSKHFYVNVILAQRSNLMWAISLKRNFSILLFTVSVLYLFLTIAFGFFVNMSMQEYIIKILLPSMSILIYGFKTSDELKKQSNKLEALGNSIISKFDTGNLSEINASACREYQDAIFVYNRIRSILIPEWLYWLRQQKDDEKMIQINIRLTKKSNLF

Function: 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-B CBASS system . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 34347 Sequence Length: 295 Subcellular Location: Cell membrane

Q9LVM0

MMQFHFQFYVGPVFTLRPSKGFLSTCLVSFLFVTTTFCSYAIADLNSDRQALLAFAASVPHLRRLNWNSTNHICKSWVGVTCTSDGTSVHALRLPGIGLLGPIPPNTLGKLESLRILSLRSNLLSGNLPPDIHSLPSLDYIYLQHNNFSGEVPSFVSRQLNILDLSFNSFTGKIPATFQNLKQLTGLSLQNNKLSGPVPNLDTVSLRRLNLSNNHLNGSIPSALGGFPSSSFSGNTLLCGLPLQPCATSSPPPSLTPHISTPPLPPFPHKEGSKRKLHVSTIIPIAAGGAALLLLITVIILCCCIKKKDKREDSIVKVKTLTEKAKQEFGSGVQEPEKNKLVFFNGCSYNFDLEDLLRASAEVLGKGSYGTAYKAVLEESTTVVVKRLKEVAAGKREFEQQMEIISRVGNHPSVVPLRAYYYSKDEKLMVCDYYPAGNLSSLLHGNRGSEKTPLDWDSRVKITLSAAKGIAHLHAAGGPKFSHGNIKSSNVIMKQESDACISDFGLTPLMAVPIAPMRGAGYRAPEVMETRKHTHKSDVYSFGVLILEMLTGKSPVQSPSRDDMVDLPRWVQSVVREEWTSEVFDIELMRFQNIEEEMVQMLQIAMACVAQVPEVRPTMDDVVRMIEEIRVSDSETTRPSSDDNSKPKDSNVQV

Location Topology: Single-pass membrane protein Sequence Mass (Da): 71899 Sequence Length: 654 Domain: The protein kinase domain is predicted to be catalytically inactive. Subcellular Location: Membrane

A0R4H4

MADADVIVVGAGLAGLVAACELVERGHSVIIVDQENAANIGGQAFWSFGGLFFVNSPEQRRLGIRDSQELALQDWLGTAGFDRPEDHWPREWAHAYVDFAAGEKRSWLRARGLQTFPLVGWAERGGYDALGHGNSVPRFHITWGTGPALVEIFARRIRDSVRVRFAHRHRVDELIVNAGLVAGVRGSILEPSNAPRGVASSRKVVGDFEFRASAVIVASGGIGGNLELVRKNWPARLGRVPDQLISGVPAHVDGRMIGIAESAGAHVINNDRMWHYTEGITNYDPVWPNHGIRILPGPSSLWLDANGDRLPVPLYPGYDTLGTLEHICRSGQDYTWFILNARIIAKEFALSGQEQNPDLTSRNVRDLLSRVKPGAPAPVQAFVDHGVDFVSATSLRDLVAGMNDLPDVVPLDYAKVAAEVTARDREVANRFTKDGQITAIRAARNYLGDRFTRVVAPHRLTDPKAGPLIAVKLHILTRKTLGGLETDLDSRVLKEDGTTFGGLYAAGEAAGFGGGGVHGYRSLEGTFLGGCIFSGRAAGRGAAADIA

Function: Able to catalyze the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids, but the ketosteroid dehydrogenase activity is low compared to KsdD in the cholesterol degradation process. The low activity could be due to different substrate specificity. Sequence Mass (Da): 59024 Sequence Length: 547 Pathway: Lipid metabolism; steroid biosynthesis. EC: 1.3.99.-

Q9ASS4

MMMGRLVFVIWLYNCLCLLLLSSLVDADQANIDCLRTFKSQVEDPNRYLSTWVFGNETAGYICKFSGVTCWHDDENRVLSIKLSGYGLRGVFPPAVKLCADLTGLDLSRNNFSGPLPANISTLIPLVTILDLSYNSFSGEIPMLISNITFLNTLMLQHNQFTGTLPPQLAQLGRLKTFSVSDNRLVGPIPNFNQTLQFKQELFANNLDLCGKPLDDCKSASSSRGKVVIIAAVGGLTAAALVVGVVLFFYFRKLGAVRKKQDDPEGNRWAKSLKGQKGVKVFMFKKSVSKMKLSDLMKATEEFKKDNIIATGRTGTMYKGRLEDGSLLMIKRLQDSQRSEKEFDAEMKTLGSVKNRNLVPLLGYCVANKERLLMYEYMANGYLYDQLHPADEESFKPLDWPSRLKIAIGTAKGLAWLHHSCNPRIIHRNISSKCILLTAEFEPKISDFGLARLMNPIDTHLSTFVNGEFGDFGYVAPEYSRTMVATPKGDVYSFGVVLLELVTGQKATSVTKVSEEKAEEENFKGNLVEWITKLSSESKLQEAIDRSLLGNGVDDEIFKVLKVACNCVLPEIAKQRPTMFEVYQLLRAIGESYNFTADDDILIPSESGEGDFIEELIVAR

Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 69142 Sequence Length: 620 Domain: The protein kinase domain is predicted to be catalytically inactive. Lacks the conserved Asp active site at position 429, which is replaced by an Asn residue. Subcellular Location: Cell membrane

Q5L2C9

MATVDPIRYPIGTFQAPQQFEAGEVQEWIAAIRGLPSDLRTAVSGLNDEQLNTPYREGGWTVAQVVHHLADASMNAFLRTKWGVTEDGPTVKPFAESEWAKTADACLLPIEPSLLLLDGLHARWAALLESMTEADFHRTVRPEGAAGEMPLYVLTALYAWHGKHHTAQVASLRKRKGW

Cofactor: Binds 1 zinc ion per subunit. Function: Possible metal-dependent hydrolase. Sequence Mass (Da): 19713 Sequence Length: 178 Subcellular Location: Cytoplasm EC: 3.-.-.-

B1W5S5

MLLLISPDGVEEALACATAAEHLDIVDVKKPDEGSLGANFPWVIREIRAAVPADKPVSATVGDVPYKPGTVAQAALGAAVSGATYIKVGLYGCATPDQAIDVMRGVVRAVKDFRADAFVVASGYADAHRIGCVNPLALPDIARRAGADAAMLDTAIKDGTRLFDHVPPEGCAEFVRLAHEAGLLAALAGSVKAADLATLTRIGTDIVGVRGAVCEGGDRDAGRIQPRLVAAFRAEMDRHARAFAAAPAAS

Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P). Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate Sequence Mass (Da): 25746 Sequence Length: 250 EC: 4.2.3.153

Q54LH8

MTDKYNDWVKNKKHNNYNMAEDPLYYIKSNWVIERQLSKGSFGQVYKAHKKLDPNFVCAIKVIQYCKFTMKEVDYLKKLNDPKFVKYYSLEFNNSKTYAYIIMEFIEGESMKSIIENKKFSDIEIKEIIKELLKALVYLNDKGIMHRDLKPENIMFQNQNQNQNQNNKINLKLIDFGLSKAINENIINKTVKLQTISSVGTTLYMAPEILLNNKGSNSSLDIWSLGCIIVEMKWGLNQLCLQRPNNIPVFPVNSLFTEILNLCFQTEPSKRIKSHQLIKHPFFNDENEQFYNDNKEYFDFLKENERDSYIEIHNTESIGSNSTCSINEIRFENLYLIQSTYENQYPIKTITLHEKYTGISKLSHLNSKFKIIYLFLILLFLMTILVNLNRHVQTKFSIIQRDNIFLSITPESNPIKKPSPTQSSDYNQYSEGSQSSYESSSSSESSSESSSSESSSSESSSSSESQSSEINYSSNSNDLQPTDSSTTDPPVTDPPITDPPITDPPVTDPPITEPPVTETPKPTINPFFNTPVFICSQKIDQCLTVLNSQDLEFIDKKGRDQSMVLEYDGNAEQTFSIREKGGMYICLSGEHYHFSEKLKGRLNANKDGRDCTFNLITQFNIDKQANLYSFRSPNDQYIQSDETTRFISTKPGGLGSQSQFFIYFSHSLGPN

Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] Location Topology: Single-pass membrane protein Sequence Mass (Da): 77102 Sequence Length: 671 Subcellular Location: Membrane EC: 2.7.11.1

O29527

MIEAVDLHFCYGDAEVLKGVNFKAERGKVTVLMGRNGAGKTTLLKHLNGLLRPKSGKVIIDGRELKYDRKSLLEVRKRVFYVFQNPDDQILSPTVWQDVAFGPRNLGLKGERLERVVRNALEAVGLSGYEKRLCSTLSGGEKRRLAIASALAMNPDYCIMDEPSANVDGEGLRMIAEIIRKLREEGKGVVVSTHDADLAKEVGDYFYFMDDGKIVWEGEEFSYSVARKLGIRSFSLGKVILAESKIDDHPCFSADELERAVLKAFEGETVVVLGRDDWVIKELEKYPLEVERL

Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 32858 Sequence Length: 293 Subcellular Location: Cell membrane EC: 7.-.-.-

Q55624

MTEVLRVGQPAPDFTATAIVDQSFQTVKLSTYRGKYLVLFFYPLDFTFVCPTEIIAFSDRHSEFTALDTEVVGISVDSEFSHLAWIQTERKMGGIGNINYPLVSDLKKEISQAYNVLEPDAGIALRGLFIIDREGILQYATVNNLSFGRSVDETLRVLKAIRHVQSHPNEVCPVDWQEGDKTMIPDPEKAKTYFETVAEP

Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O Sequence Mass (Da): 22510 Sequence Length: 200 Subcellular Location: Cytoplasm EC: 1.11.1.24

Q8ES61

MNEKYPIGEFQFDGEITNIIINEWINEIEDLPRLLKNTVIDLNNEQLDTSYRSGGWTVRQVIHHLADSHMNAYIRLKLAITEENPVIKPYDEKEWAELYDYNLPIEISLSLIEALHKRWCSLLRDLSPTDMERTFKHPESGSISIGKNIGIYAWHGKHHLAHITSLCKRKDW

Cofactor: Binds 1 zinc ion per subunit. Function: Possible metal-dependent hydrolase. Sequence Mass (Da): 20166 Sequence Length: 172 Subcellular Location: Cytoplasm EC: 3.-.-.-