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Synthyra 8

B5TQ41

IFWLLTWVAEYFFKSKNNKQKHQFYECGFRALSELNIQINLNFSIVCVFLILYDVE

Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.2 Subcellular Location: Mitochondrion membrane Sequence Length: 56 Sequence Mass (Da): 6825 Location Topology: Multi-pass membrane protein

A0A3B6I0I8

MLRAAARLLIPRRLLSPAAATATPTVWNLRHFSLSTPQPRPAEAEIFTPAEAQRMVRLVGLEVLKRRLRNREDEVVTYQEFLDACVEAGAAPTHSRAEALAGAMDHSGTIVLFRGKVYLHPEKIVDLVRSAVPPVLEIENDTRREEFELLKKKKGEIDQQACKQVRRILWSGFWFVQATVGLCFRFTFWEFTWDVVAPITFFVAGAHLLSGYAYFLITSRKLSYRTYMERLFKIRRRELCTKHDFDMERYLEMERHMRCPLGGDYSQAATKAIFGEIERRMQDEVISHGEPLGALMESGLMPMEAEALVQKMDEMSLVLLVRGKTYLNHKKIVHLIRRAVPFALAAEDDVRKDEFRQLQMKMQEIDGMAHSHAVRILCFGFASFILQFALFFHLTFWEFSWSIMEPLAYFLAGLQLIFCYGYFLRTASNPTLQDFKRRLFLARRRKLCAKLSFDMDRYLNLQKHSRVPPEGDY

Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Subcellular Location: Membrane Sequence Length: 473 Sequence Mass (Da): 54954 Location Topology: Multi-pass membrane protein

A0A0Q3GYN7

MASDSRVAMMWCVLVLVLQSAGGGDMPCRREEQPEGERRAQGRLPQAQLSAGGVHCSGRGRQGPLREPGPRRGPDPHGLPRLLRPRLRRVGPPNFPSLRGFEVIDEAKSILERACPGVVSCADTLAFAARDSAYFLSRSRINYAIPSGRFDGNVSLESEALEFLPPPSFNLSQLVASFEAKKLDADDLVVLSGAHTIGVSHCSSFTDRLPPNNTSDMNPRLATLLQGQCPANPNFTDDTVVQDVVTPKLMDSQYYRNVLKKDVLFRYDAALLESRRTARKVLQNAFVRGRWERGSLRRPWSRCPGSSSRPPPMARSGECAGSSTANWVAACRLAISLKLTVDRTCTLLLPFRFLLQFSVMFCIAVVLVD

Cofactor: Binds 2 calcium ions per subunit. Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. EC: 1.11.1.7 Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O Subcellular Location: Secreted Sequence Length: 369 Sequence Mass (Da): 40583

A0A3Q9DD29

VTFINRWLFSTNHKDIGTLYLIFGAWAGMIGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALTQYQTPLFVWSVLITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVT

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 260 Sequence Mass (Da): 28150 Location Topology: Multi-pass membrane protein

A0A158PLD2

MSTAKQRYDAVRPRERVEFGGYRFVIPSLNFQMPKFLCCNGIHEGIMSEHHDENSFDLNECVSEVEDTSMYIIFSMFSINQGTLEHLVFQGFVFRMLCDIMLLCLDMHGQFRGFLKDDSDEFEDDVAALGEPLGQEVYRTLKEKFGFNSFRHRQKTTITAILLGHDAFVLMPTGAGKSLCYQLPAVLSDGVTVVVSPLKSLIEDQRLKMRDLGIPCEALTSDLSLSDQTVIYNRLMCSPPDIKLLYITPEKISASGRLASVFGSLHRRNFLARFVIDEAHCVSQWGHDFRPDYTKLQSLRRDYAEPKVQIVALTATATPKIVADTRDHLGIGDSKLFISSFVRTNLTYEIVLKAAKTFINVIQKMTQLYPGKAGIVYCLSREECEMVCTSLTNAGLNADVYHAGLPDKARLQVQHRWLRNTINVICATIAFGMGIDKPDVRFVIHYSLPKSIEGYYQETGRAGRDGQPAYCLLLYNYQDAIRLRKMIETPASVRAMHLQNIHQIVSYCENVSVCRRKILVEHFGEVYDAQMCLKSNTPCDVCQRLKRNPEGVKLFDVSDEAVLILTAMTKMRNITLRYLADLFRGQLGKKAAEQAARLGHTALPFYGRGVGMSEQDALRFMRKMVVEGYIVERLYRTKFESTVAYAELTNKSRQAIMGGAKPKQCLKHRRSKKSSLLFSMVRFFHTVVATVVCLRHMVKYGDVFARCLQSLTQLVTEIAEECNLSGPYAVISQDGLEQVAALLPRTNSDLVQVDSMTLRKVEKYGARVMATLKPFWKEVDGEICLLTPVGGALQHAWNRWLPPWPTKPSIPRGSVSLGG

Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate EC: 3.6.4.12 Subcellular Location: Nucleus Sequence Length: 819 Sequence Mass (Da): 92455

A0A2A6BKT1

MEMENGDPSSGTIRFEIDNISMLTNVGRYSEAVEVEGVPWRLFAQKLVEPDNKVYVFVFLAYVKSDSNLWSFDVSAEFDLVCNTKKPTLKFQRTYNNEMFSRGFRMGYIKDGKLTVAVKFSLKNIMGIRRIARVDFSDKDEPHDDIALEIGGENYLSLHSPVFDAMFFGNFAEKKKKIVEIKDVDRQEFVELLKVIYPSQDKITDTNYKYFLSLADRFQIKLVIDKVEQHLISTTKLSIPEKLKLADDFRLVKLHDVCLDSFITVQDITKIKSTESYKSLSDKAKQLKNHSDNSKIVEFVFNSMVLLVQSVNAINMVAPIMIGLPKLTIFDEVRRMDVRQITYQFLNLAMVVSSTLMLWKGLFVIAGNASPITVVISGSMEPAFFRGDVLILTNDDDEPVRVGDITVFRIEGRKIPIVHRVIKVHEKDANNTKVLTKGDNNQVDDRGLYAPGQLWLERKHIIGKASGLIPYIGMVTIIMNDYPQVKYVVLGCLALFVITHREK

Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. EC: 3.4.21.89 Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 503 Sequence Mass (Da): 57385 Location Topology: Single-pass type II membrane protein

A0A1C6FI01

MKNRIDACFEKLKAENKKALVTFITAGDPDMDTTEKCVLEMYKNGSDIIEIGVPFSDPIAEGATIQKASLRSLSGGTNLDKIFDLVRKLRTQTDKPMLLMMYINTIFKFGTAKFFELCKETQIDGVIVPDMPFEEREELQGEAEKNGIYTIFLVAPTSHERVKMIAEKSKGFLYVVSSLGVTGMRSEITTDFNELLAPIRNNDHCPCCIGFGISNPEQAKKMSQYADGVIMGSAVVKIVEEHGKDAPEYVGKFIKSVREGMDN

Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. EC: 4.2.1.20 Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan Sequence Length: 263 Sequence Mass (Da): 29261

A0A497G4E9

MSLQKIRCFIAVDIDDPVIVDRIVSIQYRLSGTGVRMKLVEKNNLHITLRFLGEISRPLLEKVIDIIKTVSFNSFQIKLQNIGCFPTPSRPRVIWIGVTEGEEKLREIHNELESKLRKLGFPKEKERFVAHLTIARVKSFSQVSRLIQVLNELRDIEIGEFTVNCIRVKKSTLTPKGPIYSTLYEQKATK

Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester. EC: 3.1.4.58 Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+) Sequence Length: 190 Sequence Mass (Da): 21891

Q9C0P5

DFSSETIAGLQSLSQKHNFLIFEDRKFVDIGNTVQKQYHGGALQISQWAHIVNATMLPGPGIIDALAQVASAPDFPHAAHRGLLILAEMTSKGSLATGKYTELSVEMARKYRGFVLGFVATRSLADVDTAAK

Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. EC: 4.1.1.23 Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP Sequence Length: 132 Sequence Mass (Da): 14245

A0A3B6KKN3

MEEKIGMTKLWALFLVVFVLLRNAQAAADGNKSRGGMRRLAGAPGVPVPMTLLTSAVAMGAVCLDGTPPAYHMDPGSGAGKNRWIIHLQGGSWCESVGSCLYRKASSLGSSNLMNKQIYFGGILSSSPLDNPDFYSWNQVVIRYCDGASFAGEGYDAGSGLFFRGQRIWNAAIQHLLAMGMSSADQVLLTGSSAGALAVVLHCDQFGAVFAGRGTTVKCLADAGFFLDAVNVAGWHTLRYYFGGVVATHGVAQNLPRSCTSHLDATSCFFPQNVIGGINTPIFVLNAAYDTWQIRESLAPDGADPGRAWRACKSSRLACNAFQMNFLQAFRDQMVGTVLGVSRSRRNGFFINSCFTHDQSEYLATWNAYGSPSIQNKAIWKSVGDW

Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties. EC: 3.1.1.- Subcellular Location: Secreted Sequence Length: 386 Sequence Mass (Da): 41537

I1H4Q3

MASSLAARRLLSHAAAARRVLSCASPVPSSPSFRRLATDASPPTPLPPPPLQPTVDPPKSEGASSSDGAGAGGAYQAGHGAATGSRRPGGAGYEEEQEKVLRASLLHVPRMGWSESAMIQGARDVGVSPAIVGAFPRKEAALVEFFMDDCLQQLIDRVDAGEGEQLKNLILSERLSRLVQLRLEMQAPYISKWPQALSIQSQPANVSTSLKQRAVLVDEFWHAAGDGGSDIDWYVKRTVLGGIYSTSELYMLTDNSPEFRDTWTFVSRRIKDALDLGKSFKEVTYLAEAMGAGMGGSIQGVLNKVFQK

Pathway: Cofactor biosynthesis; ubiquinone biosynthesis. Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Subcellular Location: Mitochondrion Sequence Length: 308 Sequence Mass (Da): 33056

I1IHZ5

MSTAKGNPPSPDPAAVEEMARDATAWCAMHGLVVGDRAEQRSGTVPGVGLVHAPISLLPARLPESFWSQACELAPIFNELVDRVSLDGDFLQDSLSKTRQVDDFTSRLLEIHRKMMDINKEENIRLGLHRSDYMLDSETNSLLQIEMNTISVSFPGLCSLVTKLHRVLINQYGNLLCLDSKRIPENVASQQFAEALSRAWDEFNVDSAVVMMIVQPEERNMYDQYWIVKYLKESHGVTTIRKTLSEVEAESQVLPDGTLVVDGRTVAVVYFRAGYTPNDYPSEAEWSARLLMEQSSAVKCPSISYHLVGTKKIQQELAKPNVLERFLENKEEIAKLRQCFAGLWSLDDEEIVKSAIETPDLFVLKPQREGGGWFFNKNICVLFFSLLVDMLFIYREQHIRS

Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. EC: 6.3.2.3 Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate Sequence Length: 401 Sequence Mass (Da): 45366

A0A7M7R8V0

MNIQKLTNATMNFDQSAIDEKINSIRSRVYKLEKHVKTTWLIKAIGFLDLTTLGSDDTPAKIEALCDKAVHPFKLSNNSNLHTASVYVYPLRLMDAITALEKLDKDHKISRATVGGGFPSGQYLLETRLREVELDVELGADEIDIVINRPLVLMHQWQKLYEELKLFRTACGNKCLKVILGTGELGNLENVYKASMIAMMAGADFIKTSTGKEAINATLPVGIVMCRAIKDYYESTQKKVGLKPAGGIKAPQEALEWMMLVQMELGEEWLCKDFFRIGSSNLLDNIIEEIQSN

Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. EC: 4.1.2.4 Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate Sequence Length: 293 Sequence Mass (Da): 32802

A0A2N6V324

MVLAPIGWYRKYISPAIAPRCRYYPSCSTYAVEAIEVHGVFKGLALSAWRILRCNPYSRGGVDHVPEVGHWRYAYPKDVARFQVPSASAGQDAPQTRQGQLG

Function: Could be involved in insertion of integral membrane proteins into the membrane. Subcellular Location: Cell membrane Sequence Length: 102 Sequence Mass (Da): 11382 Location Topology: Peripheral membrane protein

A0A3B6LQ29

MPMIFPFPVAVAAALFAAAALAPRHASALTRHDFPEGFVFGAGTSAYQVEGAAAEDGRKPSIWDTFTHQGHSSDGSTADVSADQYHHYKEDVKLMHKMGLDAYRFSISWPRLIPAGRGQINPKGLEYYNNLIDELILHGIQPHVTIYHFDLPQVLQDEYGGLLSPRFIDDYTAYANVCFKSFGDRVKHWVTVNEPNIEPIGGYDNGSQPPRRCSYPFGADCAEGNSSTEPYMAAHHLLLAHASAVSLYREKYKAAQGGQIGITLLGWWHEPATDTPQDAAAAVRMNDFHIGWFMHPLVYGDYPPVMRSRVGRRLPALPAPEPAKVRESFDFIGFNHYLIMRARSIDTSSGQEPRDYYVDAAVENPAADITTGEVETAPWSLRKLLEHLKLNYGNPTVWIHENGYADGPGTRSKAEEEEDDDEDRAEFLQDYMETLYLSIRNGSNARGYFVWSFLDVFEFLFGYRLRFGLCGVDMGDAARTRYMRRSARWYSGFLAGGELRPAARAQKSYVQ

Catalytic Activity: DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA EC: 3.2.1.182 Subcellular Location: Plastid Sequence Length: 511 Sequence Mass (Da): 57334

A0A7R9R3M1

MALRIEGKVWRFPDNIDTDLIIPGKYLRTTDLSVFAAHAMEGIDPDFAKKVGKGDIIVSGRNFGCGSSREQAPLALKHAGVGCVVAESFARIFFRNAINVGLPIMEASVGCRTGDHAIVDIEAGTVACNGRVYHGTKLPDFLVEILADGGLVAHRRKESR

Pathway: Organic acid metabolism; 2-oxosuberate biosynthesis. Function: Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate. All these reactions are part of the biosynthesis pathway of coenzyme B. EC: 4.2.1.114 Catalytic Activity: (2R)-homocitrate = (2R,3S)-homoisocitrate Sequence Length: 160 Sequence Mass (Da): 17235

A0A2A6D1H9

MCDDAVREVAFDPNYDPKRKGEGPGGDYAAYFSVRLRVFCDEQEISIDDEVDGADEKCKHYALFKGSQAVAVCRLSIEPPYAKIERVACLKEARGQGYARTLMLAVLRIVDAEYPNEIVAAHSQSAVLKFYERIGFIAVSREFLDEVDILHRSIVFPPRREKIRTLSLLSSPPSKHNEFAGDLYDGQVVTTIRRMLNEIENLSFIPLCSLVVSSISSLFIPSSLHEALCTVALRAQRANGYAENYTPFSPRLSTIEGVSDEEYLKAVAAKKMNTGEKITVEMLPLTALPGTGNGQDGLGCEGVTPFARGRSDNGTRCGRDTRRDDEEINDRAVLQRCPSFRR

Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2. EC: 2.3.1.4 Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate Sequence Length: 342 Sequence Mass (Da): 38012

A0A1E3FK49

MTARDGIAPPRATFGSHVLADLAGIDAVLLRDAARLESILTEAAQQAGARVIGAHFHHFGGDHGVTGVVLLAESHITIHTWPEHRFAAVDAFMCGAARAADAVDAIAAALGTQAQVRQQVARGGAPTSAGHSSP

PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. Cofactor: Binds 1 pyruvoyl group covalently per subunit. Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. EC: 4.1.1.50 Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine Sequence Length: 134 Sequence Mass (Da): 13701

A0A3B6HXW6

MSAAQIRAEINGLIASKFAEGTVDQYFLQLYVMWRYKNIRKGMVVEVMERFLQDADKILTEIAVLLSAPLSLWCRHSRLFGNQPQLDYDKVEGIADQLEGCSSSSVGAKRVNLSCVEYFHPEATTEEGNQIVVDFRKVDALVQQLKGCSSSVGANKLSVSCMHFRRFNHSKTKEGYLIALAPIMNEFCDVRNMFLTILQMEEQVDALGPKY

Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction. Subcellular Location: Cytoplasm Sequence Length: 211 Domain: Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer. Sequence Mass (Da): 23842

A0A3B6NRW2

MVCSSHFLERIKELRSTASEISLELNDAVRALGDLHLKHRQLTEKHHEERYLNARSKAEQKRLKVELASAAAELEESNHKLAVLKAQGDTTHGTPILFPTLGNKSFPQDNVRDKQKELQDLGASHKEFTGLISQRLAEIRRLHEERIEILNKLATFQNILTDLKSISSSKAFQVLKDQLQKSQAELDHCRTLLEKLQVNKDKLIWQEREINVKVDLSGIPHRVSLNCESTLAVLDQNLRKVVDEKNMLALKLEESSREPGRNQTISEFKALVSSLPEEMGAMQTELSKYKDDASELHSLRAEVRSISDILARNEHAINESLCKSTRAGPEARDLRSRVRELRQTNCELKLFVEMYKRESTDSRDVLESKDREYCEWARAHSLKSFLDDSRLEQRVKAAIEAEATSQQRLASGEAQIAELRGKMESARRDIGSLSELLKSKHEEGEAYLSEIESIGQAYEDIQTQNQQLLQQIIERDDHNTKIFMEGVKVKQAQDTLHLELCNLNRNLRQAKGLMDLYKDKIAQLDDKLKVWSEQTARLSEDGRRHSVSSGNAQRKLADVLGEAQQLRQSMDQVQSNVGRSRLGVAGLLVELEKDRFSKRRTEDDLESLSRKASSLRAKTEGSSVLEKVHQEVNEYRGILKCGVCRDRQKEVVITKCYHLFCNDCIQKLLRNRQRRCPSCALSFGANDVKPIYI

Pathway: Protein modification; protein ubiquitination. Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC: 2.3.2.27 Subcellular Location: Nucleus Sequence Length: 693 Sequence Mass (Da): 79173

A0A0Q3RDA1

MASSPRRGHAVVVLLLLLACHAPSAAADDRDFDDDKPAKFPDCDNHFQKVKVKYWVGGEEQSALTGVTARFGRLLPDTTAAAQKLPAVVPTPKNGCAKSSASLAGSVALAERGVCTFFEKAKTIESSGAAAMIVVNDMNDLSKMACTPEDKISRIDIPVVMVSKAAGAKFTSAMEGGAKVAILLYSPTKGPFDGAIPFLWLMAVSITACAAVWTVVVVGEEPKKPPTTEVVDQEAAEPDVVELQTKTALVFVVTSSCVLLFLFFFSSIWSAWLMVVLFCIGGLQGLHFVTATLIMRVCSGCRDSKVKLPVVGNVTVVTLVVLPIALFIVVMWAVHQSSPFAWAGQNLLGICMMILVLQVVQMPNIKVASALLISAFLYDIFWVFISPLIFKKSVMITVAKGNEDGPSLPMVLKMPKYFDPWNGYDMIGFGDILFPGLLVAFSFRYDRTHGKDLTGGYFLYLMIGYAFGLTCTYVGLHLMGSGQPALLYLVPSTLGTIVALGAQRGELSQLWNAKA

Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Subcellular Location: Endosome membrane Sequence Length: 515 Sequence Mass (Da): 55388 Location Topology: Multi-pass membrane protein

A0A077RFF4

MAMVQSVARRGARSVATAQLGMHLFSVSCCSPAALGVGTARTAATLKKGEKEAASYWGVAPARLVKEDGTEWKWPCFRPWDAYEADVSIDLKKQWRTQGVCQKHHRPATLGDKVALWTVKAMRWPTDLFFQSLRRFEQSGGWIRPLLEEAENERMHLMTFMEVSQPRWYERALVVAVQGVFFHAYLATYLASPKVAHRMVGYLEEEAVHSYTEFLRDLEAGKIDDVPAPTRRTTGTSNHYASDIHCQGHALREVAAPIGYH

Cofactor: Binds 2 iron ions per subunit. EC: 1.10.3.11 Catalytic Activity: 2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O Sequence Length: 261 Sequence Mass (Da): 29436

A0A341RP79

MENGGEPSIKKSRLQKEPMAVKHERAETRESQGGEGALLAVEEAMQVPWVAAEVNPLFYLCFACQLPLRPPVHQCEGGHRVCGRCHGDRCTACDPPAAYSPFPFMDDALAAVRLPCCYRADGCGRKLMYHEAADHALQCAFAPCHCPGHGCSMWASPPALLDHITAAHSWPVTEVGYGSPFRIAVPAPWRGGGTHLLVERNDPRLFLVTLSDFGEATAVTVVCVREGTAAAAPRFRSTVWAEVASNTEEKLFRRQSTVPSSSSGGSLPGGGPPVCLLVPPDFGSESEDLFLGVRIDKL

Pathway: Protein modification; protein ubiquitination. Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. EC: 2.3.2.27 Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Sequence Length: 298 Sequence Mass (Da): 32050

A0A0R3C2Q1

MLRIWKATINSRNGLAFAFRSEQAVREEIFALLLSVPLAWFIGATAMRAVELVCSVAFVLTVELLNTAIEKLADRLTLDHDKQIGRVKDMGSAAVGVALLMTGAFWIIAIIERLGFL

Function: Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis. Catalytic Activity: a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) EC: 2.7.1.107 Subcellular Location: Cell inner membrane Sequence Length: 117 Sequence Mass (Da): 12890 Location Topology: Multi-pass membrane protein

A0A2A6C1F7

MRLLVVVLCLESALGFKFLAYNPLFGSSHVNFMGKISDALVEAGHEVVMLATQTDDAIKLTATKARVVHVPQCSASVADKQLLDDIVTNLWLANDPFTMIIQFHHMMTSWIDQCNVVDLHTLQSARENRDMGEALEKLSSLIAATIRHPGLLDALRAEKFDAAFSETLDPCGFGLFELLGIENRAVTQTMAIVDGTHYFTQTPANPAYVPTLMVAPSGEQMPFLDRVRNTLSHLVMVIHNMNSMRRFEPVFRAADPNFDSLEKSMQSNSLVFMNSDPLLDFPAPRSSRVIDIGGISVSFGHSMLNETWSAILDLRPTTVLLSFGTFVQSHAMPERYKMSIVEAFRSFPDVTFIWKYEKPEDRISEGVDNIIETTWLPQHDMLNDARLSVFITHGGQGSVTEANTAGIPLIVIPVVTDQIRNANQVKRNGLGIVVDKESLDTPDSLIAAIKTMLEDDSYRKKALKTARMLAKKPFAARDIFVRNMEFLAEFGPLRQLDHYGAHLNFIQYYLVDVIAFLSLIVLMPLISFEQAMN

Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP EC: 2.4.1.17 Subcellular Location: Membrane Sequence Length: 533 Sequence Mass (Da): 59572 Location Topology: Single-pass membrane protein

A0A936SK26

MDTNAINSDRHNDQHETVIQATAVSRGVAAGRAVCLFGTKRQYFLTHIENSAIDHEIGRFRTAVTTASKQLNDLIKSPDIKAKSSGDIFDAHLMMLEHSTLAADVEAFIRSALVTAEWALRRVAENFSNKQAAVSDANLRDRIADFEDLCDRVLNALDGKAVTLPVITSDSVIVASIIRPSTLIELGRQKPSAIVTEHGGWTSHSFILARELKIPAVTGVKSALKLIRDGTSLSVDGFTGALTIDPSSETLEQIKSHTFVAEPIKFDAASTRSTTIDGREIILRANIDLVDPAPLLAQTAAKGVGLLRSEYLFQDVSVGYPSEDAQFEAYKLSASNCGPEGVRIRTFDLQVDQVNHPAEIREMNPALGLRGLRLSLADRPHFREQIRAILRAGAYGNVSMVLPMVSGVADLSTVREMIADETAALAAQGTPVPPMPLGAMIEMPSAVLTVDDIAKHADFLCLGTNDLVQYLLSADRDNESVAHNYQTLHPSVVRSISMVFRAADLQGKSTVVCGEMAGSPFYLPLLIGLGAREFSMNPDSLGAIRQVIGRISFDECRELARKASVLETADAIEAYMNDFYRRNWPHVFPGGISSST

Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate EC: 2.7.3.9 Subcellular Location: Cytoplasm Sequence Length: 596 Sequence Mass (Da): 64667

A0A1C6GYZ5

MSEENRTNAPEEELTQEDINSLKKIRMDKLEELKAKGKNPFEITKYDVTASCAEAKAQYEKLEAELKEQAGEDEEKLKELLEANRITVSVAGRVMSRRLMGKASFFDLRDKSDKVQVYLRMNEIGKEEFDDYKKGDIGDIVGIEGFVFRTKMGEISIHAQKFVLLSKSLLPLPEKWHGLKDQDTRYRQRYTDLICNPEVKDTFIKRSQIISSIRRYLDRQGFMEVETPMLVSNAGGAAARPFETHYNALDEDVKLRISLELYLKRLIVGGLERVYEIGRVFRNEGVDARHNPEFTLMELYQAYTDYYGMMDLTENMFRHVAQEVCGTTCVPYGDVMIDLGKPFERMTMIDAVKKYSGVDFSQVATTEEAKALADEHHIEYEARHKRGDILNLFFEEYVEEHLIQPTFIMDHPIEISPLTKKKPENPDYVERFELFITGREMCNAYSELNDPIDQRERFAAQEEALKQGDEEANHTDEDFLRALEIGMPPTGGIGYGIDRLVMLLTNSPAIRDVLLFPTMKTLE

Cofactor: Binds 3 Mg(2+) ions per subunit. Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys) EC: 6.1.1.6 Subcellular Location: Cytoplasm Sequence Length: 523 Sequence Mass (Da): 60326

A0A1W4XBR3

MIHTFATIKANFKLFPQSIYIDNYVFKLHYRITTLLLLVATILVTSRQYIGEHIRCISDNGVPPHVINTFCFFTATYTVVKYLNSSLVDLEAIAHPGVGAFGPLGYNSPEPIIRHSYYQWVPFVLFIQAIMFHLPHLIWKHYEGGQMHFPQVRSLRINSVPRCHVHYGFKYNKRQDLHVPLVLVFILADRVHFGNGLAFSHVLSTCTQSSVQ

Function: Structural component of the gap junctions. Subcellular Location: Cell membrane Sequence Length: 212 Sequence Mass (Da): 24386 Location Topology: Multi-pass membrane protein

A0A3B6PFI6

MGGGSNSGKPGASEALSLVFRITTVGLSLASAIMTAASTQSQCVHDDCNGEATATVSFGNYNSFKYSALADLLSAVLQGVAICLEVARKDKAAKVVEFIDKLLLALTSTSAALLLAVDDITSCGSPRGGGRRRSRRFCTQAGRFCGKIRASSALSLVAAVSVSVTVYTRHIPVSFTLTPRLRASPPAREIPMKGHPTAPPPSVRPKPPKPESPTGPKCGEEPGPCTDIGTPQPPVMPRPCGGCTTLTIPQGCEIAEQVVSPPCCGCPRRTIPQGCENPEPCGAACVYVHE

Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal apoplasm and the extraorganismal apoplasm and prevents lateral diffusion. Subcellular Location: Cell membrane Sequence Length: 290 Sequence Mass (Da): 30061 Location Topology: Multi-pass membrane protein

A0A842LQ96

MLEELIKRSGAIKFGDFLLRSGKRSHYYIDKYMFETDPEALRGIAEEIAKRIDPRDFDRVAGVELGGVPLAVAVSLKTGLKSLFIRKRQKEYGTANRIEGDFRSGMRILLVEDVVTTGGALLDAINIIEEAGGIVKKIFVVVDRMEGGVERIREKYDVEVLTNVRSLGISEEIRKS

Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). EC: 2.4.2.10 Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate Sequence Length: 176 Sequence Mass (Da): 19719

A0A2C9JT88

MADHTNGSVQRRNNGDDRDFHDNGDTSESVVKDNNSTHSPGQSLSTQPVKRFVNQTLVPITLLLIMPNFVIVIWYTIVHCHGSYLKMVSVMFEKSVFSGLVHIWSLTRSPSPVIIWSLVLYCAYALAMMKLLPGKTVYGPMTPKGNIPEYKDNGFLFFVLTIGMFWALVLLLRPFGISPSIYYDKMDEICVTLNIFSLVFCAFLYLKGKLAPSSTDSGSSGNIIFDYYWGMELYPRIFGFDVKIFTNCRFGLMIWALMVCIHAVKSYELHGFVDSMFVSALLQIVYLAKFYWWEAGYLSTIDIMVDRAGFYICWGCLALVPVLYTSVTCYLVTHPVRLGLAVSAAMIFIGLLSIYTNYEADAQKQKVRKTNGDCLIWGKTPDIIRAKYQLENGGIKDSILLASGWWGMSRHFHYIPEIMLALMWTLPALFENMMPYSYVIILTIILTHRSSRDEEKCSSKYGHFWRQYCNKVPYRIIPNLF

Pathway: Steroid biosynthesis; cholesterol biosynthesis. Subcellular Location: Membrane Sequence Length: 481 Sequence Mass (Da): 54974 Location Topology: Multi-pass membrane protein

A0A967FKB7

MWNSINRIGTXTGSARLRFSSHFYLVAMFFVIFDLEAVFIIAWAISFKEVGWFGYIGVLIFIFILLVVLIYEWRIGALDFGTSGKNIVKLYKKLNKKEFI

Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.- Subcellular Location: Cell membrane Sequence Length: 100 Sequence Mass (Da): 11635 Location Topology: Multi-pass membrane protein

A0A3B6SFV7

MVEEKRERAEEASESPQKSPRLDPLAGPGCSDAPASPTESSDEWPSSGEVEAGISSDSTGDSMDDSGRCDHIRFDLDMVVHDLKVANQVLKEPRKCQHRNCKTTWEGASEDDQGMMKCIDCSYFFCSGWPVDRDDPQGHARWHAGEHQHWVAQWCDEPNLGYCFMCARPMRLSDWSEDDYAVAARNEKDQQMPGDSVAKDGWGSVSGIAKDERQRVPRIAMDDVASGYAIGDGHVIKGMPNHGQTCFMNATLQCLLALGKLRTKIRSPDAHLGSIGLHLQQLFKETRISNDARGMLDPCMILAAVRERYPNRFEAWKMEDSHEFLLSLFNAVNAEVEVENGRHVLEGGEVFPTFHVSLFGGQLFETTSCQRCPPKDPKTVDFGELYLSLPEKDPPARSVASPPRNKSHGSQTDKSDGDNKIQTTAEGSTSPISGSGLGDGAMEKTPKPLQVDSSEVKDVVHGHMQTQKNDVPQEINEVPIEILDFIPDLFDDTEGMEEATIDSRNPEDKETTYSVKVTTKEKEEAQSSDIVHDEAGHMNSLVSIEDCLELFARRVLERCENCSKVAEQIMASTNINTTVDRDQTELSDRKTCPSERSSDCNSLSVESPSRQPYRSDVHHQVILSENITTEEITSGASCGEKDSASCSTASEKAEIDQGVQEAGLPADKQTDLLSAQDSPDTSTQNQGCAKQAMLDDHIAQQMEENQSEQKDGNSCAIQTQLINKLPAVLIIPFKRYSNDLSKLRGHVSFKEILHLGPFMDPRSEDKDNCSYRLVGVIEHEGHQINGGHYIAYVRGAGHNHQSSGSSSWVRASDLDIKEVSLEKVLGREAYMLFYERMED

Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. EC: 3.4.19.12 Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Sequence Length: 839 Sequence Mass (Da): 92952

A0A497GLW4

MKYLRGIKVSDEIFEDCGVVGIKSYKGENVVPAIYWALLTLNHRGQQSYGIVTYDKKFNVVKGLGLIADLDIERMSGWCVKLRASLGVGHVRYATSGSIDKRKLFEDAQPIIVAHEGRKVCIAYNGNIANVVPLRREIEEMGIEINGTSDAYVLAYELLLGIEDEGDLIEGVKRVLEKVDGAFSVVGITSEGEMFAFRDPHGIKPLIFGISEDEETVGIASENVALAVNGILKNRSIAPGELIVAEEDVNSYQLHNGTEALCAFEYAYFARPDSKLSNGKYVYEVRRELGRRLARRYHEVAQRVDIIVPVPQTAEDAAYGFHIETGKPIEPIIVRHRYLRHRAFIMTKREREAIVSHKYNILYDKVRGKRIALIDDSIVRGDTLKYIVHVLRRAGAKEIHVFSTFPKIISPCFYGIDMATFHELIGFNRDEEEIAKILGVDSVNYQTIRDFCEAVGTNNLCLACVTGRYPTPYAQKIADEGRKLALSGSRIRGRLVEWGG

Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. EC: 2.4.2.14 Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine Sequence Length: 500 Sequence Mass (Da): 56019

A0A1C6CUF7

MRRVVITGMGTVNPLGKNVEEFWANIKANKNGLSYVDQFDTENFPVKIVGAVKDFDCTEYIDKKEAKRMDRFTQFAVCSAKQALKMAGSDFKDVDPFKAGVIIGVGIGGLNMTEKEVTKFNEKPDKVSVFFIPMMIGNMAAGTVAMHTGFKGDNFCTTTACASGTHAIGEAFRKIKDGYLDVCLCGGSEACISHFALSGFNNMKALSKATELDKASTPFDLNRQGFVLGEGAGILCLEEYEHAKARGANIIAEIAGYGATGDAYHMTSPSPTGEAAAHAMKYAYEEAGLKPEQVNYINAHGTSTGLNDKYETTAIKLALGEEAARKTVINSTKSMTGHLLGAAGGMEAIVTALSVQNDFVHKTINYTTPDPECDLDYCVEGNREMPVYAALSNSLGFGGHNATICIKKCD

Pathway: Lipid metabolism; fatty acid biosynthesis. Function: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition. EC: 2.3.1.179 Catalytic Activity: (9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP] Sequence Length: 410 Sequence Mass (Da): 43951

A0A7M7GWC2

MTEKKRVLMICLGNLCRSPIAEAVFYDQINKLGLSDSWEVDSAAIIGYHIGKNPDHRSMSIIREKGITDYSHKARQITRDDFFKFDWILAMDNSNIKYLNSMKPPNTTAKIELLGKYDPEGELTIRDPYYVYCFNMMFTLLDFIRYMNNVCEVQKHFWKNIKINNQIEALK

Function: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate EC: 3.1.3.2 Subcellular Location: Cytoplasm Sequence Length: 171 Sequence Mass (Da): 20089

A0A2A6C3V7

MQQLVWKPTIGLLWFALYHKRARIEVVEVTFLICISMFGISASVMVICSAFIIEALRSMKVSTAKKVQQRMLFRALLIQTLIPCIFSYFPLCIIWMFPLFTGIALGAFGNILTMTSTVFPSVDAIIIIIFIPAYRHSVKMWILNKIRPSDLVIVSTPCRIQMLGRAAGRIASSHRRAQILTQLRLLNLQEYQSKGILDRNGCSVQKFVTATSLKEAEEKLKDFSVYEYVVKAQILAGGRGKGRFIGGPKDLGGVHISYKPEEALSAAKEMIGRRLVTKQTPKEGVLVEKVMIAEGVTIKRETYLAVLMCRETNGPVVVASPAGGVDIEHTAEVSPELIFKEPINIREGMTDEQARRIARNLEFKGDLEEKAAVEIRRLYELFLKVDATQVEINPFVETDDGRVFCVDAKMNFDDNAAFRQKEIFEMEDTSDKDPREVAANKLNLNYIGMDGNIACMVNGAGLAMATMDAIKLNGGEPANFLDVGGSVSDEQIMKAFEIITQDANVKCVLVNVFCGILNCATFARGAISAFKNATIPVVNLFVVSRNRRAINKVTNGMRGTNVEEGRRLLRESGLSVISADGLDDAAAKAVAAAARQ

Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. EC: 6.2.1.5 Subcellular Location: Mitochondrion Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA Sequence Length: 596 Sequence Mass (Da): 65779

A0A7M7MQ32

MATTKDDSTDSVQFFEGVEKLLEIWFTSSSSINRKQGDLRQIPQWKWQSLLKIVRCEIISICRTEHVDAYVLSESSMFLSKRRLILKTCGTTTPLQCLEPLLELIKEYTGFEEVENVFYSRKNYKKPELQISPHQAFEEEVGLLDTFFPGGEAYCLGSVDSDCWYLYTLNKEKSVDEPSEPDQTLEILMTHLDPEIMALFTRDVCSSADEATQKSGIDKLIPNMIIDDFLFEPCGYSMNGVSKNGNYMTIHITPEPEFSYVSFESNIPEASYEEIIRRVLNTFKPKKFVVTVFANKESIAASCPRDLEQTDFLKCSGDWLRTDVQYCRFKNYDLTCAFYSRFPS

Cofactor: Binds 1 pyruvoyl group covalently per subunit. Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. EC: 4.1.1.50 Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine Sequence Length: 344 Sequence Mass (Da): 39630

A0A3B6AZG2

MSLAAESPSPSPSSSSGSDDFAALLDAELDLASAVDSASVGDPSTSPTSSDDEEDDDEDVVADVETVEQSSAKRRKVKVQYQDRETAIRPDEDSIGSSEDAQIKICPPHPGYFGGLCFRCGKRQDEEDVPGVAFGYVHKGLRLGTTEIDRLRGSDLKNLLRERKLILILDLDHTLINSTKLHDISAAENNLGIQTAASKDDPNGSLFTLEGMQMLTKLRPFVRKFLKEASNMFEMYIYTMGDKAYAIEIAKLLDPHNVYFNSKVISNSDCTQRHQKGLDMVLGAESVAVILDDTEYVWQKHKENLILMERYHYFASSCRQFGFSVKSLSELMQDERGSDGALATILDVLKRIHTIFFDSAVETALSSRDVRQVIKRVRQEVLQGCKLVFSRVFPSSSRPQDQFIWKMAEQLGAICSADVDSTITHVVAVDVGTDKARWAVKNNKILVHPRWIEASNFRWHRQQEEDFPVKVKKNEKDKENDVAAATDAANGKVNDVVAAATDPANEKDKEDDVAPAATDPANEEDKEIDVAAAVTYSTNS

Function: This promotes the activity of RNA polymerase II. Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate EC: 3.1.3.16 Subcellular Location: Nucleus Sequence Length: 540 Sequence Mass (Da): 59806

A0A077RPY2

MQGAGAEGGNRGSPSTMEKADESAKKARLELPNGHVKQEVGVQHAVGGDDGGAIVPAEAGHGSRVELAVKIDMSVLHCPLCTLPFKPPVLQCNKGGHLACGGCVALLPGGQCRACEDGGGFFSPCPALDAIVSSTKIVCPNAGCQTYVPYHEAADHRSACPHAPCHCTEPGCGFVGAPQALAGHLVDLHSVPVRTVQYGRVSQVPVSGRRQLLVAEEDGRSFLLTVGALGAAAAAVSVVCVRASASTQPRFSCKMWVNLVQPASGGRADMVLVDIQMRSSATPGAVVAVDEPTFLAVPRMYMVPVDGDAASMEVPLNIRVDKISR

Pathway: Protein modification; protein ubiquitination. Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. EC: 2.3.2.27 Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Sequence Length: 325 Sequence Mass (Da): 33561

A9HS47

MTLLKIARMGHPVLLRRADEVADPTAPDIARLIDDMIETMEDARGAGLAAPQVHVSLRLFVYRVPAERSAGGDDPPRETSVLINPVLSLVDDEMALRPEGCLSIPGLRGMVPRHVRIAYSGLDRAGQAVQGVASGFLANVLQHEYDHLDGILYPMRMTDLGQMGFDEEIGRYGVRT

Cofactor: Binds 1 Fe(2+) ion. Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. EC: 3.5.1.88 Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide] Sequence Length: 176 Sequence Mass (Da): 19243

A0A0Q3GY12

MVPRSLNSTSLPDADTPPPPPPPPIDPNDDAEEQLSAEAPDLAARLEALELAASERAADLSSSSRAGVILEEPAEPSSSKPWWSPPRGWRVAFSTATISDTLERLDDSIVLRLRGRALHCFNNEAYDLQCYPIIHSNGQYLFKGSLFQYLFFEDEKLHAEIARYKFSSYETPFLPSLLMEPITRIPWSLQGLHPAAESININERVLIRYFYEFLPMLVNEGSDGQPVSSSQCDVKILQALSNRIHYGKSVAESKFLEEPEKYTSAIREQDNDNLMETLTNPDAEEEVITRVKNKAMVYRQEVDPELVGELYDKLVIPMTKEVQVQYLLRRLD

Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. EC: 5.4.99.5 Catalytic Activity: chorismate = prephenate Sequence Length: 332 Sequence Mass (Da): 37587

A0A6I9SL11

MDLKSTNGSLIVADPAPITKSRLGAYSGLMPYSQSGPSFSANITTVPRKKPGKLDDVRSNGWLDAMISSSPPRKKIHKDFNAFDIVSDEADVAYQSWMIRYPSALKSFQLIMDRAKNRKLVMFLDYDGTLSPIVDDPDRAFMSNEMRSAVRSVAKHFPTAIISGRSRDKVYDLVGITELYYAGSHGMDIMFPTRDTVSPNHLNCVKSTDLQGKEVNLFQPASEFLPMINEVYRTFVEITKDIKGAKVENHKFCVSLHYRNVDENSWPLIAQYVHDILKDYPRLRLTHGRKVLEVRPVIDWDKGRAVEFLLESLGFSNSSDVLPIYIGDDRTDEDAFKVLRKGNRGYGILVSTIPKESNAFFSLRDTSEVQDFLESLVRMAQQDAKGL

Pathway: Glycan biosynthesis; trehalose biosynthesis. Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance. EC: 3.1.3.12 Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate Sequence Length: 387 Sequence Mass (Da): 43693

A0A088E7W1

MKVVPSIDISKGMAVKRVRGREGTGLVLGDPLKIAEELRNMGYTSVHLVDLDAAEGKGDNVEVIERVMKDFSEISVGGGIRDRSRLERFLSSGATKVVMSTLAFTKPDTFRRVVAGYENRVLVSVDYCERKVLIKGWNESAMSFEEAISHVNSLGVRGVIFTYVCNEGTRNGIDPEIGRYVNLVQGEKGYAGGIGSIQDLQELDKMGFHFAIVGMSLYAGVLRGVTSV

Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide EC: 5.3.1.16 Subcellular Location: Cytoplasm Sequence Length: 228 Sequence Mass (Da): 24870

A0A370LIG4

MAKIWVEAYGCSASYADSEMISGLLVNGGHSLAENSDDSDLSVVVTCSVKDATANKMIHRIKSLKDKPLVIAGCLPKAEKSTVEKFSENASLLGPNSLGKTLEVINATLNGKKKIELLDSDLNKVGLPKVRLNPVIGIVEIASGCMSECTFCQTKLSKGDLSSYRLGDIVRQVKTEVDDGCKEIWLTSTDNGCYGLDIGSDLSELVNAVSDIPRDFRIRVGMMNPMYMPRIREGLLKAFENDKVYKFLHIPVQSGNNKVLNDMKRGHTAETFRDVVMRFREKFPKFTISTDIIVGFPSETDEDFNDTVNLLKETKPDVVNLSRYSARPGTEAATWKQVDIEKVKKRSKEVFDLTKKISLENNEQWLGWQGPVLFNEKTDEGIKGRNYAYKPVFVPDNVEIGASPMVKIVKVSFQSLIGKIIS

Cofactor: Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. EC: 2.8.4.5 Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine Sequence Length: 422 Sequence Mass (Da): 46848

A0A657AVF4

MNKARQYHSDLASLLLGIQHVPSALNTQIHGLVSDSRKVKQGDLFLALPGINSPASTYVQDAIERGAAAVLIDCNANEANDLTVHEDGRAIELFVPNLSNFVGEIAHRFFHKPSEELQVIGVTGTNGKTSVVNYIAQFFASLGVSSAVIGTLGYGLCARDEELTDTGHTTPSVVDVHKYLANLRDAGAELVAMEVSSHGLDQGRVDGVRFEGAVFTNLSRDHLDYHQTMAEYAKAKARLFASEGLRYAVINADDEYASVMFQALRPEVRKLRFSLNGSAEVLVKDFQLGMTTTAKIEVADKIIDLNSDLLGQFNLYNVMAVLGVALAKLCSVIELNAINQLKAVKGRMELHRVTDKPALVVDYAHTPDALENVLQTIRNLEPKRIHVVFGCGGDRDQGKRAQMGLIAKEFADVCVITSDNPRTEDPEQIISQIASVFSDQDDVICIADRAQAISHAYHSASVDDVVLIAGKGHEDYQEVNGVRSYFSDSDCCDHLLAEEVQK

PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP. Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. EC: 6.3.2.13 Subcellular Location: Cytoplasm Catalytic Activity: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate Sequence Length: 502 Sequence Mass (Da): 54738

A0A965C9S6

MRPSDRQEVEPARLDNVWTALDQCAKTLGLAIIRGYEYTVRPVLGPSCRFLPNCSEYARQALQSHGSVKGAYLSLRRLCRCHPFHPGGIDEVPAPSSSHGTKPAEARVSKKNDREPAAS

Function: Could be involved in insertion of integral membrane proteins into the membrane. Subcellular Location: Cell membrane Sequence Length: 119 Sequence Mass (Da): 13101 Location Topology: Peripheral membrane protein

A0A2W6APG5

MKSRLASGPRRPEVVIWGAGAIGGLVGAWLARAGVDVTLVDRDEEHVEAIRARGLLVDGIRGEFRVQVPVVLAAELREPVDLAFLCVKCLHTESALDELVPRLADGGRIVSLQNGLNEEVIARRIGRRRTLGCFINFGSDLLGPGHIRHGGEHPVYIGELDGARSESVEHVRALLANFCDTVITDNIWGYLWSKLCYASLLFGTAMVDAPVHDTVRQPEAGPVLLGLVREVIDVADAEGVRLERLADFWPDEFRDGDWRSAMKRTAAHYQGQLKTRTGVWRDLAVRHRRTEVDCQVGAAIRKGESLGIEMPLNRRLLELIHQLERGDRSMSLQNLSALTEK

Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2. Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. EC: 1.1.1.169 Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH Sequence Length: 341 Sequence Mass (Da): 37762

B1G158

MTDKHRLIHITRDTHRVDIDLVYATPRNFTGKPIYREAHCLLLEPAEAALRKAVELAESIGMSLLIFDAYRPPQAQKVLWDFLPDPTYIAELGRGSNHSRGTAIDLTLIDGNGEPLDMGTGFDEMVKASEHFHHGLPQHVQRNRLLLLGIMHAAGFTHIASEWWHYELPGSRALPVIDNSESGPLKLM

Cofactor: Binds 1 zinc ion per subunit. Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. EC: 3.4.13.22 Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine Sequence Length: 188 Sequence Mass (Da): 21132

A0A967FAR5

TGRWTCPECGHMYHEEFNPPVEDLVCDNDGAELYQREDDKPETVKNRISVYREQTQPLIDYYEKQGVLTEIDGDQEISEVTDELLSILS

Catalytic Activity: AMP + ATP = 2 ADP EC: 2.7.4.3 Subcellular Location: Cytoplasm Sequence Length: 89 Sequence Mass (Da): 10338

A0A454XZJ7

MTDFMPDVNSLFAGRTVFLTGGSGFVGKVVIEKFLHAIPDVKRLYVLVRPAKGKSAQERWEAIHTKSEIFNRTRADCPETIAKVFPVEGDITIDDLGLSEENLKRVLEETSVVIHCAATVRFNDTLKSAIELNIKGVNRMIKLCKRMPKLDCFLHCSTAYVNVDKEGDIEEKQFDVVCDPYKLMDAQSWMTEEMLEGISNSMSNKYFNTYCFTKHVSEELVRRECVDLPTLIFRPSIIGGIWKDGIPGWADAFQGITANALGFGTGTIPRMPIPDTTIPLDAIPVDIVSNMMIVCAAYRLHLTNLKDKSMPIFHCNSSHLNPLPITLYRNLMGSTLSTYPVEKFIFAPCTSTRGTVRMENAIHKFKHRVIGPALDKVGGVMGHKPFWEKTFGKVREVYSVFIPFTYKRWIYKTDNMIELIGKMQPDDVERFDFDIRKVDWNDYISDVILGMRTFLVKNDVYSDKKLNETRRNVRIHQGIEFFAILFIGWLLALLITGSTSSYKIAAAIGLSLYYYIHIRTFQMVRIGTIESYRERLTETMRCVPLDHQNNNNNSSKAK

Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. EC: 1.2.1.84 Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+) Sequence Length: 558 Sequence Mass (Da): 63621

I1ICA9

MDLSNGSPVITDPMAMGQPLMGVLPSNMMPFSVMPGSYSSPAGAGLNVSRRKIEEVLVNGLLEAMKSSSPRKKHNLVFGQENLPEEDPAYTAWTATTCPSALASFKQIVAGAQGKKIAVFLDYDGTLSPIVDDPDKAVMSPVMRAAVRNVAKHFPAAIVSGRSRKKVLEFVKLKELCYAGSHGMDIMTSSANYEHNTEKAKEANLFQPAREFLPMIDEVSKSLLEVTSGIEGASIENNKFCVSVHYRNVDEKDWELVARLVNEVLEAFPGLKVTNGRMMSRRFCRF

Pathway: Glycan biosynthesis; trehalose biosynthesis. Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. EC: 3.1.3.12 Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate Sequence Length: 286 Sequence Mass (Da): 31349

I1IE59

MDGRESAAASGANFSPFYVRPWGMGAARAAAGNPDGLHGPPPVGYRQHLDAVSAGYSFQQPHFGGSHIGQEYHHDHVEGSPHVVQHTAGMDIVAVGVDAKGGDQGSVEGQDEQVKKKRGRPRKYKPDRAVTLGLSPSPSTPHSSSSGMGAMVTTPGAGFGSGTGSGGSGSGALTEKRGRGRPPGSGKMQQLASLGTWFLGSVGTGFTPHVIIISAGEDVAARIMSFSQQGPRAICIISATGAVSTATLYQDSDSGAVTYEGRFEILCLSGSYLVLDEGGTRKRSGGLCIALCGPDHRVIGGSVSGVLTAAGTVQVIVGSFMYGGGSKKSKAKAEQDMENEEKNGGAEDTPTMALTEHNMPPHPMSGWPGLMNQMDSSSPMYGGSKKNKGKAEQDMENEEHNVGGEKTPAVALPEQHNMNMPPHPMSGWPPGLMRQTDSRSSNIDINSIRE

Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). Subcellular Location: Nucleus Sequence Length: 450 Domain: The PPC domain mediates interactions between AHL proteins. Sequence Mass (Da): 46781

A0A3B6HYW4

MARAVSLSALCLLLAAAAAGARVDPIYSGKLVLDWSKEPKFKLQNFSLNREDNLQLLSRSRDVTRRKLGERTGVIKMETVQQDDEALVKLENAGFERSKAVDSAVLGKYSLWRRENENEKADANVRLMRDQMIMARIYSVLAKSRDKLDLYRELLARIKESQRSLGEATADADLPKSASERAKAMGQVLSKARDQLYDCKEITHRLRSMLQSADEQVRSLKKQSTFLSQLAAKTIPNGIHCLSMRLTIDYYLLSPEKRKFPNSENLEDPDLYHYALFSDNVLAASVVVNSTIVNAKEPEKHVFHLVTDKLNFGAMNMWFLLNPPGDATIHVENVDDFKWLNSSYCPVLKQLESAAMKEYYFKADRQKTLSAGSSNLKYRNPKYLSMLNHLRFYLPQVYPKLNKILFLDDDIVVQKDLTGLWEVDLNGNVNGAVETCGESFHRFDKNGRRRTLLEFTISGRT

Pathway: Glycan metabolism; pectin biosynthesis. EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 461 Sequence Mass (Da): 52531 Location Topology: Single-pass type II membrane protein

A0A497FAL9

MGKVFVVPGSASENLARKITQEVGVEVLGVERKVFPDGETYLRICAEDLSGASVYVVQSLARKPNDYLLELLLLVEAAKGLGAKKVTAVIPYLAYARQDSRFKPGEPISIVAIARALEAVGVDEVVTVDMHLHRFHDVSEVFRVPATNLTSIPLLAKFVKEVWKLEKPVIIGPDEESEQWASIMGRELGTTYSVLEKERLSATEVQIKVRGEVSVKDRDVVIVDDIVSTGGTVAEAAKVLKQLGARRVFAAVVHLVLAPGAIERMKSAGVVDIVGTDTIESPYSHVSVAPVIAKYIKEREGL

Cofactor: Binds 2 Mg(2+) ions per subunit. Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). EC: 2.7.6.1 Subcellular Location: Cytoplasm Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+) Sequence Length: 302 Sequence Mass (Da): 32780

A0A454XR98

MSSDDSPIEFIDITNDEGLRARVLTWGATLVSLWFKDKNGREHDCVLGYDTIDEYKSDRVQMGKTIGRVSNRIKNGEFEVNEEKIQVEKNEGNNHLHGGPKGCSQRNWSIHRRAHNSVTFLITQTHDLDGYPGDANMKCTYTVNDLNQLVVEHWAETTVPCPIAMTNHAYWNLDNDSTTCLDHHLFVRAHYYLPVDDDKCPNGDTKPVFGTSYNFNKMRRIGPSPPIDHDLILTDHEKTKIVLALENPTTGIRMTMRTTYPSIHIYSAEQFDGSIIGKGGRSYPESAGIAIEPQQYTSAVHFDWFPPVIVDPSTPYEQEIIYSFQHIQPKLIA

Pathway: Carbohydrate metabolism; galactose metabolism. EC: 5.1.3.3 Catalytic Activity: alpha-D-galactose = beta-D-galactose Sequence Length: 333 Sequence Mass (Da): 37839

I1IV26

MADSAMKKYLVQVEEGRAAAAAAEDGTAGAPSVGPAYRCAAGGGAASPPVVPGLDSCWDIFRLSVEKYPGNPMLGRREIMDGKAGKYIWVTYKEVYDSVLKVGASIRSCGVSKGGRCGIYGGNCPEWVVSMQACNAHGIYCVPLYDTLGAGAIEFILCHAEVEIAFVEEKKIGEVLKTLPNATKFLKTIVSFGKVSPDQKEKVEQNGLYIYSWTEFVLKGDGNEDKYELPPKEKDDICTIMYTSGTTGDPKGVLISNKSIITIVSAVDEFLSNSNEQIRENDVYISYLPLAHIFDRVIEEVFIHHGASIGFWRGDVKLLVEDIGELKPTLFCAVPRVLDRIYGGLQDKVSTGGFMKKTLFNVAYKYKQGNMIKGTKHEDAAAIFDRLVFTKVKRGLGGRVRIILSGAAPLSNHVEEFLRVVTCSHVLQGYGLTETCAGSFVSLPNNMSMLGTVGPPVPYVEARLESVPEMGYDALSEESPRGEICIRGDTLFSGYYKREDLTKEVLVDGWFHTGDIGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENLENIFGQAPNVDSIWVYGNSFESCLVAVINPNKQGLERWAESNGVTGDFASICGHPKAKEFILEELSKTGKEKKLKGFEMIRTVHLEPVLFDLERDLITPTYKKKRPQLLKYYQTIIDDMYQSMK

Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. EC: 6.2.1.3 Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate Sequence Length: 672 Sequence Mass (Da): 74254

A0A839V128

MIDHLVETLRTPLAFVVVLGVLVFIHEMGHYLAARLVGVHVDVFSIGFGPVLRRWHDRVGTEWRLCALPLGGYVKPHGFEEPDESDVESRAGLRPGQTFHDKPVWARAVVILAGPAFNFAFAVLLFSALYMAAGKPVSSTRVESVTADSAAASAGILPGDRLRSIGGVRVDDFDDIMAQVAPAPGRHTQVVLERDGHTLSVPVTIGRAVSDGTPIGRLGIGGVVEPGPRLGPLAAVSAACGETWTVSVQTLRALWQMVTGYASPRALQGPLGIARLSGQVAKLGVASVLSFMALLSINLGLINLFPVPVLDGGRLVFYAIEAVRGRALPRAAREASLGVGMLLIGALFVFSTVNDLTNIGLFRWLAHSAG

EC: 3.4.24.- Subcellular Location: Membrane Sequence Length: 370 Sequence Mass (Da): 39153 Location Topology: Multi-pass membrane protein

A0A3B6U1S4

MAAQNNKEVDALVEKITGLHAAIAKLPSLSPSPAVDALFTELVTACVPPVRVILMMSFGLLYSCFLASSYICIYDCFCLLVIQVAYFPNMVLELGLFSRTHNSC

Function: Synthesizes nicotianamine, a polyamine which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron. EC: 2.5.1.43 Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine Sequence Length: 104 Sequence Mass (Da): 11334

I1ITB2

MGCGGRSSTTAMTWPRWRRRHGWQLPLHPLQLVAAAVFSVLVAAFYVVLGPYLGSTVAGNTLLALFSFSAAATAALYVRCTAVDPSDRTHAKKMKRQRSLARGGGGGKLPRLRYGYILWRYAVRLLKRVEARVMNRWVRRSYLEQWNTSVQLDPMLPFAFTSLDDIVSPHATEDQDISFCPVCDCEVKLRSKHCKTCERCVDGFDHHCRWLNNCIGRRNYAAFILLMFFVLLMLVIEGGTAIAIFVRCFVDSKGVKMEMEHRLHIRLPKGAHAALSMAFVIFTMYSTAALGQLFFFHVVLIRKGMRTYDYILAMREAAQAFDPFDDSDSSSDESIDFDSPEKPSFLSRIFCRKDELNESSRKLSIRIDEKEPNDATRRKDDIQINPWALIKMSKEKAMAAAERARERIRQKLPSTTTSPMKPLPLETKRGPLNVDRRQIVTGKEIVPVCTKSWLSGSPTTRLSSPRRRFSGSPSPKPQRYRTNFDLRLAEVSRELDTHISKQVLCSVVMKGVEDEDSFS

Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 519 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 58979 Location Topology: Multi-pass membrane protein

A0A2G8B1E1

MHIEARLFEFVAAFFIATAVLYGVLTQLFATGGVEWAGTTALALTGGMALIVATFFRFVARRLDTRPEDYEGAEISDGAGELGFFSPHSWWPVLVALSGSVAAVGIALWLPWLIVAGVAFVLSSAAGLVFEYYLGPEKH

Function: Part of cytochrome c oxidase, its function is unknown. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Cell membrane Sequence Length: 139 Sequence Mass (Da): 14900 Location Topology: Multi-pass membrane protein

A0A965SC64

MTGVDSPPQNPTVWSDPAPLTVSALNRLARERLESAIPLLWITGEVSNLTRAASGHCYFSLKDADCSVRCVMFRGRVAASGLQLVNGQQLDVRASATLYEARGEFQLQVDALRLAGLGSRFAALEALKQRLLAEGALDAARKRALPTMPRAVGIVTSPSGAAVRDLLTLLEQRMPSLRVVVYPTLVQGDSAPSTIAAAIELAGQRLEVDVLIVGRGGGSIEDLWAFNSEAVARAILACPLPVVSAVGHETDTVLSDLVADVRAPTPSAAATLVCPDHRQLLAHLTQQQQRLQRGMQMRLEDREQRLDHITARLLSPAQRVELQLARLAEWRARLSSAWLDRLEQRLDRLAGGLDLLSPHRVLERGYAWVSRGDGSVLRSVAGVASDERLDIHLADGTLPAVARPGSDV

Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates. EC: 3.1.11.6 Subcellular Location: Cytoplasm Sequence Length: 408 Sequence Mass (Da): 44033

C3XU25

MDVVQDVAEVFATLPLFPVFNACHYTLMILTTRYDTGSLALSRSNPLANWVASMIACFGGYILADLLLGHSVLSFLAHPEDVVLASAIWYLLFYCPKDLFYKIISVLPLKLVITALKETARVRKLVAGIGAAAKVYPHSLLAQVIVGVAKACGNEFLLNFEQAVRGVWKPDINAILQPSFSIKACVVGAVMIILGRSDVLMGISQEMVVLAVSLWLISVAVSMKAFHADDPFKPVENLFSPFIFGSADSLPADAHHHHPPAPEPSPAPKPPSGRRRGKAAKAD

Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. Subcellular Location: Membrane Sequence Length: 283 Sequence Mass (Da): 30586 Location Topology: Multi-pass membrane protein

A0A0Q3HC50

MADVVLLDLWVSPFGQRCRIALAEKGVAYEYSEHEQDLSQKSVLLLQSNPVQKMIPVLLHSGKSVSESLLIVQYIDEAWPETAPRSSPPRSLRPRSGPLLGRLHRQEGAYSFGALVIEVE

Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+) EC: 2.5.1.18 Subcellular Location: Cytoplasm Sequence Length: 120 Sequence Mass (Da): 13381

A0A2A6B4F5

MKWRDEYFEPYQWTADQQETQSECMRQSISGNDILCQAESGAGKAALLVIATLQQLDILDGQLSTLVLCFSRENVYKIREYYERFAKYMAIKTEISLGGMSCDKDREIFEKESPHIVIGTALRIRNIIQSGSLKMDKFKWTFFYLENYGFDVKGKANFAFLTDSH

Function: RNA helicase. EC: 3.6.4.13 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 165 Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. Sequence Mass (Da): 19117

A0A183LS69

MNSKHSSPSVGLKRLYSLLKLLLNITASVTDSLDDYVVCGNQMLTDNLLRWVLGERGQLRHVYVKHHRVGETLPPSQYTILDDVIYTIKIETKDDNGNWVPFNADDVQLEFVRIDPFIRKKMEHKNGEYKLVMKLPDVYGVFKFVVDYYRVGYTHLLSVTQVPVRPFTHTQYERFLVAAYPYYGSAISMMIGLILFSFVFLYLKDDKEKGE

Pathway: Protein modification; protein glycosylation. Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 211 Sequence Mass (Da): 24526 Location Topology: Single-pass type I membrane protein

A0A536ZB31

MSELQVGLLVVGAVVVTAVFLYNKWQERRYQREAEARFASHREDVLMRSGGGIGLGTPLTPGPEQFGPALVSFEAEHQGVGHPGRGLSEFLDFIVPIETPQEVSAAALIGATAAALERCSKSISWEGFDETAASWEPLDPDRSYSRLRSGMQLVDRRGAADAEELAAFGAAMQKAAASVGALATLPDPAPALAKARELDRFCGEIDIRVAVHIISDAAPLKGTQLAGLAKAAGFRLDEPDGKFRLPDEAGRIICALANFEPTPLSVDGLNALSTRGVTLELDVPRAPYGAFNRFRQSAQMLARELKARIVDDNREPVGPAAFDAIGAQLQAVHASMEARGIAPGGALALRLFS

Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins. Subcellular Location: Cell inner membrane Sequence Length: 353 Sequence Mass (Da): 37493 Location Topology: Single-pass type I membrane protein

A0A662FXH8

MKIAYLVKSSTAHTSPDFNIRSIASTSGRFDLILRSILSAFSMPNRFKGMIKFYALLEGPPSPPLVIEIDGNRVSSLPESEIDLCEILIDAMRGRKFPGIKLYKLDFRKLVTNLIREFKPIYLVEDGSPIQEFNFNRKVNYLFILGDQKGLCVEQERFLNNVNATRISLGPVSYLTSQCITLVNYFFFKKIT

Function: Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs. Catalytic Activity: pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine EC: 2.1.1.257 Subcellular Location: Cytoplasm Sequence Length: 192 Sequence Mass (Da): 21916

A0A811KZE1

MCSDGAGFTKDFPGLTRHLTTLDIQFKIPFRRTILSAFGVIPASSRFITKLLSNKTRNGTSLANGTSGAKTLASGTNGTHMPSSGVYGITNRAVSANSTINLTSGTNGTINLVSGTNGITNLASNANGTPNFISGANAPKIPKQTQNPQPTGKAICLVVGGAEEALESHGNVYKLRLNDRKGFCRIALKTGSYLVPVYAFGETSGYRQVRNPIGSKLRDWQTKIKKVWGFSPVLAYGKDLIPGLPSVTPFEGEIVVVFGSPIPVTQLDDPTDEQVDQLHSLYKTKLVALFEEHKGNYGIPKNVQLSFY

EC: 2.3.1.- Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 308 Sequence Mass (Da): 32981 Location Topology: Multi-pass membrane protein

A0A6A4WDS8

METVSMSMPNYSYVFKFEEDFAEKERRQWMSENWYVCMYYIGAYMIFIVVGQHYMQSRPRFELRNTLALWNFFLAVFSIIGTMRTVPEMLFVLRHFGLHHSCCVAGPSFVQNNTVSAFWSYLFTMSKVPELGDTVFIVLRKQPLIFLHWYHHVTVLIFTWYR

Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA EC: 2.3.1.199 Subcellular Location: Membrane Sequence Length: 162 Sequence Mass (Da): 19521 Location Topology: Multi-pass membrane protein

A0A7S3IW43

VGDIIDVKSLNIVEDRTPAPGFLSEADLITMMEANGIGTDASIPTHISNIIERNYVTVKEGRKLVPTPLGQALVKSYCEIDPELVLPKVRSNIEKSCELISKGRAD

Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. EC: 5.6.2.1 Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. Sequence Length: 106 Sequence Mass (Da): 11519

A0A426YQG5

GNGGEETWSHRLVRRRRDAHRPEEGPIRSVIDHLSGVITPQMLEFMRDLREVVKDPALYFVVTVGVVGGSDLVKITEQLGKPVMNDYDYVFSENGLLAHKNGELIGRQSLKSFLGDNSLKVRYSILHVIHEAF

Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Function: Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose. GDP-mannose is an essential sugar nucleotide for the synthesis of D-mannose-containing cell wall polysaccharides (galactomannans and glucomannans), glycolipids, glycoproteins and the antioxidant L-ascorbate. Catalytic Activity: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate EC: 5.4.2.8 Subcellular Location: Cytoplasm Sequence Length: 133 Sequence Mass (Da): 15026

A0A7T4T5L6

MAWQAEALCAQTDPEAFFPEKGGSTRDAKRVCSECPVSTACLDYALAKDERFGIWGGMSERERRRLRRQSR

PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO). Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit. Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA. Subcellular Location: Cytoplasm Sequence Length: 71 Sequence Mass (Da): 8084

A0A2A6CRF0

MSIACVATHRRRTTFTEEYLRMADQSAGSGHIKSKSRNGFDVFINFTDPHRVMCGQPNSSIQYFMASRGDLNHGFPHNQTLTNFIQWQQYYICFSDGLIWTINAFTKAWNVVTVRNSDDFEWQPNSRHDFLHTEDDRMTLVKFLPNRANCERVILHEYTLFVHNDNHLNTEVHTPITSSRSGRHPSEISQSTTSSTNASHNSSFSQSHGSIDSTTPIFSTQSSPSASEPLLEPENDDISECSTGQSATALESSDKSDDKSNYLSCKICLIEYGNRARSAIVPCGHLACSNCIRQSMKENNRCPFCRKNIECTLRIYE

Pathway: Protein modification; protein ubiquitination. Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC: 2.3.2.27 Subcellular Location: Nucleus Sequence Length: 317 Sequence Mass (Da): 35917

A0A811JSG6

MQAAARLIEKVKSRHDDDVIDRANYVYTATMFGMFATITMAKQYVGEPLQCWIPPEFKGWWEKYSESYCFVENTYYANIHEKLPDSKADRESRELQYYQWVGFMMIGQMIFFILPKAVWNSLNLKTGLNIQSLISTSKLTLKKGNNAVIKDNTKDDIQKASEYMKTLHRFNKDRISTQSRKPLNAKFWNGYITKLYLLFKVINLFNSIIQLYALNRFLGPKYTFWGYGLLMDLLQGKQWQESGHFPRVTYCDVDVRLPGDVVAQYTLQCVLAINMFNEKIYIFIWFWLFGLSILNFLNLCNWIFLVLSEKNAIKFVQTQLAYKNVDLDSVKTKEFMGSYLYLDAVTTLRLVQLNCGDFVSSDLISYLYKDYAPVIEETKSEPELPVEAKVPPMLQSDPEKQAPIHFH

Function: Structural component of the gap junctions. Subcellular Location: Cell membrane Sequence Length: 407 Sequence Mass (Da): 47559 Location Topology: Multi-pass membrane protein

A0A811L1S0

MGAKLILTSVLIAITSLYVYNRITAEPEKVNWPKAGYFGPGKPKPDDEKVYPFKIQVPEAAIKDLSSRLKNVKISHDDLEDAVGMTYGFTKKLLHVFKDYWLNNYNWRAEEEKLNKLSHFKTEIEGINLHFIHQKSDKYKKVLPLLLSHGWPGSVHEFSKIIPILIDPKSHGIQSEYAFNVVVPSIPGYGWSSASAKTGMNAGAVARIFHKLMIRLGYNKYLVQGGDWGSVIVANMARLYPEHVTGCHLNMFSSFRPDSLLQSLLITVAPGYFLHEESLKDYNIFKTLKFMIINGGYFHIQATTPDTLGIGLNDSPIGLLAWTVEKYILATNLKYAQNPDLKEITKRISMDHLLTAVSLYWFNGNMLQATRLYKENTHSAELMQLHKQYISVPTGYAAVENDAVPAVPKRVIETAVNLTHYSFIPDLGHFFALEGPKQLAMDVFKFVDDLQ

Catalytic Activity: 1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-yl)methyl]methanamine + H2O = 2-{[(4-methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol EC: 3.3.2.9 Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 451 Sequence Mass (Da): 50982

W8CAS9

MAENKTDSNVLTSAARNSSSSSDSSTDVPVGPYPEDKLNTLMNKCWTDAIIKSGVGFGIGFLCSVLFVRRFWPPLLGASFGLGVAYKECERNLLSLTECEPIFEVKGKRIL

Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Subcellular Location: Mitochondrion inner membrane Sequence Length: 111 Sequence Mass (Da): 12095 Location Topology: Single-pass membrane protein

A0A0Q3K901

MVATFASMSKVPGTRDLWSYHSQRQFVGILITFSRGLRPQETTEQHQLIQIHSIDPSMARATRTSTMVLAAALATLLLLASAPALATAARTAPAADKASPDEKSSTAAAADVDCEGGAETAEECLARRTLAAHTDYIYTQEHHN

PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion. Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation. Subcellular Location: Secreted Sequence Length: 144 Sequence Mass (Da): 15424

A0A497FX20

MKKWEKISILLELALRGAILSPIEISTVEMAKILGLSQQSVSRKLIRLEEAGLIARRMRRRKSIILITDKGFKLIYEHYLKLRKIFDKTTQTIILRGVAVSGLGEGAYYVTIPYYYEQFKERLGFSPYPGTFNVKLTKDSTKMKQLLLYTPGIEIEGYYDGKRMYGGVKCFRVVINNEIKGALLLIERTHHEPDIVEIIAPVCIRSTLGLSDGDFVVIKVLLNDL

Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1. Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). EC: 2.7.1.161 Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+) Sequence Length: 225 Sequence Mass (Da): 25672

A0A965CAD4

MSTQNNRWNSALIILLGFSCLLYLYRIDKPSAPFWDENYYIATTERYKAGLAHLESHPPIGLMLIAAGDWLTGANSTLSTAPLARERHVSGDQIPKGYSFVGIRLFPSLFAILCIAAFFALLRRCSGSDSVALAASVLLLVENSFITHFRAAHLDSIQLFFVLCTIYQLVVVWKRNLAIGVKDFAIFGALCAAATLVKVNSVFLLALAPVMLLRDLSFVRSASRYGKFDRVFTNLGGLSGGAIAVCFAVFALHTILGSHTPDRNSPSGQVTWAHSSDTYKAYYTGQEGLSFFVVLHVIRDYGRFMNQDHRGVPKLDICKPGENGSHPTSWPLNRKTINYRWDSSDGRTSYVQLVGNQVNWAIGLIGVILAISITLARRIFKSTTVDHRVGEFIELILGLYLLYMAIVFYMAEQRVMYLYHYFVGLLLSLMLAGLSFKAIIEIHRIKRVKANIILVTVALASTANFAWLAPLSLHYPLTKAECEARNFLQRVVECQ

Pathway: Protein modification; protein glycosylation. Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+) EC: 2.4.1.109 Subcellular Location: Cell membrane Sequence Length: 495 Sequence Mass (Da): 55168 Location Topology: Multi-pass membrane protein

A0A811K8E1

MGANCNIVCVHCGAEATDLYRNYGKNVIKLCECDNCGKFVDHYIEYDSVLIYIDLLLQYTAAYRHVFVNRVYLVKSLWRIVCLFSICEAYRKWAVRMESANKSVLDGFIDLEWKFYECIVESLSEIAAFGFSTLGFSLIFDLKTKLSLRSVFWISCCGYYGKAFVLLAVIWNLHHTWEYVFLIEAFLILSHYQIQNILFSDSPKLNALMVLLSWITSYLAGSYCHIVFDYTNQNYKSWFDYIRAL

Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes. Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 245 Sequence Mass (Da): 28618 Location Topology: Multi-pass membrane protein

A0A0N4THY5

MTISYTGNFCRLLIRWKGSLWRLVWRELFIFLILYYIIRLIYNQILPLLDKENPEKYRFEFERIAITFDQYTRMIPLTFLLGFYVSNVVIRWWRQFECIPWPEDILSLLCTLIPGKDIKSQQRRHTIARYVNLVAALVYREISSTIRRRFPSLSHLVQSGLLTETELQLINECSVSTITYANLT

Function: Forms chloride channels. Subcellular Location: Cell membrane Sequence Length: 184 Sequence Mass (Da): 22064 Location Topology: Multi-pass membrane protein

I1HU91

MPLSAAATEAAIKPIPRALSITAAAAAAVTTSLLLISAVVSRARPDPPSPPPSTSASTTAALPPAPEPSPLLPDHPRPPPCPPNASHLTPCHEPPPSGERHCPPPPPPPHPPHSPDDPPPHPPHSPDDPPPHPPHPPPPPPHCRVPPPPGYHPPPPWPVRRERARYANVDLPLLTAAKTAPSGSLDPARARGEWLVFPKGVGTYVEKLERVVPLRGGTVRTALDVGCGVASFGDYLLSYGILTMSIAPRDIHDAQVQFALERGLPAMIGALGAHRLPYPSRSFDMVHCADCHVSWTAHDGRYMLEIDRLLRPGGYWVVSSAPISWKAPNKHLNWTTVSIDGEQSAMEDIAKKLCWKKVANKGTITVWRKPSNHLHCAQEANFLRSPPLCTEDNPDSAWYVNISTCITHLPRVELVSDIAGGAVERWPQRLAAVPPRIAKGEIKGTSIQAYKHDNSIWKRRVGLYGKYLEDLSHRSYRNVMDMNAGFGGFAAAMSKYPVWVMNVVPANITDNTLGIIYERGLIGTYMDWCEAFSTYPRTYDLIHANGVFSLYINKCGLLDILLEMDRILRPGGAAIIRDAANVVLEVKEAADRLQWRSLVVDAETETSDPQKLLIVDNSLPPQGS

EC: 2.1.1.- Subcellular Location: Membrane Sequence Length: 624 Sequence Mass (Da): 67956 Location Topology: Single-pass type II membrane protein

A0A662HXI0

MDFQEVMHLKHLSKTIRPKGGKTVKIEAWVSENKLEKVMFSGDFFAYPAEALEELEQRLAGSPLNVEEIKSVFKQYKGKVSLVGASLNVLEEELLRLLGLSAE

Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. EC: 6.3.1.20 Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+) Sequence Length: 103 Sequence Mass (Da): 11593

A0A811L3W2

MGTESTKNVANWEKWLQLAQVYYFFTLFVVGSVFTPILLVVLLFTRFWWYSVFYATWTIVHKFYFFTLPKPWEWLRNHTFWDHYGRYYPMKLHKTAELPPEKNYLLIWHPHGILSFSAGATVMTNITRFTETYPGITRYAATLPLHFLYPLRSFCMAMRGFIPSNFSNIFKVVSHKQGGNAVILAVGGAEESLESHEGNYKLVLNSRKGFVRLALKSGCSLVPVYAFGETSTYHQVLNPVGSKLRRFQTQVKKILGVAPAFFYGTMGFWRLYGPFPLSAELNTVVGAPIEVEPVAEPTQEQIDQLHDTYKSKLIELFEAHKAKYAVPEDQHLEFL

EC: 2.3.1.- Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 335 Sequence Mass (Da): 38653 Location Topology: Multi-pass membrane protein

A0A2A6BD57

DLDTSQLQSNRSTFLWSVDDPFSGARAYLFGTIHVPYTAVWDQISPRVKEAFDRADSVAFEVDLHDEIAMRKLVRCKNLRKRQNVHSYLPNSMYKRLNKVMNSFYDRIYNALAGKNAHSGEEVEAVRIQAQRIHEAITENWDRKRPEWLLLLLYQLCENLNERMGSAPILDLFLAETASASGKTMHSIESVEEVLFAINYTIAYLEKPEKLIAARRKERTLSDIVRDYRCGQVEHTMKSTRDLAIVIDPEMDRKEQLIEDQLKDDILVTRNERMARRIASLMQAKPHSKMFAAVGTGHFFGPRNILDHLNNIGYVVAPVAETDFVRYSHARREHRVNSLWQRQSEEIEETRNDMDVIIELAELPNHSVNRAVTVLTALTVIALM

Cofactor: Divalent metal cations. Mn(2+) or Co(2+). Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway. EC: 3.4.-.- Subcellular Location: Cell membrane Sequence Length: 384 Sequence Mass (Da): 44340 Location Topology: Single-pass type I membrane protein

A0A2A6BMX3

MNFLGDPFKLIKPRFDDSGVDRLNYYYTPVVIIVMAVTITAKQYVGEPLQCWVPAQFSRAWEQYAENYCFVYNTYWVRPGEEIPSDVDERLAAQLIYYQWVPFIMIIEAGLFHFPAKIWAVLSKTSGLNLAGMIGAVVKAEEGNDESKLQSAALNVCHLLENSNKMRKLRTVGASRMGKYARLGELDGTYLSNVYLVAKLIYCINTVVQFTSLNKFLKQPDMFWGASVLNDLVHGHNWEDSGNFPRIAMCDFEVRTMGNVQRWKGPQHMTGLLTLIDSLAHFITMKMPSRRQRFVKRFITCPPEEKAVLEDFTKEYLNPDMFLILKMIDGHTSEIVTGNILQQLYDNFRNSTETLNDHPYLRHLDLARQESEFASEDPLSNDNTVQEAFLRTLQVPSPTENFEFRRLSMTRSPISR

Function: Structural component of the gap junctions. Subcellular Location: Cell membrane Sequence Length: 416 Sequence Mass (Da): 47909 Location Topology: Multi-pass membrane protein

A0A0N4TDH9

MVYSKKQTFRIVNWLLFIVASISWICVFIASVNISKRYIENLVHGNTKLQNTQQHIAVALPFLYSHYCSHYSLHSRHNEYREQAAVYYKQRFIILLKGKAPNDYYVWSSYPLLNHAEETHIRIAVIEEYESDFNDDGKPDL

Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling. Subcellular Location: Cell projection Sequence Length: 141 Sequence Mass (Da): 16688 Location Topology: Multi-pass membrane protein

A0A023TLZ2

GIWAGMDGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWSVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 213 Sequence Mass (Da): 22877 Location Topology: Multi-pass membrane protein

A0A811JWF0

MTTFNIYWPKISGGEDVEGQMMDSSSSGYRRMGGRSAPPRNIFFFGVLLILVVLFSVFFLYLSASSDLTALRDEVHYLNDQISKLKSDLLNVNSQLEGSNNKLTACNVEIKQKTSELESCTTQKSADRTKVEALTKQNSELQIEKKAIEDEMTSKMAAMKTVGVNQEAILTKQNETIDLLRRDLILKDELIQKLQKNEANPVLNTDNGQAKSLDATSSSLNGQAGTIGRLSSVNDVNRQASSVNVLNGQSSRAVGQVTTTKFNENINVVLRPVENLNGGVMSNGQAQNIINNANSLKPIQNAMENVAPKPQEVAKPVQAQVLDSAQNPSADAVLIPPQAQPGARVRVQEQTNSEQDGELIQPVEAEFSQNSLEVTTLKSLQNLQDEEYDILVIVCETADSFDLGHALQLLKPRGQLFVIEKEGGKSTIKKDLEFSGFDDINVDEKSGLTLAKARKANFSVKSQPLKLKSKKKIDLDNLQGDALEEDDLLTSEDLKKPNNPMCTPNPTDKKKRACKNCTCGLAEQEAEEAAASGNIKSSCGNCALGDAFRCSSCPYKGLPPFKPGEKVLLNDIDDL

Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. Subcellular Location: Cytoplasm Sequence Length: 575 Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation. Sequence Mass (Da): 62745

A0A158PDT0

MSALFLPDKSLTCRIESTAMLYIAKYFPSLRYTILREKKCRLLINDISAIMAHREELEVLKNYGFDAAFAEQIDFCGIGVIRYIGIKNLLWISTTPIMDAVSYNLGIPAPPSYVPTIEENDNNDIMTFWQRAFNIYMYIGAIFIHRWSTNMMTEIFRKVDPDFPNIREIASNASLCFVNIDEMFDLPRPIIQKNVYIGGLGVQKPKPLDQKFSILMEKGEKGVIIVSLGTIAPFHAFKQVTKVAFANVFKSMLDYHFILKIEKGRSKEQRSTKFRNLLENRHEETNRMQDV

Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP EC: 2.4.1.17 Subcellular Location: Membrane Sequence Length: 291 Sequence Mass (Da): 33616 Location Topology: Single-pass membrane protein

A0A183LI06

MWRYVALFSGARKYCSTQSNYMLNELCIVVDKCDHVLGFANKKVILFGKSLLHRAFSLFLFQEDTIQKRSANKLTFPSLWSNTCCSHPIMNFPDELIESDAIGVKKAAQRKLFHELGINNTFVPLNRIHFLGRVLYTAPNEPCTQAAFAEHEVDYILVSVLDPVASKLFSCSSFPFVLF

Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). EC: 5.3.3.2 Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate Sequence Length: 179 Sequence Mass (Da): 20364

A0A1C7L1W0

TLYFIFGIWSGMLGMSLSLLIRMELGNSNPFINNDQIFNTIITAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNLSFWMLPPSLMLLIFSSFIEGGAGTGWTVYPPLSSNIAHSSSSVDLTIFSLHLAGISSILGSINFITTTINMKPKIMKFESLPLFIWSVLITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 219 Sequence Mass (Da): 24160 Location Topology: Multi-pass membrane protein

A0A4P8JBM3

ILILPAFGVISHVVSHYSHKKSTFGPLGMIYAMLAIGFLGFIVWSHHMFTVGLDVDTRAYFSSATMIIAVPTGIKVFSWIATLHGSRPKFEPALLWALGFIGLFTMGGITGIILSNASLDVALHDTYYVVA

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 131 Sequence Mass (Da): 14216 Location Topology: Multi-pass membrane protein

A0A0N4TTY9

MLFTCTVHQLRSLGIRCLANSAGDSHTHYPISTVTRKSIDEVLEPSQAPTKIKVSDEVQKQTVDLSGVPVDFLRSRRVRIYRPAREATQSGWARTRTWKIELDNLERWENSLIGWSSTGDPLSNISMAMDFASKEDAVRYCETNNLNYEVIEPNERYVLFCYVLKLSGLPPGDYKMTTLSPIQCKRTQILGLEHLLRKLICTFASAIFYTNKAFIVFNFHVHIYYGY

Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Subcellular Location: Mitochondrion inner membrane Sequence Length: 227 Sequence Mass (Da): 26067 Location Topology: Peripheral membrane protein

A0A0Q3GP92

MEAAAAATTTNKAPSMADPEDDFDLSRLLNHRPRINVERQRSFDDRSLGDLYLSAMDGRSGGYMDSYDTMYSPGGGLRSLSGTPASSTRHSFEPYPLVFEAWEALRRSLVCFRGQPLGTIAAVDHSAGEVLNYDQVFVRDFVPSALAFLMNGEPEIVKNFLLKTLLLQGWEKRIDRFKLGEGAMPASFKVLKDPKRGVDTLSADFGESAIGRVAPADSGFWWIILLRAYTKSTGDLTLAETPECQKGIRLIMNQCLAEGFDTFPTLLCADGCCMIDRRMGVYGYPIEIQALFFMALRCALLLLKPEGEGNKDTVERIVTRLHALSYHMRAYFWLDFQQLNVIYRFKTEEYSHTAVNKFNVIPESIPDWLLDFMPSKGGYFVGNVSPARMDFRWFALGNCVAILASLATPDQAAAIMDLIEERWEDLVGEMPLKICYPAIEGHEWQSVTGCDPKNTRWSYHNGGSWPVLLWLLTAACIKTGRLKIARRAIDLAEARLAKDSWPEYYDGKLGRYVGKQARKHQTWSIAGYLVAKMMLEDPSHLGMISLEEDKAMNPVLKRSASWTV

Function: Invertase that cleaves sucrose into glucose and fructose. EC: 3.2.1.26 Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides. Sequence Length: 564 Sequence Mass (Da): 63368

A0A811KMH8

MSVCTNRWGFNLDKRKTSTLILVAVLVHTCTASITEKDVIDKSKQSEETTLNSKDFENAPSKEEDLKRIGIKVPDDPTMGSKNEGDILMPKLKEKVFLDERTGLGRNAIRQSYRKWPNNEIPYTLSTQYGSYSRSVIAKAMNEYHTKTCVKFVPRDTKKHRDYVYIHPDDGCYSLVGRVGGRQPLSLDSGCIQTGTIVHELMHTVGFFHEQSRYDRDQFIEIVWPNVINGADDQFEKYGTNVIDQFNEPYDYSSIMHYGPYAFSANGKRTILARRNGANKMGQRVQFSEIDLRKINRLYQCDSQSMIKKPPRPQLPVQVSTTTITPITISTTTISEISTAAPTITLSVKPTPTSVKKQPSVTELSHNTETLITERNNNLSKKDDKSETNTQVPITVSHPKSRQFMLFRVPRRFRKKSVTLSSNQTDAASRFTAVGAKTKAPHLVRPRQSQQQLPLSRRPQPIQQQNLQPQSKPQPKMRPPPSPVKRPHESASTKIGDAPSGQCRCLATAISTLKSAIRFARSRVGRVRRIAQPRLSVHCVDKSAACSRIHQTSCESPLTQLLCPRVCGACSDTTFPADFNIDPAHQKPTFFPPPIFAQLASSQQIGGPEVGLNPTEAINPASPFNPQTGHTFGHQFNRPQNQFENQPVNPRFENRPAHISPNDQPIFPINSQEPEIDLGSALAFRTRHRAEGRNVNPNQQKANSNNKDDNSKTKSQESNISGSQAPNENPDITFKLDRNVLCFDVSEAEICAHVAEVQLCAVRLDCARTCGLC

Cofactor: Binds 1 zinc ion per subunit. Function: Metalloprotease. EC: 3.4.24.- Sequence Length: 773 Sequence Mass (Da): 86510

I1IH32

MAILACLLTVVPTILGLAIRRLRILLRFPSPHAAAGFFHPYTNDGGGGERVLWCAVRAVQDLCPGLPCAVFTGDADASPDGLAARALDRFGVRLLRPPQVVHLNKRKWIEASTYPHFTMIGQSLGSVYLAWEALNKFAPQFYFDTSGYAFTYPLARLFGCEVICYTHYPTISSDMVERVKQRNSMYNNNSRISGSIWLSRCKILYYTIFSWLYGLVGSCAHLVMVNSSWTRSHIVNIWKIPECTKRVYPPCDTSALQMLPLERSTMPPILISVAQFRPEKAHGLQLEAFALALQRLDPDSIKPKLQFVGSCRNKEDLERLQKLEDRSVELRIDELVEFHKDISYRDLVQLLGGAIAGLHSMTDEHFGISVVEYMAAGAIPIAHKSAGPMMDIVLEEDGHQTGFLASDKEEFTEAILKVLRMPETGRQEMAAAARKRAQRFSEKRFHEDFTDAVRPILSATEGRHVQMSPLIE

Pathway: Protein modification; protein glycosylation. Function: Required for N-linked oligosaccharide assembly. Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H(+) EC: 2.4.1.131 Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 472 Sequence Mass (Da): 53048

C4PV68

HPEVYILILPGFGMISHIISQESSKKESFGVLGMIYAMMAIGLLGFVVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGIKIFSWMATYHGALISFNPSSLWSLGFIFLFTMGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAILAGIVQWFPLFTGLTLNNKFLKTQFMVMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYTQWNAISSIGSLISLVSVFYFIFILWEAFAVKRMNLSASSMITFIEWFQFLPPASHSYLEVPAVTSNF

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 276 Sequence Mass (Da): 30955 Location Topology: Multi-pass membrane protein

A0A967RIF3

MMEAAALGKPTLFGPHAFNFRQTVDALLEDEGAVMVKDEQDLLQTMQKCLTDADFAQKIANNGRQVIKKNQGATQKTIEQITALLNDRYI

Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis. Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+) EC: 2.4.99.12 Subcellular Location: Cell membrane Sequence Length: 90 Sequence Mass (Da): 10025