ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A8T6SBL1 | CIVDMPVELGISEVLKMKAFEAGGLTDYEEKAKVAAKAMETQNAIYVHLKGPDEFGHDGDAIGKMKNIEEIDQRFFKTLVENIDTSKVAIVVSADHSTPCINKGHSDDPVPVLVSAEFIKGDSSVRMTEKEAEKGKIGLIAGADVVSTALELIKSQK | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 157
Sequence Mass (Da): 16932
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A0A1B6GAB3 | MGFFLGSRLSFIIIVAIAGFVAYDINKHGSFRGSKTGVFLRDCGALRYGELAWTRFRSYSQQAYRWSQKHVPGYMSFMRESLTVYLIIIRDVVTSLATHLWASISQIWHYFEDKKPVIAKWVDQYFPGLSDRVNSWLSQSWSFLLQCAKFVIQWLKDNIFVGSLSAENLQRLSWEAFNTTQTFARKTLSWINGKMAPVIVGSST | Function: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 204
Sequence Mass (Da): 23507
Location Topology: Multi-pass membrane protein
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R7TV57 | MSGIGKLLRGCLEFNALKKPKLLEQFKAVKEHPAPKAVTFSCMDNRIIITKLLQCDVGDMYLVRNAGNLVPHCETLSYDAVSTEPGALELGCVMNEIPNVLVCGHSDCKAMNALYGMRDQTQIKEGTPLTLWLKKHGHSSVKRYNELLNSPDGIGPLEFKIPGKTLRAYIDPDKKLSEVDKLSQVNVLQQVENACSYDMLKDKLQSGQVNVTALWFNIQTADFFMFSKEKERFLEVNESTIDHLVSDAGGH | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 251
Sequence Mass (Da): 27988
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R7UTF9 | SDAILFHGRHINGRNVPLERDPRQKWVFYEEDPPSHTWRNKKDSFRNWFNITATYSHTSDIPLIQRRLRCREKPEERAARMVNKVNYATGKDGRALWVVDECVTPSQRERYVEELRKHMIVDVFGACGKPLCNSSSSCLEELINSTYKFILIFEKALCHEYLSADLSSILSANVIPVVLGLYDYSNMLLEGSFVEARRFESPQMLAQYLEYIDQNDKVYNKYIRRKYSMECVPLESQTFPCQLCHYLHLNVKTQKEISDVKRYWSE | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 266
Sequence Mass (Da): 31353
Location Topology: Single-pass type II membrane protein
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R7TFU0 | FPRVTLCDFKVRQLGNIHRHTVQCVLPINFFNEKVYMVIWFWLAIVSIINVINLITWIARTLFRLDQLQYIRRHLRYMDKMDRPEDKKISRRFVYEYLRCDGVLVLKLVAMNTSDIVASELTAELWDYFKSNPPTFYKKKNDFVDV | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 17641
Location Topology: Multi-pass membrane protein
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K3Z2P3 | MAARCYTAATVVFSSRAGAPDLSLSLPAAAAAAVPSARPGPRGAWTYGGGYSHRPATGRAMGSAPSSSSFPSPQTPPGQAQEKANTSLTEEEWKKRLTKEQYYVTRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYKPIGDNVKSKLDMSIIFMPRTEVLCAACDAHLGHVFDDGPPPTGKRYCINSASLKLKPQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer.
EC: 1.8.4.12
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Length: 212
Sequence Mass (Da): 22840
|
A0A2E4WXX0 | MARLRDIDLSKALFVLPNLFTMSSIACGFYAILKASSNEPTSRDFLTACLAIVFAAIFDTMDGRVARLTKTQSDFGVQLDSLADLVSFGVAPGVLVYRWALQDHGVLGFLFAFVFVAAGAARLARFNVLVARGQEATSDFVGLSIPLGALAVISLVGFCVRAEIDPASFHRLVTLYVVVVSFLMVSNLRMRSFKDFRVRGSALLGIAILSLIPAILAFFLREPYGVLLALSWLYIFYNSIRAVWRRVWTAAPELVAETEEVSAEI | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 265
Sequence Mass (Da): 29045
Location Topology: Multi-pass membrane protein
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K3Z4V9 | MASSSAVPSSAVAVAAAVLLLAAVGAEAETRKYQFNVQMASVTRLCGTKSIVTVNGQYPGPTLFAREGDHMEVTVVNRSPYNVSLHWHGVRQLLSGWADGPAYITQCPIQPGGSYVYRYQIVGQRGTLWWHAHISWLRSTLYGPIVILPPAGVPYPFPKPDEEVPLMFGEWWRNDTEAVIAQALQTGGGPNISDAYTINGLPGPLYNCSAQDTFRLKVKPGKTYMLRLINAALNDELFFSVANHTLTVVDVDALYVKPFAVDTLVIAPGQTSNVLLAAKPAFPGARYYMEARPYTNTQGTFDNTTVAGILEYEDPSSSSSSSSSSSATTAAAANLPIFAPTLPQINDTNFVANYTARLRSLATAAYPAAVPQSIDRRFFFTVGLGTHPCAVNGTCQGPNGSRFAAAVNNVSFVLPTTALLQAHFAGRSNGVYTTDFPAVPLMPFNYTGPPPNNTNVMNGTRVVALPFGTTVELVLQDTSILGAESHPLHLHGFNFYVVGQGFGNFDPVNDPAKFNLVDPVERNTVGVPAGGWVAIRFRADNPGVWFMHCHLEVHMSWGLKMAWLVQDGSLPNQKLPPPPSDLPQC | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
EC: 1.10.3.2
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Subcellular Location: Secreted
Sequence Length: 585
Sequence Mass (Da): 63047
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K3ZQD2 | MLRAAAAAAAVFPARFAAAPAVAAAEDLRSPLLRVLGTLRGGRGSVLLGRRARFCSNSSASDSEAAAAEAEAKAEDATVAEGEADGKASSAIVPTNPKIEDCLSVVALPLPHRPLFPGFYMPVYVKDQKLLQALIENRKRSASYAGAFLVKDEEGTDPNIVTGSDSEKSIDDLKGKDLLKRLHEVGTLAQITSIQGDQVVLLGHRRLRITEMVEEDPLTVKVDHLKENPYNKDDDVIKATSFEVISTLREVLRASSLWKDHVQTYTQHIGDFNYPRLADFGAAISGANKLLCQEVLEELDVYKRLKLTLELVKKEMEISKLQQSIAKAIEEKISGDQRRYLLNEQLKAIKKELGLETDDKTALSAKFRERIESKKDKCPPHVLQVIEEELTKLQLLEASSSEFNVTRNYLDWLTVLPWGNYSDENFDVHHAQKILDEDHYGLSDVKERILEFIAVGKLRGTSQGKIICLSGPPGVGKTSIGRSIARALNRQFYRFSVGGLADVAEIKGHRRTYVGAMPGKMVQCLKSVGTANPLVLIDEIDKLGRGHSGDPASALLELLDPEQNVNFLDHYLDVPIDLSKVLFVCTANVIEMIPNPLLDRMEIIAIAGYITDEKMHIARDYLEKNTREACGIKPEQVEVTDAALLALIENYCREAGVRNLQKQIEKIYRKIALQLVRQGVSNEPDQEALIVTANEEPSSGDGAIAKDEILKDSAVEANEANLAKEAVLHEVHTTEAVLHEVHTTEAPKEDSVSEGKDTDGAKEDGADKAIEKVVVDSSNLGDFVGKPVFQAERIYEQTPVGVVMGLAWTAMGGSTLYVETTKVEEGEGKGALVLTGQLGDVMKESAQIAQTVGRAILLEKEPDNQFFAKSKVHLHVPAGATPKDGPSAGCTMITSMLSLAMGKPVKKDLAMTGEVTLTGRILPIGGVKEKTIAARRSAIKTLIFPAANKRDFDELASNVKEGLEVHFVDTYGEIYDLAFQSDARTETS | Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
EC: 3.4.21.53
Subcellular Location: Mitochondrion matrix
Sequence Length: 988
Sequence Mass (Da): 107938
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A0A5E7V9C3 | MSRAPDTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSGRFFIRVEFRQPDGFDEQSFRAGLEERGQAFGMIFELTAPNYRPKVVIMVSKADHCLNDLLYRQRIGQLSMDVAAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEESGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEAVDHSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; formate from 10-formyl-5,6,7,8-tetrahydrofolate: step 1/1.
Function: Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
EC: 3.5.1.10
Catalytic Activity: (6S)-10-formyltetrahydrofolate + H2O = (6S)-5,6,7,8-tetrahydrofolate + formate + H(+)
Sequence Length: 285
Sequence Mass (Da): 32278
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A0A3R7YI94 | MVAGVMFLAWRVQMNGSSTTLYTWSIYENEFAHLPSFVSKAMSYAHVHTLYLWKLLWPQYLCYDYGWNTIHAVTSIYDVRNLASSVAYMAVVGAVGTSASHRRTSPLFVLLVLGICPFVPASHVMFPVGTILAERLLYLPSVGFCLVVGYATERVLLAATPASKPKLVALLGLVLAVATSRTIRRNLDWHDEHTLFQSALSVAPTSVKVLTNLGQDILPKDARTAVLYLERAVALMPSYSLGHLNLAAGYAALKKPLQAMHHLVQSIELVQEPKAYTSLGQHFVEFWESHVGAGQNQLAYTILAFFLNVFVLHDRAMMNASTFWDCASLVNNAAACFHRANRSMDALKLLDKATKRHPLQVVLWTNAGYMAESVGHQAQALTYFEAALRLEPDLAHLRTKLELAFKQQQP | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum
Sequence Length: 410
Sequence Mass (Da): 45563
Location Topology: Multi-pass membrane protein
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A0A290U6Q0 | HKDIGTLYLIFGAWAGMVGTSLSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTIEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFG | 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: 241
Sequence Mass (Da): 25865
Location Topology: Multi-pass membrane protein
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R7TUU5 | MDALSFRVKAIERLSKNSQLAYAQAEHIHKEVLKPGGHWTPEECAARQRVAMVVPYRNREDHLRIFVSYMHRFMQAQYLEYQIFVVEQASPDVFNRAALMNIGFLEALKLHDFDCFIFHDVDLLPLDTRQPYTCFQAPTHLGAYMSKFSYQMPYDGFFGGAVALSTENIKQMNGFSNLFYGWGGEDDDTLNRVLWRNLTVHRHAQDIGKSYMIKHEKDEGNPTNPNRGIGHEMKPDQYNRNGINSIKYIKQSTDLNVLYTRVLVSIGEN | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 269
Sequence Mass (Da): 31133
Location Topology: Single-pass type II membrane protein
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A0A7R9BQF3 | MPFYAVVRGYNPGIYYSWAECEPQVSGFSGADYRKFPALECAEAYCRDPEAFWRLGLPIRRRSRRPYRRYPFPGAHLQPAIPLRILVQARLAEDDDFHFTEDGFAICYTDGSCMGRLRNAGVGVWFGNDHVANICEPLPIPGTNNKAELLAVLYAIHAARESGLDMLEVRTDSRYAIYSLTEWLPKWKSNNWLTTENTDVQNQGEIRAIDEVRNYMEVRFEWTPGHAGNSGNSAADSLAKRGAARALTVYRQ | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 252
Sequence Mass (Da): 28607
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A0A7R9BM08 | MVNKVAIAIIAAVIQIVVALVITLPVLYTDCNQLKKCKRSNAEIEQKMVSKVATALIAAFVLVVVALTITLPILYTDCSLLKKCKRSNAEILKTILDEVPLIDGHNDFPMLLRTAIQNKLSKVDLNKSLKDDPAFNKFVYNHVDIPRLRQGQVGAQFWATFIGCSRQYNDSLHEALEQIDVTKRMIEAYPEHFEFVTNAEGITKAHKRGKIASLIGVEGGHMIEESLAVLRMFYQLGVRYLTLTHNCDTPWARYHEISAPGSGRVKGLTRFGHKVIQEMNRLGMMVDLSHTDAQTMRDAMTVSDAPVIFSHSSVYSVCNHSRNVPDDVLEKLKHNEGIVMINFYSGFIKCDVNMTESPPSNNAVIADVVEHFNYVKNLIGVNYIGIGADYCGVGVLPEGLEDVSTYPKVLEALLNAGWSELEVRKVTGLNMLRVMRQVQKVSSDWQRKGLRPLENLIPLEDVPADFSCGSSEMTALDEIYKDATLTPTGKNIRRKGQWHLTDPAAEKDNET | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 511
Sequence Mass (Da): 57016
Location Topology: Lipid-anchor
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K3ZHQ5 | MAASAKPFCSTTQQPPTPIANRLPSPSQPPALSSRAAPRFAHGLSAAAGVRASPSARRLRALARPIRASSQHQQQQQLPRRRPEYVPSRIDDPNYVRIFDTTLRDGEQSPGATMTSAEKLVVARQLARLGVDIIEAGFPASSPDDLDAVRSIAIEVGNTPVGEEGHVPVICGLSRCNRKDIDAAWEAVRHARRPRIHTFIATSEIHMQHKLRKTPEQVVAIAREMVAYARSLGCPDVEFSPEDAGRSNREFLYHILEEVIKAGATTLNIPDTVGYTLPYEFGNLIADIKANTPGIENAIISTHCQNDLGLATANTLAGARAGARQLEVTINGIGERAGNASLEEVVMAIKCRGELLDGLYTGINSQHITLTSKMVQEHSGLHVQPHKAIVGANAFAHESGIHQDGMLKYKGTYEIISPDDIGLTRANEFGIVLGKLSGRHAVRSKLVELGYEISDKEFEDFFKRYKEVAEKKKRVTDEDIEALLSDEIFQPKVIWSLAAVQATCGTLGLSTATVKLIAPDGEEKIACCVGTGPVDAAYKAVDEIIQIPTVLREYGMTSVTEGIDAIATTRVVITGDVSSNSKHALTSLNRSFSGSGASMDVVVSSVRAYLSALNKMCSFAGAVKASSEVPESTSV | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
EC: 2.3.3.13
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Length: 635
Sequence Mass (Da): 68331
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R7TWQ8 | MGHVEGKGLGKNQQGRAEIIEASKQKGRRGLGSQVKGFEAKDVDWDASKDEVTVDETVSWIETCSDPVPSIEEMRTWMLEGPNKKTIDDETEFCNPDILRDILSCKSVFDHLEGEEMRKARTRSNPYELIKGVFFQNRAAMKMANMDAVLDFCFTEPRTVEGRSLVQPNELLYFADVCAGPGGFSEYVLWRKAPGETKGFGFTLKGNNDFKLEDFYSTHSEFFEPHYGKGGMHGDGDVYNPENLMEFQEFVLNSTDQKGVHFVMADGGFSVDGQENIQEVLSKRLYLCQFLAAMMILRPGGHFVCKLFDVFTPFSVGLTYLMHRAFHRVSLFKPVTSRPANSERYIICQNKRSDSLDIQTYFWEINLRMHELRSCTSFEQSTGVQHVVPLEMMKQNEAFFSYVVQSNHDLGHKQIISLAKIQTYAQNEELQEYDRQVQIRDQCLEKWKIPNNVRKAPERAVNLMQKLQALLNQTDLSDLLCQPVMLTADNLSRTVHSVHDYRCMVVGSKEPVLLLSKGKSAVMQWNGRVQSRWERMHQVNVELPRDTVVLAERVEELKGEGRGQRKVTAVHIIDGLVLCGTDIRHLHFRERIEKLRKFMRAISRPSRSDLAPIRVKETFRLEHIGKVLTSLEMRRLKSSGLPFRLCHCCHTVENGQSSYMIPAGISLYKTMKVPWMMAATRGAQAKLYFYNTETRKSQFDFPPEAQASYESCQKTQLFWEWGQGVVLNDEQQRVTNMNHHPDKVSGNAMIQYVHEKLNPKK | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.57
Subcellular Location: Nucleus
Sequence Length: 761
Sequence Mass (Da): 87369
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Q7ZZM8 | MRLKLRNIFLVYFVVSSVGLMYALLQIGQPCDCSQHLRSGSNAHGRSRHSFVPKGPRDLSEDDQLPVIYVVTPTYARPHQLAELTRLSQTLLLVPSLHWILVEDSAERSKAVADLLAQSGLHYTHLNVQTPPVMKLKDSDPNWLKPRGVEQRNEALRWLQLNRSPKDSGVVYFADDDNTYSIRIFQEMRYTQKVSVWLVGLVGGLRYEGPLVEKGRVVGFHTAWKPHRPFPIDMAGFAVSLSLLLSHPGARFDPNAERGFLESSLLGQLVSVGELEPRADNCTKVWVWHTRTEKPKLKQEEVLEKQGRGSDLNVQV | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular Location: Golgi apparatus membrane
Sequence Length: 316
Sequence Mass (Da): 35764
Location Topology: Single-pass type II membrane protein
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A0A1I8JJP9 | MLTDAFFSGLAASPRRLSLLLAGAGAAAAAAYLLSVAYRRRRGGGRSIRGAGGAARRRALRLSVTSAEPLLHLLEQTCRDEPSELPVVCQFGDTKCRLVMKNRRRVLEKLQSLMRGGPDALEVITDFDHTLSKFSENGRRVPSSHGIMESYPDLSAEDHKYFRELYTKYYAIEICPDMSDEEKLPHMIEWWTRSHDRMVLAGFQKSVLAQTVDVSGVALRDGWHQFFDRLEELGIPCLIFSAGIGDIIQEILVHFDIRGKLIRVVSNFMLYNEKGVLRGFSEPLIHTFNKRFSAFASSEASANDLVGATDRRHVLLMGDTMGDLRMSEGCNADLVLTVGYLNDRVQDRLSGYADKFDIVCLEDPSLCVPLAVIEAAATGGTA | Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
EC: 3.1.3.5
Subcellular Location: Cytoplasm
Sequence Length: 382
Sequence Mass (Da): 42338
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A0A150IID0 | MAKLAPSILSADFSRLGDEILEAENAGADLIHIDVMDGHFVPNITIGPLVVEAVSKITELPIDVHLMIENPSDYVEMFFKSLDKNDRDVSLDYISFHIEASYHPHRLLNKIRELKVKSGIALNPSTPVNTITHLLDSTDLLILMTVNPGFGGQSFIETMIPKIKEAKKLVKGHDIEILVDGGVTEKNIKRIKDAGADILVAGSAVFNKNDSIKNNIIRLKALV | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 223
Sequence Mass (Da): 24513
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A0A2E7ZS57 | MEHRSIAVLHGGPSSEHDISVISAREVLNSLRGGGYTALSVWVDRQGLWHFAGAQAPSGSSVADPLCLPEALARLRDEDVLCAFLGFHGTYGEDGRVQAALELAGVPYTGSKVTASALAMDKPLARRILASAGVRVPAGRDLVSSDVLGNEAHVAQELVTEFGLPLVLKVSAGGSSLGVEIPNTLAEVQGALSRLAADTQILLCEQFIIGKELTAGVLSRIDGQLEALPAVEIAPKGEGFFDYEAKYDPSLTDEICPARISEHVENKCRHIGVLAHRALGCRGISRTDLILDEQDQLWVLETNTLPGLTPASLLPKSAAAVGCSYLQLLERIVATAKLP | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 339
Sequence Mass (Da): 35837
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A0A2E7ZQK6 | MDDNKRRNIKIFVSMTLIGAVLDLATKAWAEGALTQLPGQSMMIFEPWCEFALSYNQGTAFSAIFDLGEMVRLILGIASLLVVGLLGWSVTRPEVVQIEVWCYGMLAGGAIGNGYDRVFREAPSGGTGVVDFVKLNYPWGGSWPTFNVADSLLVVGVALLIIRWWTHPPTDDANVRAERS | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 180
Sequence Mass (Da): 19725
Location Topology: Multi-pass membrane protein
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A0A0C4EEL9 | MINDESASHQTSHPSIISFCHYFLLSFPSVISYCHLLLSSPSVSISWHYFLASSLLSLYTFTRPKMRFSLAVTAAFVARALAAPLTLLETEYSFPRRLVARQTVGTEANEFKNGPCRDIVLLFARGSTQDGNMGQQPGPDLANAMKAKFGADRVAAQGMSYAAILAGNLAEGGATSMESSDFADLIKDVAVKCPDARIVVSGYSQGAALVHRAMRSCSVNVKTHVAAAVTFGDTQNKQDGGRIPGFDASKTLIICNDGDMVCDGTLMVMGPHMQYQSRVPEAVNFISTLVA | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalytic Activity: cutin + H2O = cutin monomers.
EC: 3.1.1.74
Subcellular Location: Secreted
Sequence Length: 291
Sequence Mass (Da): 31232
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A0A6J1MEB9 | MDWSSGKHPLPPNANNKRLTDNNNQSMIVDLTYSLLRRSPRSHQPDAAHPLASLNNQTDDTMEVPEPAPAPAPAPVPVPVPAPAPAPAPPPPAPAGPIIFPPPLANGQKQSQDINLPADITESDEDGKHHAYECPICLENVSGRQPATTKCGHVFCYGCILSVLRVNHKCPICSVHLATRRAIKRIYI | 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: 188
Sequence Mass (Da): 20251
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A0A0U3H9B8 | MDVEVLVPLNISGVWYPVYTNNPLTTGSIGIGLVVEPRIMVRGKRSNKAEVEFNGKIIEFPNLAILKRLGELKISVQSQVPLGFGYGLSGSISLAYSYLAYELGLTSLKEALYTAHESEVVNKNGLGDVIAEYIGGGIVYRKVPGAPGIGKAEKINVSWSEQVCSKPEMALPTTVLLKKNENALTYIEEFLKNPDLTKFFEVSRKFTEELGFVSNIPNSFRKKGLIIKHGDCNKEWIQHTPATNGVLIH | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
EC: 2.7.1.169
Catalytic Activity: (R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+)
Sequence Length: 249
Sequence Mass (Da): 27413
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A0A0R3SE94 | MNEVSPRPMKLKKFLWRNSNKDESNGRTILVNSIPSLSQEARVNNGKFGNNEIISSHYKWWNFLPINLFEQFHVVANFFFLLISILYFFGETPINPVTTIAPLVTVIGISMAKDAIDDIKRHRVDNTFNRIQFMVLTHDSKDNTSSFVQRNSQDIHCGDIVICYDNSSLPCDMLILASSNLNGKVFITTDNLDGESSIKTTNALAFTQNLFTPTVKKIENDQLYNIDLGLERSTIICQNPCEDLKAFEGSLNLPHESIPLALNSVVYRGARLCHTTFMLGVAVYTGKDTKLSLNSKPGFRKFSSSAGRFNTILLCFMGAMFLLTFIITILHFIFNEKPYGSPWYYFTPVATPWRRVQQYLTLLFIINYLIPISIMVTMELQQLVLALYITKDVEFYDPGSNEKAQVNATNLADELGQIEFLFSDKTGTLTQNKMIFKSYSLANDHHIYSVEEGALFMIRSSNKASTISDPTKKSSINFLNVNATNYFSSSEDEDESAEDGLGSSDDLSSQMAKKRIYRLSKEAEQFWTNVVLNHSVEAKTSINEDTLEEFISYNAASPDEKALVDAAAKVGLTYIGLDNTVRSKDTDYNIHMVRFNPGILSGKPSKVKTRKFRVDAVIEFNSVRKRMSVMVRDEEGRCFVYTKGAEVTMLDPRRCDKTPSHIKDEIIHKVTEFALTGLRTLVFAMRELDSDTYDSLLKKYKYAQCQLGIERARAMEEASAEIESNMSLIGVSAVEDKLQPGVKQCLQSLISAGIQIWVLTGDKEETAVQVSQSTGHFPPGTTLIRLTNGQSVEDVGRAIYVQQEGMKARLEVKKGWSRFKRFFRKRVTLDASGLDSDGFDSDTSTDSDDVEAEIQQTKGSFFSRFNRRFRSAVADGLRRHRRKNPGGANEPVGLVIDGTTLRYAISVSITLFQIFC | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 916
Sequence Mass (Da): 103194
Location Topology: Multi-pass membrane protein
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Q6DEA4 | MARAFLGAVACTLILAASAMYSPSDDVIELTPSNFNKEVIQSDSLWLVEFYAPWCGHCQRLTPDWKKAATALKGVVKVGAVNADQHQSLGGQYGVRGFPTIKVFGANKNKPDDYQGGRTADAIVDAALNSLRSFVKDRLGGRSGGSDSGRQSHSGGSGGSKKDVIELTDDTFDKNVLNSDDVWLVEFFAPWCGHCKSLEPEWAAAATEVKEKTNGKVKLAAVDATVSQVLASRYGIRGFPTIKIFQKGEEPVDYDGGRNRADIVARALDLFSENAPPPEINEILNGDIVKKTCDEHQLCIVAVLPHILDTGAAGRNSYLEVMLKMAEKYKKKMWGWLWTEAGAQMDLETSLGIGGFGYPAMAAINARKIKFALLKGSFSEQGINEFLRELSYGRGSTSPVGGGAIPKINTVEPWDGKDGELPAEDDIDLSDVELDDIGKDEL | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 442
Sequence Mass (Da): 47784
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A0A7R9GCG9 | MFPTPRLLTSASFLRRLFRFPFNTQPELDESKLNPCQRALLEERCLLVTERDAVTGSATKRDCHLWQNGSCPLHRAFSVFLFNGKGEMLVQQRAMTKITFPGFYSNTCCSHPLDTQEELQEKDFIGVRRAAVRRCEYELGIQLDPQDLTVVTRVLYKAPSTDVWGEHEIDYVLFARKDVKLLLNPNEVQDFKWIPRENFQEFLAKCASRGIPLTPWFQIVAAKFLQHWWQNLDNLKAVQDLENIHKVISVSGTEVEDLDVRLQILKNQEYRHWWQNLDNLKAVQDLENIHKVISVSGTEVEDMDVRLQILKNQEYPSLGKNENKIDNEKARTFFGILKPFNESLGLLEKHTLPFRRMSLSIPVQNNIFAQNIRLVQEQHDFMERLHETHVIVAIFLNLDEQREFCLRVVPRKVGKHWRIVLEVLESLLSNKFLLFVPFHTPHHGIPENRHNVLVFQVALAHRVLDVGSAPVDVNTQEINIWPLKIARCGCARALPAARMNTPPVAQRKYRQITFIPQKPSSNKPAASL | 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: 528
Sequence Mass (Da): 61227
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A0A6V8NF18 | MRIVNPSVTKELLKQYRVTLRKRLGQNLLVDPNILDKIIEVAQIREDDCILEIGPGLGALTQELVRRARRVVAVEYDRKLCQILKEIFASTQNLLVINADLLSLDLASLAQEHTLTKVVSNLPYNIASTAALRIMEECSNIAEMTVMVQKEVAERMAASPGSAAYGSYTLKLRYFAQVFPLFQVPRTVFLPPPGVDSTMVKIGRDTYWQKVYPVRDFLFRIIELGFGQRRKKLVNCLYSGSALRLSKEDVVQALNSAGIDISARAEELSLEKFVQLGQALWPLLHQSSTRFNNKSPD | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 297
Sequence Mass (Da): 33438
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A0A9D4J8M0 | MSLEWSPWFYTPCDVTCGTGSRSKLRSCSTTRDEDCSGNAYDTESCNLQECSSLGKIAPGDH | Function: In the vertebrate host, binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes and is required for sporozoite invasion of the host hepatocytes.
Subcellular Location: Cell membrane
Sequence Length: 62
Sequence Mass (Da): 6785
Location Topology: Lipid-anchor
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R7VCD1 | MAREEFKRIVPNVTFGSDPVKAKVAGGTLVTLHVRHRGDIMKENYQNMRYTFPGRSFFENSIQFFADADPNLHVVVCCVDIEWCRSNLTDLPATFYFSESKNAIVDLAIMSMGEHAIMTTGTFGWWGAWLANGETVYYSNWPRHGSQMVQIRYVRQDFFMPHWIVLWWRSKSDKNNCSLTSRDQETKPLRPDEANKEITPNKKQPPLHATEKPPKNTTKVYVTGNVYGFRRTGNRLFVFAAIMAVTWRYSMTSVLSPEFELQKYFNIDYRARPGVGISNWAGGRM | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 285
Sequence Mass (Da): 32906
Location Topology: Single-pass type II membrane protein
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O48949 | MNRWNLLALTLGLLLVAAPFTKHQFAHASDEYEDDEEDDAPAAPKDDDVDVTVVTVKNWDETVKKSKFALVEFYAPWCGHCKTLKPEYAKAATALKAAAPDALIAKVDATQEESLAQKFGVQGYPTLKWFVDGELASDYNGPRDADGIVGWVKKKTGPPAVTVEDADKLKSLEADAEVVVVGYFKALEGEIYDTFKSYAAKTEDVVFVQTTSADVAKAAGLDAVDTVSVVKNFAGEDRATAVLATDIDTDSLTAFVKSEKMPPTIEFNQKNSDKIFNSGINKQLILWTTADDLKADAEIMTVFREASKKFKGQLVFVTVNNEGDGADPVTNFFGLKGATSPVLLGFFMEKNKKFRMEGEFTADNVAKFAESVVDGTAQAVLKSEAIPEDPYEDGVYKIVGKTVESVVLDETKDVLLEVYAPWCGHCKKLEPIYKKLAKRFKKVDSVIIAKMDGTENEHPEIEVKGFPTILFYPAGSDRTPIVFEGGDRSLKSLTKFIKTNAKIPYELPKKGSDGDEGTSDDKDKPASDKDEL | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 532
Sequence Mass (Da): 58237
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A0A251UJP0 | MDEEKEKKVVFVWDMDETLILLKSLITGTYTKAFNGSKDVEKGIEIGKTWENQILRICDDYFFYEQIEGCNKPFVDSTREYDDGLDLTDYDFANDAFVGAAFDDDANKKKLAYRHRIIAHKYKKGLRSLFGEKMIKSWDNLYEVTDDFTDKWLSSAKACVAQCAGDSGAENINVIVTSGSLIPSLVKCLLFRLDDLISYDNVYSSWEVGKYQCFSLIKERFDGPNVQFCAIGDGWEECEAAENMQWPFVQIDPVPVSTSHRFPGLNLETLGHYIGVVYGGDSDDEDE | Cofactor: Binds 1 Mg(2+) ion per subunit.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 287
Sequence Mass (Da): 32646
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R7UND8 | MATIQDFYRDRDVFLTGASGFLGKQILEKLLRSCNVRHVYVLVRPKRGRSSEERKDILLKSEIFTPLKMTDQSFSTRVVLIAGDMTSPGMGLQEGDAELLRREVSVVLHAAASVNFTEKIRDAVTVNVLALKEMIKFCKSLPHLQAFVHISTAYVHCYDPFTPECIVKPKESPQVVLDLVKNETDQRLEELTPKLIHPWPNTYTYTKCLAEWMLQEEADDLPCCIFRPSIIGASAEEPYRGWVDNFNAATGILAGIGIGVCNPVYGDASNKADVVPVDLCANAVIA | 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: 286
Sequence Mass (Da): 31833
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A0A660WVH0 | MEKAGNGILEHVKDSHYYDIFGYHLKLPEIPPVKVLGITFDFSITRMVVLLWIAALIISLCFFFSFRKRKLIPSKLGILLEYVILYIRDNIAYPILGRKLGDKYFPLISTLFLFILVCNLLGLVPLLGSPTSNLSVTSGLAIIVFVIIVLEGIKQHGLLGYFKSFIPGGIPAWLIPVMLPLEVLGLFIRIIVLAVRLFANMVSGHINIVVLFFLIIFLKTYLISPFSFGIALFVSLLEILVAFIQAYIFTMLSAIFISMSVKSH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 29628
Location Topology: Multi-pass membrane protein
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A0A1U8PD78 | MATAASSSSFTMLHLASLISIFALTNARIPGVYTGGSWETAHATFYGGSDASGTMGGACGYGNLYSQGYGVNTAALSTALFNNGLSCGACYEIKCANDPRWCHPGSPSIFITATNFCPPNFALPSDNGGWCNPPRPHFDLAMPMFLKIAEYRAGIVPVSFRRVPCRKQGGIRFTINGFRYFNLVLITNVAGAGDIVKVSIKGTNTGWTSMSRNWGQNWQSNVVLVGQALSFRVKGSDKRTSTSWNVAPTNWQFGQTFTGKNFRY | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 264
Sequence Mass (Da): 28498
Location Topology: Peripheral membrane protein
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A0A8S2LHK9 | MLRIFRYRCIILRYIILWLFLMTMTKLTITFYDDLQQQSIDSTSLALPSDDSELNKNKKQDSFNLTMNESQYVNATAINRTVIEYYREYVQKTNQEQFMHNKHLFSLRTTRYILLVQVHTRVIYLKKFIEMLKDVQAINQTLLIFSHDFIDIDINLLVTNIDFVPVIGNYKGFQIDSTVLYNLL | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 184
Sequence Mass (Da): 21971
Location Topology: Single-pass type II membrane protein
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A0A1T3A290 | MKSSKFSLLAFLMSCLFAGWGLVYVGRIKWAIRVAALMYIGVVLMGVSGLAATPVGLYVFIAFIITLKLATAIASAVLARRYDGPPGLPRKRFHVLYVGVLIVITLLLFEVFRAPLLGFKNYFIPSGSMAPTLSVGDYIISDLRPGAPKVGDIVVYRWDGTEAVKRVAGIGGDTLAIVNGELIRNGENLGLFHAPAERVKKDYSLTLAPLRVEPGHVYLLGDNRDVSNDSRFMGQVADEDVVGKVTGIWFSGDLGRIGTTFP | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 262
Sequence Mass (Da): 28351
Location Topology: Multi-pass membrane protein
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A0A650D3A1 | NVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGPSVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISLYQIPLFVWALLITAILLLLSL | 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: Membrane
Sequence Length: 145
Sequence Mass (Da): 15524
Location Topology: Multi-pass membrane protein
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A0A251U3H4 | MGDNVLNTPPFYTTKDAETGSLSRRLFRSYDVMHVALRLVCLSASLASVVVMITAKEKSTMSLYGFDIPVYSKWSFSDSFDYLVGVSAAAGVHSLLQLLMTSRMLLRKSSIISSKKHAWLLFASDQVFAYAMMSCGSAASGVTNLNRTGIKHSSLPNFCKPLHSFCDRVAVSIAFAFFGCFLLAMSSVLDVVWLSAY | 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: 197
Sequence Mass (Da): 21589
Location Topology: Multi-pass membrane protein
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A0A496SUN3 | MRLVFMGTPDFAVPSLRKLLEDGHQIVGVVTRPDRPRGRGKHLVPSPVKKEAMTKGLRVLTVEDLKDLDFVRSLRQMSPELIVVVAFRILPPQVLTIPPRGVINLHASLLPKYRGAAPINWAIINGEKQTGLTTFFIDDRVDTGDIILQRAVPIGQEETAGELHDRLMSLGAELLSETVSLVESGDFPRRPQPREGASKAPKLKKEDARIDWSKPAEQIRNLIRGTNPRPGAFTHRKGSVLKIHRASALTAPQKGAPGEILRADPKDGIWIATGQGALFLSQLQPQDRRPMSSAEFVRGYGVRKGELWA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 309
Sequence Mass (Da): 34142
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A0A7Y5TRA6 | MTGVSPLIGPVLLLGAAGQLGQALAPRLARLGAVVPLTRADVDLERLDDVRALVRRVRPGLVVNAAAYTGVDDAEGHEARCRLVNEMVPAVLAEETARLRVPLVHFSTNYVFDGLQPMPYTEDAPPSPLSVYGATKADGERAVAAANPRHLIVRAAAVYGGSGRTFMRRILELAREREELRVVDDQYVSPTPAWVLAHATVAAIDHLLAEHPAAQGLLHLTTTGAASWHAFALRILELDPDRAAHRVRSVVAVDTAGYPTPARRPANGVLDTGKAERELGIRLPGWEEALRRTWAGEGACR | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 301
Sequence Mass (Da): 32352
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F5L506 | MTPTERAYTLTLTVQEGQEGRLAAFLREQHHFSRRLLNKLKREGTVQVNGQTAFFHTQLKTGDKVAVCFPVEKPNPELKPQPMVLDIIHEDQDVLVVNKPAGLTVHPTMTEQEGTLANGVIHHWQKRGTCASFHPVSRLDKHTSGLILIAKHSFVHQQLDVSRQHHGLTRRYYAWVHGVVEKDNGEIVAPIGLEEGSIIKRRVRADGQPARTRFRVIRRYADYTWLELTLDTGRTHQIRIHCQHMGHPLLGDDLYGGSRHLIQRQALHACALAFVHPRHKKVCSFSAPLPEDLKRLAAG | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 299
Sequence Mass (Da): 33923
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R7TRE3 | MRRTGKRNGSSAEQSSTKKESKETATKEIPSQFFHLFGFHLSDFSSWGSFQRLLHRPTDPSSLGVLRILYGLLMVMDIPQERGMSHADYKWGDEDECRFPLFDFLSPLPIAWMYVVYLIMWMGALGIMLGLMFRVSCLMFACSYWYVFLLDKTVWNNHSYLYGLCSLLLLFSDANRYWSLDGLWHRHKRNAHVPLWNYTLFRSQFFLVYFIAGLKKLDADWVTGYSMQKLSEHWVFDPFTWLLSNDLVDLWVVHRGGLAIDLFIGYILFFDKTRIIGIIFGGSFHLMNSQIFSIGMFPWMMLATMPIFCHVDWPRRLFSAFPQCLERVLPLSGQPQKNPHCLYSKEEVKPDDESSPTQSSPAESSRAVRSQPSFYHRMASIGCVLYLATQCFLPYSHFVTKGYNNWTNGLYGYSWDMMVHSWSTQHIRITYVDKDSGKEGYLNPDAWTRGGKRWCAHADMVKQYARCIEQRLKNFNITRTELYFDVWRSLNDRFQQRMFDPTVDILTADWHPFKATPWLKPLLTDLSDWRERLDEIEKKIYDKSNITDVTFIADFPGLTLENFIQGELNDTKLTVLKGQVTVDFPENEETAVTLSEGQVYQIPANMFHNVRTISDTPSCLMYVFRNTTEEALYSELSTYEQEVKDFEKKREQSLATDSDHPEAKNPEVAKLWHQVTEKKNQVEYNANLTAIERAEKFLMHKYRTFTRGFTMVRVALQSIIMRDSFESVFNRTLADHDLDFFESVSS | Function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.
Catalytic Activity: 2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol
EC: 4.1.1.90
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 746
Sequence Mass (Da): 87272
Location Topology: Multi-pass membrane protein
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R7UHU5 | MVGKPTPLQLFWCAQTFLAGSSTVYLLLKRSHWVKLALPSGDLSPGFFRFRKRLGMIKSEGSMPRRKYCGGTDTLNGYFNDLFTWATTPKQTNSDFAPTLLALFLFVGHLGRRLYESWGISVFSRRQLLGPIEFIRVYAFYIGAGLTIIAEAPPLTGVASCASLDGLGLRHLLILPIFYFSSRLHHDTHIALAKLRRNKAGHIVTTDHKMPKGGWFDVMSSPHYFAELLVYTSIGLILGTSNVTYWWMVTYVFTNQFYLAYNTHKYYEGKFENYPKERNMFIPYLL | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Catalytic Activity: di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol + H(+) + NADPH
EC: 1.3.1.94
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 286
Sequence Mass (Da): 32685
Location Topology: Multi-pass membrane protein
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A0A0H6DCH8 | MKKPLIVQKFGGTSVGSIERMQTVAEHIIKAKNDGNQVVVVVSAMAGETNRLVGLAQQVDSVPNARELDVLLSAGEQVSMALVAMTLHKMGYAARSLTGAQANIVTDNQHNDATIKHIDTRTITELLEQDFIVIVAGFQGINENGDITTLGRGGSDTSAVALAGALNADECQIFTDVDGIYTCDPRIVPSARKLDVIDFPSMEEMARKGAKVLHLPCVQYAWKHAVPLRVLSTFEVNQGSLIKGSAATHAVCGIALQRDMALIRVESESFPSIIKQCQMLGIEVCTTIDEPTHSAFVIKRDAYAKLQLVGADKIRGSEPVSLITKVGIQAGALVAHARQTLAQHGIDVRYVSASEQSSMLMLDPANVDRAANILHETYVTSEIPQEFGLKQTFLG | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 395
Sequence Mass (Da): 42470
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A0A2E4WXX9 | MNQDPNQLTFLEHLDELRSRLIRSLACVLVTGIGAFVFKEELFELYKRPLLPLLEKNPNLLVVLSPIEPFLVYIKISAVTGIFIGLPFLLRELWAFLVPALSRDEKRASLPFLLAGTLCFMGGVLFCYFLVLPAALTVLHGLLPPAVHASYSMALFFNFITAMLLAFGLAFDLPVLMVLLAKLGILHPAWLARYRQYVVVGLFVLAAMVTPPDPFTQVAMALPLWLLFEIGLVISRLVIVASPVPPPTVAAPKVEENHESH | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 261
Sequence Mass (Da): 28956
Location Topology: Multi-pass membrane protein
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R7UM91 | MTAATMTHSSDGKSEPLKSSCESSCSTRRFVLLGVGLVVSSLLLAWTRTSPAAKASTPAPPNRWGIPSNKNNEFMTILYWSNTPGEEKRELEWSRQRQPQAVSCQQNQIKCMFSSDQSLAPESDALLIHVSKTEHYPNTRPTKQKWIFYEGSSPPRKKGEYPAAFYHHDDHFNVISTYSPRQSQIPASMIPWAKCKQSSTLTEKPIDFSLDKSRKVAWLANRCETGSAREDYITELSKHIHVDIIGKCNSMHCPRINARYRSVCVRSDPYLCSLCNYLHKTKDVVNRTLNIEQYWNRESLCNDADAFYSF | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 310
Sequence Mass (Da): 35329
Location Topology: Single-pass type II membrane protein
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R7VLR0 | MGKVWLLVFGIFLLNSGFILCDDDPADAEEDELDLNEIAEENDVLILTDANFQNAIADNEIILVEFYAPWCGHCKSLAPEFEKAAGILKENDPKVTLAKVDATVEKDLASEYGVSGFPTLIFFKNGAKTAYDGPRSSDGIVSYMKERADPSWKPPPDLVLHLTKANFSEFVDTAELILVEFYAPWCGHCKQLAPVLEKAAQGLQAFDPVIPIYKVDCPKESDLAREYEIKSYPTLKVFRRGKVFDYTGTERTAHAIVSYMENERRPPSTEVTSLSAVKKFMKTDDVTVFAFFKANDAAFETYENAANELRSDYDLGHTFDREAMTFYKVNAPSIAVFTAENFHTKHEQKYHVMPITKDSSVEEIRAFIAEHSIPLVGEYKTSNRATRYRGKYPLLIMFYSVDWSHDGITATQLWRRKLADIAKDHRDMTFAIANEDDHAELLKGFGFEDSGEEINIGILNELANKMPQEESKFPMPTFDSFDSDEIREFISNYKAGKISRKYKSQPVPKKSKAAVKTVVGSTFEKIVGDKSKDVVIEFMFSGCSKCKEFAPKYTALAKQYAKLQKNLVFAKIDNTLNEFPEAFLVDSFPSFYMVPANGDLSSPAKFSKEEELTPEIS | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 617
Sequence Mass (Da): 69588
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R7UUS8 | MLKKNSSVEDQANAVEQQRNRGSKVVYGQPIQLRHQFTGKYIHFSKKEMAELATKTMRVELQAYNAKQAQFRIMPRYKVRSEGDVVCIGDQVVLESFKSHGQYISVSEDVFPEDSVYAFRHEINFSVVHSTFTVYRQACAYDAQKEYLTPNGCVRFFHKEIDAYICAEGQFNDSVMQDVHLRVRGIDYSIPKTVFPSTSAITYWQIEAKNSMFPGGFLQWETPVRFQHMITQLYLTVKKDGKYTLTLTDDRNDTGTVFKLYPVVKKNEPIPKGSYCRIKHVITGYWMQALQGVSFILRRKTDLHQHNAIPEEVPRETLVQGTSTAFSDIEWTTAVMKKVGLSEQMMFADAFTIQNVEPENLTNFSFMCGYIPLLQNLIQYALKELEAWMFIDGRPIKKRQKLVRNLLGIRSMVTLLQAKWECVPYRSTMIMVQIYCVLNAYLKGDSRKNELWLARHNVFFLHQISLKGPVGQRATIMLTELLDGNRKVIDRMSEKQVDYIIELLAENMDYRYLDLLGVLCVCQDVAIRRHQKYIAEAWLKSTKKPIYDTKVGQAIGEDSNVIYVSTNRKTWTSLNEFTNKVGGTSEEQLKFLHSQLNLMSKICQNRNEMAIQILTAELKYLTWDEAMLCLTNPELPDDLRAQYCKLIIVLFVDVPGNISTAEDVLMTMEYDNIVTNNMRSDSEKILDKVVDSGELNTHLEQLKRWIMEFLSENRFMVLRLVYLLVTYCCYDTKVALREVLEPLLGILDGGTSATEEEMELFHSSGRYQMSLENNAVIDAKYQAIDLVLNIRFNNRLEAFAGLFKEVHSMKDHDHPLSPIISGNFEESSISRYRDDVMDRLGEIVDNTAILQPGVLVDILSDISAYKYDNLVMKATHLLVRYYSAFENLLSRAITAKILVNDESLKNLKKVRNRIPLLSLVVNSAINPDNAQKICPLLDELIRNFVQVTLVALARHQC | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 957
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.
Sequence Mass (Da): 110135
Location Topology: Multi-pass membrane protein
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A0A674EJ90 | MSGKVCSNNSVMQARRTVEQLRVEASMERIKISTAAAQLVQYCQEHSRSDPLLTGISASSNPFKDKKTCVLL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequence Length: 72
Sequence Mass (Da): 7943
Location Topology: Lipid-anchor
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R7TYG3 | MSLSSSNFPTICIILVGCHLSGLNGESPFTTIASKAELYSLPALTFGYADLEPFFDEATLHAHYDGHHETYRKKMNSALSEWRESDPLDSFSTEPILEILKNLNKVPENFRNAIKNSGGGFVNHALYWACMSPNPTREIRQPTGALLQDIENEFGSFVKFSLKFTDRAVSLFGSGYVWLSRNPSSGALIITTTVNQDSPISDGLHPILVIDVWEHSYYLKHQFRRHVYVADWWKVVDWENVEELDKWWREVGSYARDEL | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 259
Sequence Mass (Da): 29539
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A0A6V8Q2L6 | MANNSSRTSSWAEYLVVIAIAVALAFFIRTFIAQPFLVDKESMHPTLLEGNYIIINKFIYYFSRPQKGDIVVFYSPQEQAHLIKRVIGSEGDKIEILQDGQVVLNGRLLEEPYASYASYGVDAESGAITLGPGEYFVMGDNRGNSLDSRWFGPIKESSIKGRAFVLLWPFSRFRFLQ | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 177
Sequence Mass (Da): 20002
Location Topology: Single-pass type II membrane protein
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A0A378YXB0 | MASTLNPNLLLAIPLAPLVGSVIAGLFGKQVGRAGAHTVTILGVLVAFVLSVMTFIDVMNGASFNATVYEWARIGDLKLEIGFLVDTLTVTMMCVVTSVSLMVHIYTIGYMAEDPGYQRFFSYISLFTFSMLMLVMSNNFLQLFFGWEAVGLVSYLLIGFWYTRPTAIYANMKAFLVNRVGDFGFLLGIGLLLAFTGTLNYGEVFAKANEVAALSFPGTDWRLITVACICLFIGAMGKSAQFPLHVWLPDSMEGPTPISALIHAATMVTAGIFMVSRMSPLFELSDTALSFITIIGAITALFMGFLGMIQNDIKRVVAYSTLSQLGYMTVALGVSAYPVAIFHLMTHAFFKALLFLGAGSVIIGMHHDQDMRNMGGLWKYMPITWITSLLGSLALIGTPFFSGFYSKDSIIEAVAASHLPGSGFAYFAVVASVFVTAFYSFRMYFLVFHGKERFGQAHAHHDHDAHHEEEEDSHDHHHGLAPGQKPHESPAVVTIPLILLAIPSVIIGAIAIAPMLFGDFFKQGVAFKDVIFIGENHPAMEELGQEFHGWVAMALHSFGTLPIALSALGILLAAFFYLKRPDIPEALKNRFSGIYNLLDNKYYMDKINEVVFAKGALKIGRGLWKAGDQGLIDGAVVNGSARLVGWFAGVIRFVQSGYIYHYAFAMIIGMLGLLTLFVTLNGK | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Membrane
Sequence Length: 683
Sequence Mass (Da): 74578
Location Topology: Multi-pass membrane protein
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A0A165RK72 | MKNSYSIKYYISFCFLILFLGSCSTSKSTSYSTKGNYKSNVTASYYHKKFNGKRTASGEKFHNSGMTAAHKSLPFNTKVKVTNTKNKKSVKVRINDRGPFTKGREIDLSRKAFMKIADHKGEGLLQVDIKVIK | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 133
Sequence Mass (Da): 15019
Location Topology: Lipid-anchor
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M1Q730 | MNLKDIWKQQLNFFNSKLYSYKTIKAIPSEWVEKTIILDPEVSRFSGRYSYDLSPYAREIIDNLHPSNPYKIISVMKGAQSGITQGVIVPGMAWIISEHPDNFLFTASDKEIAKLTITTRFDNIMQSSGLKHLIRPNTSRSKGQRSGDTDFSKEFAGGSAIIEGTNNAGKFRFFSVKTVFMDDFDNAPRADKKEGSIRKLVEGRQTSYGNLAKTFYVSTPTITQTSNVYEMYLQGDQRKWHWPCPECNEFVPSDWRIKKADGSFAGIVYELDSENRLIEESVFFKCPCCGHNISNNEKHDLNNKGKWIATAIPKDKYYRSYYMNSLIIPPGFINWVDLVKEWLEACPPNKKPNSDLLKVFNNVRLGLPFEEKGEAPKMMQLMENIRDYRVGIVPDRTSIEDGNGEIILITLAADLGGIMNNETEDVRIDWEIMAHAANGATYSINQGSLGTFKRSRTRTEEDKVKESDRIKYTYMHGMKHSVWPLLEKIIKEDLIGESGDLYDIKLSVIDTGHFTKHAYEFIKKTHDSENWVFGIKGIPEINYRRNTKDVALVKKSANIQNLYLLDVEQLKDNLAANMKLRRADDETQESGFMNFPVQEKNKYAMNTYFKHFQSEVRKEVIENGESTGWKWEKKNSSVENHFWDVRIYNNAARDMFIDLIKRTDPSQFKDLTWDLFVESLN | Function: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end the packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition, and a large terminase subunit possessing endonucleolytic, ATPase and helicase activities (DNA maturation and packaging). The endonuclease activity cleaves the viral DNA generating 5'overhangs. The helicase activity separates the cohesive ends generating the single-stranded 'sticky' ends of the mature genome. The DNA-terminase complex binds to the portal of the procapsid thereby activating the translocase activity of the terminase. The terminase packages the viral DNA into the procapsid until the next concatemer reaches the complex. The downstream site is then cut generating the mature right end of the genome, the heterotrimer undocks from the DNA-filled head and remains bound to the left end of concatemer's next genome.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Host cytoplasm
Sequence Length: 681
Domain: The N-terminus is involved in the formation of the heterotrimer with the small subunit. The N-terminus part contains the translocase activity involved in DNA packaging. At the N-terminus, there is a high affinity ATPase center that is probably needed for the packaging activity. The Walker A motif of the ATPase center is responsible for interacting with the ATP phosphate and the Q motif governs force generation and the interaction with DNA. The C-terminus contains the site specific endonuclease (cos-cleavage) and strand separation (helicase) activities required for genome maturation. A second ATPase catalytic site regulates the genome maturation. The C-terminus very end is involved in binding to the procapsid. Contains a basic leucine zipper (bZIP) that may be involved in the formation of the terminase.
Sequence Mass (Da): 78504
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A0A5C2P0F2 | MKRLPQELHGRVLVTGAGVSGLGITALLKSLDVDVVVVDSGPDSLEKIQVKTGAEVCLDVDIQLQDFSCVITSPGWSPDTPLLVQAKDLGIEVLGDVELAYRLDRAEVCGKPRQWLVVTGTNGKTTTTAMLEAMIKRAGFKAQAVGNIGVPVAEALNAPERIDVFVAELSSFQLHWSEQLVPDVGILLNLADDHIDWHGSFDSYAAAKAKVLQAPIAIAGVDNEHVAQILSTTKTQKLVEFTAAEPRAGQLGIRNKMIVDCAFADSLEIVSAEGIEPAGPAGVYDALAAAAAARAMGVCADTIAAALADFHVAGHRGQIVGNARGIVAIDNSKATNPHAAGTALASHESIVWVAGGQLKGSEIRDLVLEHSPRLKAVALLGVDAPIIAETVRELAPHAAIMVTENRKPREAMDEVVSWSVAHAAPGDAIILAPAAASLDMYSGMGQRGDMFAEAIARELHD | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 461
Sequence Mass (Da): 48361
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A0A8S1C1C9 | MDRGISRYCERRFKDKKCLKLHHLKPNLNKFIITFDGKTEIHVKVLTATSEIMVNAIELNLKSVEFTPEGGVATPATVTLCVEEETAILSFAAPIEPCLGKLFFSFSGELNENLKGFYRSKYTSCENSKHTSAAVTFLCPTSARRMFPCFDEPSIKATFSISVLSDAPTILSNMPVASEEVRGDERLLKFERTPVMSTYLVAVVVGEFDFVEDTTRDGVKVRVYTPVGKKEQGKFALQVATEVMPYYTDYFEVKYPLPKIDLIAIADFAAGAMENWGLVTYRELCLLVDPDNTTTDRKQKIALTVGHELAHQWFGNLVTMEWWTHLWLNEGYATFVESMCVNHMFPEYDIWTQFVTKSVVVGLQDDALKNSHAIEVPICHPSEIDEIFDEISYNKGASIIRMLHKFIGDEDFRKGMKLYLTKHEYANAETEDLWAALQHSSEKPVKEVMSTWTNKMGFPVITVSSKQIGNSRELTLSQKRFCASADMKDDPSMWMVPISLSTSADPTKASHNFVLSDPTQIVTIDNINDGDFVKVNPGTFGFYRTCYSIEMLDQLVPAITSKQLPPLDRLGILDDVFSMVQAGHMAPTEGLKLMSTYSECEDDYTVWKNMCSWITKLNSLFNYADECKKPFLAYARSVLRKISEKLGWDAIEKESHTDTLLRARIIESLVECEDEKTIKEAKTRYEAHRNGTKILPADLRLPVYRAVLTDADASIFQEMVEMYRSADLHEEQHRISFAMGYMKDPELLQKAIDFAMSDDVRKQDTVYVISFIAFSLEGINLAWAHLTKHWQTCLDKFGGTWLITKLVRKVTEKFATVEAADEADKFFAENPISGVKRNVRLGVETARLNAAWLNRDRATIAEWLSEELARIANRATN | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 877
Sequence Mass (Da): 99537
Location Topology: Lipid-anchor
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A0A1I8J2I7 | MDPTSESLRVRRLRCPTVPCLLCLCPALLLLEQQILLGALALLCCALQLTQARALILASTGLGSVKDLRWALQLYRRLPLNAFSRLWGRCHQLPLPLFARSPAYRLYSKLCNCNLDEADFNDLREFRNLSEFFRRSLKPEVRPICPAARIVSPADGTVLHFGRVASGHVEQVKGVTYTLQGFLGPDPLGDNGSSECSTSPMERKLQDSEYHDHLKQNPENELYHCVIYLSPGDYHRFHSSVDWTVHKRRHFPGHLLSVAPRIAGMIRGLFCINERAVYMGSWRHGFFSYTAVGATNVGSISVFKDEELRTNRGGAGFQDRIFPEGSFVAGKGELFGEFNLGSTVVLLFEAPKSYRFSLRTGQKILVGQSLGTE | 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 autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, 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 prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Lipid metabolism.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.
EC: 4.1.1.65
Subcellular Location: Mitochondrion inner membrane
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
Sequence Length: 373
Sequence Mass (Da): 41775
Location Topology: Peripheral membrane protein
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A0A150IMQ5 | MKELYDILFETKSIQIDTNNPFTFASGIKSPIYCDTRRLISYPKERKMILSGFLEKTSKLKIDCVIGVATGGVSWGAWLSDWLDVPFGYVRSSNKDYGKKQSIEGDIDVSKNILVIEDVVSTGGSIGRAINLLKQSSASSLNAFSIFSYQFSESLEMFQKLNVPFESLLTLEGLLEHSSDKIGDNKSEIQLWKKNHGSGEGND | 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: 203
Sequence Mass (Da): 22594
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A0A7R9BW88 | MFSGNVSYGKIFGIAVTAFVIIQQVSTSPTRYHRFKKGPTAPVNINPDEYSKEYWNKLAKNELDKSMKINAKLNVARAKNVIMFLGDGMSIPTTTAARILKGQLTKIDSTGEEASLVFEDFPHIALSKTYNVDFQVPDSAGTGTAYLTGVKANSGTVGVTAAVPRYDCNASNIEENQVDSFLQWAIDDGRNAGLVTTTRITHATPAAAYAHCANRDWECVGFEPWEGPETELPDHCKDIATQLVNGKTGKGLKVIFGGGRHAFDGTIKPTENDPKGSCVRNVKESLIEEWQELHKDEKAHYIEKKTELEKLDAKNVDRVLGEEASLVFEDFPHIALSKTYNVDFQVPDSAGTGTAYLTGVKANSGTVGVTAAVPRYDCNASNIEENQVDSFLQWAIDDGRNAGLVTTTRITHATPAAAYAHCANRDWECVGFEPWEGPETELPDHCKDIATQLVNGKTGKGLKVIFGGGRHAFDGTIKPTENDPKGSCVRNVKESLIEEWQELHKDEKAHYIEKKTELEKLDAKNVEGGRIDHAHHALQMNAAFLELLDMESAVSAAMEMTDPDETLIIVTADHSHTMSFGGWPQRGTPLHGMGGDDDDGIAYLKMAYANGPRPYLYNETQRPDPQGEAVEKPDYQPLVPVNLYSETHGADDVAIYAQGPMAHMFHGVHEQNYIAHVMGYASCTGQYRNNCRSSASGKMAISCAWLFVLSMIVFAIPGRNF | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 721
Sequence Mass (Da): 79031
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R7TTD3 | MMVNRRDDYSRRGRDRYDRRRRPSGDQFKGSLSEGLRNQDHSSSDEEITLDDDDDDEDEDAIIERRRKEREALLKKLGAETEDSMDVPSEAPGHSSPSSHSSSPRSEVADELEKSGFDFMESINTKRGTMQPDKDSKPFKNGLDMFADEIDTHQFNSPGTVQRGSSAFENPALTDNWDDAEGYYRVRVGEVLDKRYSVMGFTGQGVFSNVVRAQDTARGKQEAAIKIIRNNEMMHKTGLKELDYLKKLNDVDPDDKFHCLRLYRHFFHKNHLCLVFESLSMNLREVLKKYGRDVGLHIKAVRSYTQQLLLALKLMKKCNILHADIKPDNILVNDSKLMLKLCDFGSASHVSDNEITPYLVSRFYRAPEIIMGIGYDHGIDLWSTAVTIYELFTGKIMFPGKTNNDMLKLHMDLKGKMPNRLIRRAMFRDLHFDSNNNFLYHEVDKVTQREKVTVISSWGNPKDLLAELIGCQRLPDDQHRKVTQLKDLLERMLTLDPTKRINLNQALGHPFIQEKL | Function: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 516
Sequence Mass (Da): 59465
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R7V6P1 | MTSVAVHIRRGDFITRNLQRNGFAVASLGYLIRAMERFKKKDPNVFFVVASDDIKWARNHLTGIDVKFSVGLSAAEDFALLANCDHIIISSGSFGWWAAWLNGGMTIYYKGFPRKGSRLWSHTDIDQYYYPQWIGME | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 137
Sequence Mass (Da): 15672
Location Topology: Single-pass type II membrane protein
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A0A452DLS0 | MAFPGWWERFDIYRKVPKDLTQPTYTGAIISVCCCLFILFLFLSELTGFITTEIVNELYVDDPDKDSGGKIDVSLNISLPNLHCELVGLDIQDEMGRHEVGHIDNSMKIPLNNGVGCRFEGQFSINKVPGNFHVSTHSATAQPQNPDMTHVIHKLSFGDTLQVHNVHGAFNALGGADRLTSNPLASHDYILKIVPTVYEDKSGKQRYSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRQPLYRFITTICAIIGGTFTVAGILDSCIFTASEAWKKIQLGKMH | Function: Plays a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 292
Sequence Mass (Da): 32827
Location Topology: Multi-pass membrane protein
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A0A7R9BJM0 | MGGLGQESAGIVTSDGSEAELKLHKGHGLVSSIFSEDLLYKLQGNLGIGHTRYSTVGGHQDNSNVQPFVVHTQEGPVAVAHNGELVNAKSLRKLVYSKGVGLARNLGIGHTRYSTVGGHQDNSNVQPFVVHTQEGPVAVAHNGELVNAKSLRKLVYSKGVGLASLSDSELITQLICLQPESSENNWPDRIKTLMHMSPISYSLVIMHNDAIYAVRDPYGNRPLSIGRILKNGSVSRSSSFLFKMHENPDSAPATNGNATPLSPDTEETEAWVVASESCAFRAVGAEFVREVAPGEMVEVSKYGLKSTFPLGDATPNPSSLCIFEYVYFSRPDSWMEGQQIWGVRRRCGIQLAKESPCKVDLVSTVPESATPAAMGFAEACGIPFTEVFCKNRQVHIRIASPPIKFPCRMGIHIPTKSELIANNKEADKLAEEIGAASLKYLTVEGLVQAVSSHAKPQGATPTPFAVASKLKSISENGAIPKCLNGASNGSGENGNNKCCSTGLSRQDSGDPQTAGYCTACLTGKYPVALEW | Cofactor: Binds 1 [4Fe-4S] cluster 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.
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: 531
Sequence Mass (Da): 56766
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A0A7R9BX21 | MLSEASVVNEKPVGVAPVKPKFHQPKLEKNVAMDYIPDEAKRKLHDAATDDDGGPPEKAAKLSRKERKKLFAGQNKNRPRPTSFARDKKPCPSIKCVTVDDEWVDCRYTGCAFLHDVKKYMDMKPSDIDDRCHVFYERGFCPSGLACRYGQCHIRETDGKNLINKDLQGKYKTEKNGIPEHLINSLRKRKHDFSKCEEVLKLYQENKDSFVDSARDADVKRVPWKSKPLYLAPLTTVGNLPFRRICKEFGADITCGEMALAKSLLNGRPDEWVLTKRHPTEDFFGVQICGSTANVLTKCVQVLVENLELDFIDLNMGCPIDAIYAQGAGSGLMRRKNVVEQVVRTSKRIVGPSFPITLKMRTGLTSEKRIAHELISSAKEWGVDMITLHGRSRTQRYKNNADWDYIEECALKADPLPVFGNGDVLSFEDAPVKRFYGSEPSATSGMMIGRGALIKPWLFREIKEQRHWDISAQERLDIVKKYANYGLEHWGSDDQGVDRTRRFLLEWLSFLHRYIPVGLLEVLPQKINERPPPYFGRSDLETLLSSPLCSDWVCFFSGASEEKKSKMAKVHVSNVTVLDNPSPFVNPLQFQVTFDCIEDLPEDLEWKLIYVGSAESENYDQVLDTVYVGPVPEGRHMFVFQADAPDTGKIPAEDIVGVTVILLTCSYNGQEFVRVGYYVNNEYADAELKENPPAVICFDKLQRNILASDPRVTRFKINWGPSKDAERVGAESSSKDSTSASLKGGIVSCEVPLMEDDDDDEEDTPFLPRERMDRVIECSQMEEGQLTPGCKFVDESGQIKARFSKDDCISMEQ | Catalytic Activity: 5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA
EC: 1.3.1.-
Subcellular Location: Nucleus
Sequence Length: 813
Sequence Mass (Da): 91959
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A0A1S3TGC7 | MVKVEKEKEKEDSYNSVELHLGVDASHSAPPEINHVITEAQRRELHHQVFIFNHLAYKLPPPHHRVQFPSNMSEYSFLGFDQGSRMVPEPHRCRRTDGKKWRCSKSVVPGQKYCERHMHRGRNRSRKPVETSQVNSSLAPKPCSKSPTKSASETLFEISNPNLIMAMQPSDTPSSIPSRSLSIDNCSSMNRSFMVFSSTFAASPGSGLASASAPKAAATLGNVASVAPDDKSYLKMCKKDNQSKSCVSNKGNRSDGKGSIVGDSNNISTGISFSPTSVLQVFGNNPSHLIDKTNIESAPDRCRRTDGKKWQCKSAVLPGQKYCATHMHRGAKKRFANHEIAAAAAAKTTTTSSAVTIARLPNFQATADMQKEGSAIPSTNLSMSVPASAPFIQCNGKGSSNSDTDTTISDTLQECSYTSF | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 420
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 45661
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A0A809XV57 | MKVLPLLVVAMGVVAWEATAQDAQCVRERAAMVEAIRAYARSAAGVLGQQGLSEKVLEAMAQTKRHLFIPEQSCSIAYADRPIPIGLGQTISQPYIVALMTQLAEVAPDHVVLEVGTGSGYQAAILAQLARKVCSIEIIPQLAETAAKTLRDLAYDNVSVRLGDGYDGWPECGPFDAVVVTAALGEPPPPLIEQLKVGGRLVMPVGPGYGTQQLTVVEKIAPGKTTTRGVVFVRFVPFTRSQN | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.77
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 25892
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A0A8J1LF58 | MRLVFFFGFSVCIVLGSVFVYYQPDHDAAMPFGCISGRNEKTYNCFSDITDKYEIGQLLCAKEFCEICLAREIQTDRLFICKKFLKKDGRKVRRAAKNEILILKMVNHPNILQLIDTFETKKEFYIIQELATGGDVFDWILEQGYYSEKDASNVIRQVLEAVSYLHSLHIVHRNLKLENLVYYNQKNHSKVVLRDFYLSCFESAEITEPCGTPEYLAPEVVSRHRYGRPVDCWAVGVVMYILLSGNPPFYDENEEENSENHNRKIFRKILAGEYEFDSPYWDVISAPAKDLVSRLMEIDQEQRITAQDALSHTWISGNAASERNLKEGVCAQIEKNFAKAKWRKAIRVTTFMQRLRAPEGASGRLPVTPRSSMSVSHEVMVEASSSSHTPSPHSSCRDITDPNRRSDPCDSLEPQIEHPKQGAP | 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: Membrane
Sequence Length: 424
Sequence Mass (Da): 48586
Location Topology: Single-pass membrane protein
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A0A2E7ZT56 | MIEAIRDAVSMMTGRITQQSIDEVLQLTDMTHVVGQVVKLIGRAPSMKGLCPFHNENTPSFTINTDQKVYYCHGCRAGGNAVQFVMETQSLSFKEAIEYMAQLVGFELRYEQFSESDQRRYQQERSRRGRLLECNEAANAWFIKNFHNPRLGREAKIYANRGRELSLSTLESFEVGFAPDSFDALNRYLQNQGFDADLIVQAGLSRPGRNGGLIDRFRNRLMYPIRNRLGDLVGFGGRALSADDNAKYLNSPDTWIGEPNQSRALYKKGDVVFGLDHVKRNIRRQPKGQRRVMLVEGNLDVMMLHQEGFDHAVCASGTKVTVEQLREIAKVADVIELVFDGDGPGRAATQEVIPRCIETGLDGYAVLLPGEIIEGKRKGDDPDSYLRKAGKDAFEQTLKSADDIITVWVCLLLEDASFTSSGKTRLLQKVGQILPWIVDPIRRELVVDQVRQLLRARGIEVSNRLINSAQSKRSGSHSGHSPRAMTPQLVVPEKQLEVVVTALRFPQLLTELRDSKRHNLLRHAALREALLLLAEQASAQPRVTPMHVNLWLQELRDDDVRQLLLKELSRPSPIDGTFDDLTASRSAHRHVVLLLDQLELQLLRQLLKVTIKGDQPIAKQQQIERQIRVLEKKVANFTRGNRQRA | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 645
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 72875
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A0A8S2IRD2 | MRVSSVGKGLRQIPSPRSHFCEHISNDDEQSYTCRQRIYVTCPHCQRSLCLHHINEHQIIIRSLLDSLVNRVNEYRYELTVTLSIPSTSQTVVNNCLDELKDVIIPYVQRTCCQNDVKQEDVNRVQVFIDKMFTIIQHIHFYWENHKKEKRSRSTDKMWIIIFAAIVIFIFFVLLYLLRPVYRPECLLTLRDVHVVITGGSSGIGKELARQLLNEHQARVTILARNQQRLDECRQDLALGNNERLLCLSVDVGQSYADIEKAIQQACQYHGNRPVSILINNAGIFYARTFEETTTDDFEKMVRINYLGVVFCTKACLASMRQHGSGRIVLVSSQAGQIGVYGYTSYCSTKFALKGLAESLQMELVRDNIYVTVAYPPDTDTPGFAEEKKTMPIETRLINDTSGVVSAADVAKKIIISTQKGSFSCWFGINGFLLECLTSGAQPITSILELISQCLTIGLARIIIVGLLNTFYSVVTRKSLKNNKTK | Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 1.1.1.102
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Sequence Length: 486
Sequence Mass (Da): 55097
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Q6INU9 | MAFKELTSRAVLLYDEWIKDADPRVEDWPLMSSPILQTIIIGAYIYFVTSLGPKIMENRKPFALKEIMACYNLFMVLFSVYMCYEFLMSGWATGYSFRCDIVDYSRSPQALRMAWTCWLFYFSKFIELLDTVFFVLRKKNSQITFLHVYHHSIMPWTWWFGVKFAAGGLGTFHALVNCVVHVIMYSYYGLSALGPAYQKYLWWKKYMTSIQLTQFLMVTFHIGQFFFMENCPYQYPVFLYVIWSYGFVFLILFLNFWFHAYIKGQRLPKFIQNGDCKNNNQENAHCKNKNHKNGLLKSKNN | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate to the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
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: Endoplasmic reticulum membrane
Sequence Length: 301
Domain: The C-terminal di-lysine motif may confer endoplasmic reticulum localization.
Sequence Mass (Da): 35780
Location Topology: Multi-pass membrane protein
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A0A833E355 | MGIYVLHTSDTHLGYRQYGIVERENDVYDVFGEIIDIALREHVDLVVHSGDFFDSIRPPPQAILIAIRHLRRLREKGIPFITILGDHDTPKRRVLPPLVLLEELGYVRLVGVGEQRLAYTVKTRSGEVFVAGISNKRKTSSSVLKLMLKKLSNPPSSIPSILLLHQCIRGMCIDYELELGDIPIGYTYYALGHVHTYKEFEIGDGVAVYPGSPEVMRVDEFRAQSERYIVLTELGKGVAYRQKIRLQRVRPQYELVIDDIESMELKVKQFIADIVSRGRASKKPFVYVRVVGGEYNRSKILNVLERFLRRVVLDYRVYIEKKSDDIGITVEGIEHVAKPLDKLELLEKLLGDKSLAELADTLIAILSSGSESEALRESLKIVLERYDIDIEFTPTSIARASTKRSSTRGSLDLLLRQQSRMR | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
EC: 3.1.-.-
Sequence Length: 422
Sequence Mass (Da): 48022
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A0A251UKY7 | MLYIIGLGLGDEKDITLRGLEAVKKSQKIYIESYTSLLSFGISEDGISTLEKLYGKALIVADREMVEEKVDDMLLEAREFDVAFLVVGDPFGATTHSDLVVRAKKMDVEVKVIYNASVMNAVGVCGLQLYRYGETVSLPFFTETWRPDSFYEKIQKNRGLGLHTLCLLDIRVKEPSLESLCRGKKQYEPPSFMTIGVAIDQLLEVEQLRGESAYNEDTLCVGFARLGSENQMVVAGSMKQLRTVDFGPPLHCLTIVGKTHPVEEEMLDFYRS | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
EC: 2.1.1.314
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-homocysteine
Sequence Length: 272
Sequence Mass (Da): 30483
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A0A7R9BHF6 | MRNWILTHVLRLYFRMAGTHSRNTPSWTNTRLNDRNSPTPLISLPDDSEPPSIVLRSFWNNLKYEWNSKRSKFATGDEVHILGRKYRIPEDETVMRRDFASRIWLTYRRDMPCPLPHSNLRSDCGWGCMIRSGQMILAQTILTHLLGRDWRPGVMCEVHRSIISLFSDHFFLSPPTFGLHRLVSLGLRKGKQAGDWFGPTCIVHILKEAVETSVVPGLRIYVAQDCTVYLDDVDMLCRPRDRNDDTDVTEATEFLQESQCVLSARQASDFVMVTKSGPFEGIQAEELNEEPECDQNDPRRNDDWSTSLLLFVPLRLGTEKLNPVYLPALKAFLSHECCVGVIGGKPKHSLYFIGFQGENLISMDPHFVQPTVDTENPDFCTKSYHCEKPRRIPFTQMDPSCCIGFYCRHREDFQNLVRFTQDCLVAEGYPLFVMKPGQETGHSFVSSNETPPHLIPEERILMMARRFINEHGEIEELEAIQEDFVFI | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine
EC: 3.4.22.-
Subcellular Location: Cytoplasm
Sequence Length: 487
Sequence Mass (Da): 56124
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A0A2N7S184 | MPAANEERSQITTHILDTGTGRPASGVKAMLEAKSASGWQEIGSGSTDADGRIKNLGPVQVEAGHYRISFETGAYFGKQGTETFFPAVTIDFFVNDVAEHYHVPLLISPFAYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 118
Sequence Mass (Da): 12729
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A0A5C2NVC1 | MHIVIIGAGAVGGYFGALLHETGTDVTFVARNESLHALRNRGLRIHTPEGLRDVPVQSVSSLSEIESADIVLLATKTLSAPELPESLPRGAVLVTTQNSVEMPQIAIDTFGPAAVIPGVVRSFLIKRGPAEVEFAGGIRSFTFGSVDPATQETVNELQKALAKAGIEPIVHPAVMEDIWAKAMFVTCFGALGALVDKPLGEIRTLYRADLRNLMQEVEEAGRALGIDLPSDIVETTLASLDRQSAQATSSMQRDLLDDLPSELDAQVGGVVRMAELGGREARMHRLILDVLLHR | 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: 294
Sequence Mass (Da): 31512
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R7TC67 | MVGPALDIAFEEAERDYGIKFIKVISLYPDDCNSVFTTGAIADMYYTQNISVLIGPGCSGDIIVCGKLATYFNLPQVTGVGDLVLGKINYPTLTRLSYSLEKQSDFVTAMLNYFEWNHVAIVYDYHDALMAVQGEALTSALREDSEFARPYSISFDTTKNPDLRSFLLEVVPHARVIFFLSSGDDLRRFMLEAESLGMTHGDYAFVTIELFPSEAWGDFSWERGDADDDRAKSAYEALLFVTLTTPSGPKWHNFVDDVKNRSASDYNYTYTGDVNYFVGAFYDGVKYLTLALNQTLEDGEDPYDGLRVAQKRWNTTFQGIMGEVYVDEIGDRIADYSLLDMTDIQLGEYEIVAKYKGSTRVIDLEPGISIQWPRGRGPPPDVPRCGFSNENPDCQPKGELRNHVNHMTIVCLDNSTTIAITCSVRRKFENALLSDAWRVDWDDIVLNKNRAAGSSSRLSLTIISGVCHTWLVCLAALCCRCSVLTTSNQIFTTIGTYKGVVVAIRKFKVDRIDLNRNVLLELKLMRELEHTNLTRFIGACVVLGRNAILNEYCTKGSLQDILANEAIQLDWLFRYSLVNDIIRGMCFLHSSDIGVHGRLKSSNCVVDSRFVLKITDYGLPTFYNSPTYKEIGNAQYKRTLSTSSKADVYGFGVILHEVITREEPYSQYDLNPKDVIGRVVKTENPPFRPRTDRSLCVSALFAMMEACWNETPSHRPTFGDIREEFKKINKENKSGGGILDNLINRLEQYAENLEVLVEDRTQAFLDEKKKSEELLYRVLPKSVAEQLKQGRTVEPESYACVTIYFSDIVGFTALSAASTPFQVVNLLNDLYTTFDAIIDNFDVYKVETIGDAYMVVSGLPIKNGNQHAAQISRMSLALLNAIRSFKIGHLPSERLKLRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRLESTGEAMKIHVSPFTKDILDAHGTFLLNLRGETSMKGKGTLTTWWLEGELADEMDLLPHHTL | Catalytic Activity: GTP = 3',5'-cyclic GMP + diphosphate
EC: 4.6.1.2
Subcellular Location: Membrane
Sequence Length: 993
Sequence Mass (Da): 111364
Location Topology: Single-pass type I membrane protein
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A0A1U8NR16 | MGIAGYSYSWFLLSFFALIPTLRAHIAEYDEYWKARELEAIENLNKAYHPNPEEVVRHYNDHFSRTMLEYNSTRRALKGKKKGPCEITNPVDSCWRCDPNWVKNRKRLADCAPGFARGTTGGKDGKFYVVTDPSDDSANPKPGTLRHAVTQLRPLWITFKKSMIIKLEQELIVTSDKTIDARGANVHICYGAGITVQFARNIIIHGLHIHHIKPTTGGIIRDAENHLGLRTASDGDGISLFGATNIWLDHLSLYDSSDGLIDVIQGSTAITISNCHFTDHNEVLLFGASDTYAADEKMQITVALNRFGKGLVDRMPRCRLGFFHVVNNDYTHWFMYAIGGSSHPTIISQGNRYIASSIYVTKQATSRGYLSPEQWKNWNWVSQGDHFMNGAYFTTSGDPNASKLFDADKIMSFQPGRLVPRLTRYAGTLHCRIGRPC | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Length: 437
Sequence Mass (Da): 49155
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A0A5E6MUI0 | MYSMTTLTPRRTAILTFIRDRIAQQGQPPSLAEIAEAFGFASRSVARKHVLALTEAGFIEVNPNQARGIRLLNQPARPEWLDVPVLGRVAAGLPIGADAEVHSRLQLDPSTFAKTPDYLLRVQGDSMIEDGILDGDLVGVRRSAEALNGQIVVARLDGEVTIKRFERSGDSVRLLPRNPAYQPIVVGPDQDLAIEGVFCGLVRQG | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
EC: 3.4.21.88
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Length: 205
Sequence Mass (Da): 22305
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R7T9M8 | MESICVSAPGKLILHGEHAVVYGKVALAASLNLRSFLKLTFTSDDSIEVFLPDIDIHASWKIKELQSLFSSPHFNGDVQSPQEANSDCLQLIRHFLSLSEDTHDTKPLALVAFVYLLGHITQKLSGMKVELRSSLPTGAGLGSSAAFSTCLAAGLLVASGSIKDSRLGWEEKELDLINKWAFQGEKVIHGRPSGIDNSVSTFGGALCFQGGKITPLEKVPKLDMMLVNTKVPRSTKILVAGLRERYEKYPDIYRPVIDSVEAISVKCEETLSHLNDVPNDPAMIQTLRDLIGLNHHHLNFLGVGHKSLDEVCSICTEHGLSAKLTGAGGGGCAFCLITKDDSPRAIASVTESLQKCGYECWRTTVGGHGVKCHDPNEVISQLN | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
EC: 2.7.1.36
Subcellular Location: Cytoplasm
Sequence Length: 383
Sequence Mass (Da): 41457
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K3ZU90 | MAKPSVGVSEVGVSAAPAQSACPCPGTLFPYPPPRGAGIAAAVRRKCLQVELGAGTGLLGGAWGVESMRASSPTHAKAAAALAAGVDDERAAWMVRHPSALGKFEQIVAASEGKRIVMFLDYDGTLSPIVDDPDAAFMSETMRMAVRSVAKHFPTAIVSGRCRDKVFEFVKLAELYYAGSHGMDIKGPAKASSRHAKAKAKGVLFQPASEFLPMIEEVHERLAETTRCIPGAKVENNKFCVSVHFRCVDEKMWGEVSEAVKGVLREYPKLRLTLGRMVLEVRPTIKWDKGKALEFLLESLGFADCTNVLPVYIGDDRTDEDAFKVLRRRGQGVGILVSKHPKETSANYSLQEPAEVMEFLLRLVEWKRLSRSRARLMSLQ | 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: 380
Sequence Mass (Da): 41459
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A0A7R9BUL3 | MRFTFLVILRIILLAAFGDASEDEERLVRDLFRGYNKLIRPVENMTQRVEVSFGLAFVQLINVVWNDYQLRWDEADYGGIGVLRLPPDKVWKPDIVLFNNADGNYEVRYKSNVLIFPNGEILWVPPAIYQSSCKIDVTYFPFDEQTCLMKFGSWTFNGDQVSLKLYNDKPYVDLSDYWKSGTWDIIEVPAYLNVYNSSIPTETDITFSITIRRKTLFYTVNLILPTALISFLCVLVFYLPAEAGEKVTLGISILLSLVVFLLLVSKILPPTSLVLPLIAKYLLFTGPRTHKMPTWIRVVFLKYLPLMLFMRRPKKTRLRWMMEVPGGGGAPGYGAGSPVLGKAHSINFGNSKVDLMELSDIHHPNCKISESPAAPRVRSSLKPSFRQTEP | Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 390
Sequence Mass (Da): 44435
Location Topology: Multi-pass membrane protein
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H9A9I5 | MSHWYLMSLQYSGSLIMNMTLFVYELAMLMIILITSIIMYLMLTLFTNKFINRNLLHGNTIELIWTIIPILILFKLAIPSLKLLYMMDELLDPLTYTVKVIGHQWYWSYEYPEFNNFSFDSYMINNNEELNLFRLLDVDNRMVLPIFNPTRILITSSDVIHSWAIPSLGIKVDATPGRINQSNVVLLRYGLFFGQCSEICGANHSFMPIVIESTNSKFFHLWTHFMTK | Cofactor: Binds a copper A center.
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
Subcellular Location: Membrane
Sequence Length: 228
Sequence Mass (Da): 26732
Location Topology: Multi-pass membrane protein
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K3YMY6 | MSTAFSDFGPLTERRRVEKQRQQRRRVMVAAGGASVVLILIVMGGAAVAYNASVQDDDASSSSTSSPSSPSGGGSGSSLLSVSKSVKMMCAQTDYRDACEKSLSKAVNASASSPKDIVRAAVAVIGDAVGKAFDRSALATGDDPRVKAAVADCKEIYQNAKDDLARTLRGIDAGGLDEVTRRGYELRVWLSAVIAHMETCIDGFPEGGLKKNMTSAMESGKELTSNALAIIEKASSFLAALHMTGAASHRRLFSIREEEHVEKQPKVNYSGTFHGERDDSPAPASRRLFSFTEEEDMEKQPKVNYSGTFHGERGDSPAPESRRLLSIEEDAPPWVNGQERRLLKGNNFQGRLTPSVVVAKDGSGKFKTINDALKAMPTKYTGRYLIYVKEGVYEEYVTITKAMANVTMYGDGAMKTIITGSRNFADGLTTYKTATFNAQGDGFIAIALGFRNTAGAAKHQAVALLVQSDRSIFLNCRMDAYQDTLYAHSKAQFYRNCVISGTIDFVFGDAAAVFQNCILVLRRPMDNQQNIATAQGRADGRESTGFVFQYCRFTAESALRDASRPAIRSYLARPWREFSRTLIMESEIPAFIDKAGYLPWNGDFGLKTLWYAEYANRGPGADTAGRVNWPGYKKVIAEEEASKFTVQNFLHAEPWLKPAGAPVKYGFWA | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 669
Sequence Mass (Da): 73048
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A0A656AB32 | MQAAERAKKDLDLAQANASDQLKEAKRTATELIEQANKRKAQIIDEAREEAQAERQKILTQAEAEIEAERNRARDELRKQVATLAIAGAEKILERSIDKDTHKDILDNITAKL | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Membrane
Sequence Length: 113
Sequence Mass (Da): 12732
Location Topology: Single-pass membrane protein
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A0A1B6FNA2 | CQTEVESGGPAGRVDKPVQTDGSVEQVSRHDRAVQTGDLQEEEEVHPRPLEECVAIYKEKGSAGSLCDAEVRALVRASYIPTYQIEKAVGDPERGVGIRRQIVGQSGDFTDALTQLPYRNYDYSKVLGACCENVIGYVPMPVGVAGPLLLDGRLVHVPLATTEGCLVASTNRGTRALLQCGVSSRVVADGMTRGPVVRFPSMTRASEAMLWMQTPENFQTMKDSFDSTSRYARLTKLHVRIAGRLLFIRFVATTGDAMGMNMLSKGTEMSLKTVQQHFSDMEVLSLSGNFCSDKKPAAVNWIEGRGKSVVCEAVVPGHIVTSVLKTSVSALIDVNISKNMIGSAVAGSIGGFNAHAANIVTAIFIATGQDPAQVVSSSNCMTLMEPWGEGEDLYISCTMPSIEIGTVGGGTQLPAQAACLDMLGVKGPNETCPGENANMLARIVCGTVLAGELSLMSALAAGHLVRSHLRHNRSSTNTAPTTSNFHPSRPSCTSS | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
EC: 1.1.1.34
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 495
Sequence Mass (Da): 52625
Location Topology: Multi-pass membrane protein
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A0A150ILN2 | MISDRVKIAFIGAGAIGSLFGGLLSKGGEDVLLIGRQPHIDAISKNGLFISGVEEFNVKIDSSSNPFDAIGSDLMIITTKAYDTRDALKDIVPILERDTIVMSLQNGAGNIEEISKFVEKQNILGSVTSMGAFIESPGKIQYRGKGKTFIGPYSEKNNCAKEVVKIFKKAGITAEYTNDIESEIWSKVIINSAINPLASIFDGENGILLDKNLLEIVREVTIEGKMILDNDGITIPDDIFEKTLEVIKNTSKNINSTLLDLRKGNKTEIDYITGKIVETGERLGIPAPFNKALLNILKFKENKLIQKS | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Length: 308
Sequence Mass (Da): 33668
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A0A7R9GJK8 | MKAHLLSLRRVRLRSTLLAVWSLIATLTSFWGIFGSRDENASSSSTCLPCHGITRESSVNTSMRLKGFQKSDPLETEPSFSCYSSKSSHPRKNQGKLPTIYVITPTYERPAQLADLTRMAQTLAHVAELFWVLVQDSREREPLVHDFLRYTNINYTYITGS | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular Location: Golgi apparatus membrane
Sequence Length: 161
Sequence Mass (Da): 18286
Location Topology: Single-pass type II membrane protein
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A0A2E7ZV60 | MHRVVFMGSPEFAVPALRRLCELSVQVVGVVSQPDRPAGRGRKMTPPAVAVHARSLGLDLFQPHKVRDGQLRQWLLERNPDLAVVAAYGRVLPAAVLDAPRLGCVNLHASLLPRWRGASPIQRAIAARDEQTGVCLMSMDEGLDTGDVYARRHINIAHDDTASSLSARLSALSAELLGYCLEDLLQSRLQAHAQSSEGVTYAPLLSKSEGAVPWHQSAEMVHAHVRAMTPWPGAWSTLITSNERWKFFAEELRTDPRSGVAGQVLAIEPGRVLIAADSGSVWFTELQRPGKRKMAASDALRGGHVGVGECFQ | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 312
Sequence Mass (Da): 33936
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A0A2D5PY95 | MKPIETLKNELSEIADLKGAVNVLYWDMETYMPKGGTAARAKQVAMLEAIVHERFIGEDVSNPLGELVNLDSGEIINGLDEETSRLVNEIWRDYHRAVALPKEFVEELSHTSSMAHPNWVEAREKNDFNLFAPHLEKLIALKHREIGYLDTQDTPYDTLLDEFEPGFTTANINVLFGELKTALVPMIKKIQESGVNTKQEILHQYYDADKQWEFSEMILKDIGYDFHCGRQDKAVHPFTIEFHPTDVRVTTRINEHNLLDCLTGSIHEGGHALYEQGLDQKWYGTPFCQAISYGIHESQSRLWENLVGLSKPFWEYYFPKLQTAFPENLSAVALEDFYRAVNTIKPGFIRVDADEMTYNLHIMLRFEIEQLIINEGADVASLPELWNDKMEEYLGIRPETDTLGVLQDVHWSHGSFGYFPTYALGNLYNIIMFNKAKEKLPDLDNQIRSGNFLELRNWLKSNIHQLGRRQTAKEMIKSISGEDVTAKPFINYLKKKYSKIYSI | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
EC: 3.4.17.19
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Length: 503
Sequence Mass (Da): 57995
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A0A251TNH7 | MGTLNHLQMVGFNSHVELGSIEGKPIMEPQDEGHSGSVSTKRNMFPVKAVVEFWGKKYIWSTVITSIKIAFLSDKINLLIPFGPLAILVDYFTGHHGWVFFLSLLGIIPLAERLGWATEQLAFYTGPTVGGLLNATFGNATELIISMYAMKHGMLRVVQQSLLGSILSNMLLVLGCAFFCGGIVHPNKQQVFNKSNAVMSSGLLLMAVMGLLFPAVLHFTHTELHFGKSELALSRFSSCIMLVAYCGYIFFQLTSQRNNSYTPIMEETNPDDGGSDDEESPDISKYESVIWLSILTLVISVLSEYLVNTIEGASVAMNIPIAFISVILLPIVGNAAEHASAIIFAVKDKLDISLGVAIGSSTQISMFAIPFCVVVGWIMGRPLDLNFQLFETATLIMTVLVVAFMLQDGTSNYFKGLMLVFCYLIVGASFFVHVDPQSIQDKP | Function: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase.
Subcellular Location: Membrane
Sequence Length: 443
Sequence Mass (Da): 48480
Location Topology: Multi-pass membrane protein
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A0A482WQH4 | MRRFTTVLKYFRRGINTSRRVESDECHHRTGGVIGINLPFDIHNETRFTVLTTIFLITGLGLMPFVVHRQLKKQNSVSDDK | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 81
Sequence Mass (Da): 9417
Location Topology: Single-pass membrane protein
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A0A7C7CBA6 | MKQSLLITALLGILGTLPMTAQATPAEDVQTYRDFFMKRFPGVPLEEFANGVYSIDQVSRDSWEAIEEFPPYEPSIEDGEAMWNKAFANGKSYSSCFPDGPAIMGKYPHWDDGKGMVMTLPLAVNNCRTANGEKPLKYAKGSINKLLSYIGYESRGQVTNVGIPNAAALAAYEDGKQFYFARRGQLNMSCSHCHMQQSGRHLRTDVLSPALGHTTGFPVYRSKWGGQGTLHRRYKGCNKQVRAKPFKPQGEEYRNLEYFMTHMNNGIAINSPSARK | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the intermediary formation of conspicuous sulfur globules inside of the cells.
EC: 2.8.5.2
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Subcellular Location: Periplasm
Sequence Length: 276
Sequence Mass (Da): 30824
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A0A7R9BIG2 | MELLALLFTIVLVSGLSVSLVDPKHYLLRYKIPIHTQVDIDPARYLCHRCNLLRQREDVKHCHECGKCVDGFDHHCYALNHCIGARNYWIMMLLFNNGLLLTTALLIAAVAFIYGVLARSRIMIPQFAQSKTDLASDKLICFGSPCLALIPLIVVIVYVIPTVLVLFSFGALVGAHWSLVAENSTTWQHFKERKSTPEKGKSLIMRQEIES | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 211
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 23822
Location Topology: Multi-pass membrane protein
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A0A1I8HF76 | MYIILQYLGACLFIFITFFFVIIPMLPNAWQYRTKMSVYYMLLLIYGFITTVLALATPRQLSNYKYPMATLAFTRWLYGLRYRVNNLARLRQLQGSYVLVSNHQSSIDLMGVGLLWPYQCTIVAKKSLMFAGWFGLAAWLCGCVFVSRGRQSAQAEMRRLAARMARQDDTVRVWIFPEGTRVSGADLGDFKKGAFHLAVQAQVPVVPIVFSNYSSFYSKRSGLFQQGEVEATVLEPLPTAGLTEADVADLTKRVRDAMSAEYSRLSAASDCKAD | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 274
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 30926
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A0A496STV3 | MAVIPVEKLEESGANPYEIVIAAAKRAKMLGELKGEPETNESDEKEEKPAIQALKELAEGKIKCVYLAEKRK | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 72
Sequence Mass (Da): 7955
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A0A966AC01 | MARKSLRQRYPHQFLDGGIVVWKPRGPSSRRVVDIVQRRLSLRGLGHCGTLDPLASGIMVLTGGMGSKFQQWLTVHDKVYEATVWFGVGSESGDAEGPLSFSAESISLPTQSDIEAILPQFIGEQMQVPPTHSAVRVDGQRAYKKARAGDMTPLKARPVRIEKLRILEWDGARCRIEVSCGPGTYIRSLAHDLGEALGVPATLMALRRTSCGVHSTEDAFRVDRVTREHWWTLERLVSHLPAMAVSTDVALKMGQGQSVEVTEAEGSEVKVIEDAAGDEDAAGDEDAAGDRVIYSNGKVQGIAVLNDNLLKPRRWLSRGQRDEISS | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 326
Sequence Mass (Da): 35706
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A0A0C4DL69 | MMAHQPPLKAAILIVSTTAAQDPTQTDDGLEEKEVEILAQGVKEGENIREVGSDISKGTVILAAGEQISAVGGELGSLAAVGVGEVKVYRRPTVALLSTGDEVVEHDRPGDLRLGEVRDTNRLTLISAARQHGYEVVDLGIASDKQGALEEKLRLALSRADVVITTGGVSMGELDLLKPTIERSLGGTIHFGRVAMKPGKPTTFATVPVKDESLGVRTPRVVFSLPGNPASALVTFHLFVLPSLHRLSGVQPAGLPKVTVTLSHEFPLDKARPEYHRAIVTVDRDGCLVASSTGGQRSSKVGSLRGANGLVCLPKGSESLQKGAKAEALLMGPVRPEL | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin = adenylyl-molybdopterin + diphosphate
Sequence Length: 338
Sequence Mass (Da): 35553
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A0A8J8BQ00 | MKRVRYALAFLTRIPVKGGTLEETAEASYVFPLIGLCVGCASFAFSWCAHRVFPYTLAGVFTLGFLMVLTGLHHTDGLLDMGDALLVTGTREKKIDVMHDHFIGIGGFFLAFFVLLTTVFCIVEFMALNSLFVGLIGSEVSAKFSMNCIAFFGTPSHEGMGSRVIQATDRKLFLKSCLISGIVLSVFLEVGALLFVSTLVFAYLLAVGAERNLGGIGGDFIGAAHDTTRMMSMILLIVVMR | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 241
Sequence Mass (Da): 26118
Location Topology: Multi-pass membrane protein
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Heavily deduplicated version of Trembl (November 2023) with dense Natural Language protein descriptions.
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