ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A086QZX7 | MRAFEDLSSEACEGGEGEQASEELHAWVEASVAPLLNFCRQEAQRFSDAGETAVCLINAYASVQEPLRRFRVCRSYLRVLAELLDQQMVKLIEVESGKILAYLGLADRLEAVRRAVEREKRRLGVAGPDALPQVGDGKAPLQVGTEQSGDAGPDDEVLLHKEGLVKFFGEFYVALYGLSALNLDYVDRLMHWHLRSHARKAVLNAVLQAYSEIYNHVSHLRVATHTPGDVALLLDV | Function: Required for normal Golgi function.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 236
Sequence Mass (Da): 26170
Location Topology: Peripheral membrane protein
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T2MJA6 | MVKLYAIELFHKSTKVTPLKSAQDLQSFSYFQRSTVREFMDFTGKIIVERTANGVRASIKEQDYLCHVYVSNDGVSGVAIADKDYPQRVAFNMLNKIINEFMECVKPPYTQDNPSVINFNLCETYLQKYQNPTDADPMMKVQAELDETKIIMYNTIEQVLQRGEKLDDLVAKSEGLSTTSQAFYKTAKKTNACCSW | Function: Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transp... |
A0A651HZM0 | MNIFLIGFMGTGKTTIGRSLAVLLQKSFYDLDEEIEKEHGPIKSIFKEKGEQAFRELERGMLKDLAQVENAVVATGGGTPVFFDNMLLMKENGITLFIDTPIEIILERLNLNKPEDDRPLLEGQNEEDIRTLYKQRLKIYKMADIIWKSDCSETSVANIVAAYMRSCRD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A2U9BZE7 | MRSSCSPLGSLWFLLLLGAGCLLLLVLVVQFLRCGLWRRPQRSSPSVFDDSSVGSKQQVTKRHRKLLLKSSAPAGGEEQQQLRLAKTQESRRHLLNEICDKYQPGITGRPVFRRQVSRVYVEDRSRLLYCEVPKAGCSNWKRVLMVLGGSAASTRHIPHDAAHYANRLRRLESYDRVGIAERLRSYTKVLFVREPFERLVSAFRDKFESPNSYYHPVFGRPIISRYRANATRSALRTGAGVTFREFIQYLLDVRRPVGLDIHWEPVGQLCSPCLLRYSFIGKFERLEEEANMVLRSVGAPGNLTFPGFKDRNPLAERTSS... | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 359
Sequence Mass (Da): 41456
Location Topology: Single-pass type II membrane protein
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A0A8B6XSY9 | MRVILEKLTQWFKKTTINILGPEPSKINLTPTLKSKTMAKDKEILKPVKFSVYLPDIICGMKELDKSLFNIKINVPAIKCNEKSCGKFQKTFKNVLLNRPHFRSIIPSNLLNSNERFILLNPEVNNFELLNDDQQKVFINENGEFCQHELLLEYKDFSAEEIFSKIFSNFDIENVSSFETVGHIAHLNLREKLLDYKKVIGQVILDKNPNIETVVNKVDSIEETFRYFQMELLAGLDKMNTTVIEHGCTFQFDYSKVYWNSRLQTEHKRLVDQVKEGDIVFDVFAGVGPFSIPIAKKKCFVYCNDLNKNSYLALKHNITL... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
A0A8B6XFG6 | MTDEPLLKRKAIQVDIKSSLDFESFTVIKVLSNDAKSKKIHVHGRFKNSEDDTIVSFEKTPFSEDSIQNILTSETVTNEVFSNDIYSQHTAMPQPYHNTLTTQVIKPATLHHIKKYTYQKLKVVEETPDSYKKITLPYIMENSMRVEWVYNILDHKSETERIIYEDSDPENGFVLLPDIKWDGKQVENLYVCAIIRNRNIKSIRDLNEKHLPLLKNLLRKGLDEIVKKYGISSDEIRSYFHYYPSYYHLHVHYNHLQADVGGTSAEKAHLLSDVIDNIENISNDYYQKKTLTVLLREQDPLYSLLSEKV | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway.
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + ... |
A0A7S8C5N5 | MRMKTIAALGIVMAMAGTLAACGTTPGERALTGGALGAGTAAGITAAAGGNPVIGALAGAAGGAIIGAATTPSGQTSDHVRWCAERYRSYDPRTDTYMGYDGYRHRCNSPY | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 111
Sequence Mass (Da): 11113
Location Topology: Single-pass membrane protein
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A0A5N5PZ16 | MRTNWSLLLTLLSAGFLTAHVAAVRPLRCVMYLTGQHPITPEIDQIRHVTHVILAFMGSSIFNEPARSEWPLIGDYTNVNQIRALFSPETKIMVAIGGWGDTYGFSAAALSEQSRKNFANNVARMVFATGVDGVDVDWEYPGGNGEDYKTVPNKAKEWEIGAYPLLLAELRQALGSKKIISAAVPGLARDMIAFNSQTVPRIMRHVDFLNVMTYDLMNRRDTVTRHHTGIVNSLEAVDAYVSAGATPQMLNLGFAFYVKWFKTSHDGCSKKLSPLGCPTLLLEDPKTGADLGRAGGFSWHDAVPAELGESFGRALDDGTY... | Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
EC: 3.2.1.14
Subcellular Location: Secreted
Sequence Length: 395
Sequence Mass (Da): 43629
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A0A1F7CMM2 | IQDVLEGPETVEFIVIDTIDPAVLNMYKNLIDWRSALVVVVSKSGGTLETMSAFFLYWNELKNAMKERASERVIAITDPHGGALRSFCMERAIQMLPIPPAVGGRFCIFTPVGLLPMALLGGDTAQFLRGAKEMDTACQASVLEENPAAMLASMQYLLDVKRGYPLRIIMPYSARLEQLARWGQQLIAESLGKTETNNPFPIAAIGTQDQHSLLQQWMAGPRLAWHLFIREEEKTRLTVPDDVENSFSHLAGKTFGQLLDACYEGTSRALIGGKRPCITITMPRLDAYHLGQLFFLFMTEVVLLGKLYRIDPYGQPAVEV... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 336
Sequence Mass (Da): 37424
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A0A024TTG2 | MVWRCLWAAALFVLPVILTAQELQSPIKLSSDVPYVLNRDGALLSFAAASAQPLATSTATTTTLVTSWSTPPLYVSLDNGAATHAAIQCHFHRPSEHWLNGRQYPFELHIVLANPANHSHVTAVVAVLFDVDHVPHPFLAQLWPHLKYGHDPRHGSLHVDLSSLRLHAQSLFLRYVGSLTTAPFTEGIEWIIHHQVQSMSLAQWTEYTAVFPLPNARPLQPRYDRQVQLIGPRNYVMDRTVTK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 243
Sequence Mass (Da): 27240
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A0A3C2C5X6 | MIDRYTMPEMKAVWSTENKFRTWLEVEICACEAMVELELIPPGALRQIKEKAGFDVQRIEEIEAVVNHDVIAFLTCVGEYVGEAARYIHLGLTSYDVVDTALSVLMKKAGEQILVRLNELRQALIGQAGTHRYTLMMGRTHSVHAEPITFGLKMLLWLAETERNIGRMQKAIETISVGRLAGAVGTYATINPFVETHVCKRLGLRPARVSTQVLQRDRHAEYLTTVAIIGSSLDKFATEIRHLQRTEVLEVEEFFAAGQKGSSAMPHKRNPITSERISGLARLLRGNA | Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
EC: 4.3.2.2
Catalytic Activity: (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate
Sequence Length: 288
Sequence Mass (Da): 32258
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A0A3D1WL55 | MITREKSEKGMLKLHLTLSSEVWQKAVEAAYERTKGKYNVQGFRKGKAPRKVIEKNYGDTVFYDAAFEDAVSNEYAEFLEKNPDVEPADYPHVAINAMTADTLDVTLSVVLMPEVVLSTEATSVKKETPKVSAKEVDEQLARFAESQARFVETDAPAATGDFVEMDFEGSVDGKLFEGGAAKDYRLELGSHTFIEGFEDQLVGVKAGEQKIVKVTFPENYPASNLAGKAAEFKCDVKKVEKKEIPEVTDKLISFSTEVSTVEEYKNSIKEKMLEAKKAQAERKFENDLIEAAVAGAKLDLPKEMIEHECHHIVDDFKQRL... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A939V049 | MTELRGKPVADRLDKESIARMAESGVTPVLAILRVGQKPDDLAYERGIIRRFDNAGAKVTVREVPEDVSQEDLDKAFDELNEDPKINAILVMRPIPKTLSLDHIKNTIDPGKDVDLMNPAHMTGILEGRKDAYAPCTAAAVIEILDHYGIEISGKRAAVIGRSLVIGKPVGLLLMNRDATVTNCHRKTPDTEGICRNADIVVAAVGRAGMMTADYVREGQVVIDVGMNVDDCGNLVGDAVYEDVSKIVDAITPVPGGVGAVTTSILLKYTTENAIRMKS | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
A0A2G6G3L2 | MKSQADICQAVANSIEQNIKTAGLHLLVAVSGGVDSMVLLALLDRLAPQRDIKLTAVHLDHMYRADAAIADARLVEDYCQDLGIACHIYRRPIASIAAASGQGFEEIARDTRYRLFRALKLALKADYIVTAHHLDDLAESVLLHLLRGSGIDGLVGIRTCDGDLFRPLLTVSKTQILAFAAAASVPYNEDLSNDDTTFLRNKIRHQLIPQLTEQYNQSLVAQLAQLSDIVRHESDYLAADTRRLFDEIVDCGQAITINRAGYKGAHSARRRRLVRYLFETFAGSLKDLTYQHITMLDNWLIEGKINSQQSLLGLHFLIDR... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A927SAL5 | MSKHRKKKRIGNGNPFKPRRYTRETVMRDREYGMFWYAWLWQVLRPAVIFLCALLIVVGLISTVWDTIYFGYISAPDETDYLTPGFTISSGESITTIGKNLQEQGYIKSPSVFKYYIQFYGLTNKIQSGMYYLSRDMNLFEVVDAISSGNATNERTIRIIPGWSVQDIAKYLKDVGAIGSEAEFTSVCKQYEPFLGYSLALINADANENLNKRAYPLEGYLAPDTYRIYLSADAESIVKTLIRQTDVVFASLFTNEAVYDENGNLVKEAEKYGTEKVPLTESEIITLASVIQKEAGSIEDMKRVSAVFYNRLAAGMKLES... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 427
Sequence Mass (Da): 48161
Location Topology: Single-pass membrane protein
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A0A7C6TNI4 | MIEFIKPTIEIKEISKGEATFTVEPLVRGYGTTLGNALRRVLYATLPGAAIVGVKIKGVKHEFSTVPGVKEDVAEIILNLKEVAVKAHLDSFERATVTLSKDTQGVVKAKDIKVPSDIEIMNGDLVICNLSEGASIDMELTIASGEGYVPAQNNKKADMPIGYIPIDSSFSPVKFATYEVIDTRVAQTIDYDKLVLTVKTDATATPTEVVSLAAKILVDHLGLFIDIVDNMSSVDVLKPEEDEVEDTKEDIAIEQLDLSARPLNCLKRANINMVSQLLELTEEELDKIKNLGKKSAKEIIDKLSLMGYSLKKAD | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 314
Domain: The N-terminal domain is essential for RNAP assemb... |
A0A972AR81 | HGTYFEMLGNFSFGDYFKDDAISWAWEFLTEVVKLPKEKLFISVYSEDEEAYNIWQDKIGIDPDYLVKLGKEDNFWELGAGPCGPCSEIYYDRGEEAGCGLPACKPGCDCDRYVELWNLVFTQFESDGAGNYKNLSKRNIDTGMGLERLACVIQGVDNLFEVDTVQNIMKHVIRLAGVEYKKNDNVDTSLRVITDHIRSTTFLIGDGVLPSNEGRGYVLRRLLRRAARHGRLLGIKDPFLAEICETVIQENKDVYHNLVEKRDFILKVITNEEENFGRTIDTGLQVLEEIISAPGLRKILGGVAFKLSDTYGFPLELTKE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6... |
A0A7Y2DZ38 | MNILISAATDLELGKFANSDHRYSNINVTGIVCGVGMLESMFRLMEHLSSSENSYDLVINIGIAGSFRKDINLTEVVNVVSECLSELGVEDVHDFKSAFEIGLIDDDQKPFKNGILKIENVPTLNIVSKLKQCSAITVNTVHGNEDSIKKISARFDPDVESMEGASHFYLSIMKDIPCLQLRAISNYVEKRNKENWKIDAALNNLWKVTEEVLFEFDNKK | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 3.2.2.26
Catalytic Activity: futalosine + H2O = dehypoxanthine futalosine + hypoxanthi... |
A0A356F1R8 | MYMKKFWAEFKAFIAKGNVVDLAIAVIIGAAFNKIVSSLVNDIIMPLISCAVGGTDVSDWKWVIKPAEYGANGEVLVAESALKYGSFIQTIIDFLIIAFTLFVIFKIFTYSKNKLEKFGKQVVDETKKLAKEQKKHWKKKKGDEVEAIEVENILETNETSQETLKSNSPVETPETVEESTPSKEDVMIELLTEIRDNLNTNKSSKNSKQTKKM | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Location: Cell membrane
Sequence Length: 213
Sequence Mass (Da): 23980
Location Topology: Multi-pass membrane protein
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A0A8T4W4V0 | MRLAFRVAYDGSRFHGSARQPAIVTVEGAIIKRLIDMDAIESAEGARVQMASRTDAGVSAAGNVVAFDTDMAPGSVASGLAYGLEHVWPLRYAVVNEGFRPRHAVRKTYRYYLADEGYDRDAMRRAARFFEGRHDMSAFARLDGRTPVREVTKVAVTGDDIATVDVAGHSFLWQQVRRMVAALQQVGRGEVQPEALRDALQRPAGQDFGVAPAEHLLLLDVEYSREPAWTDAPGMACLASRLRWLRLTVQMHRDMAGHGIEINK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 264
Sequence Mass (Da): 29222
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A0A9E2BJT6 | MAEEGALTFEKALEELEAIVEKLEHGQISLEESLAAFERGMELVSFCQARLQQVEKRVEILVERAGSFAFDPFSDGDEERA | 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... |
A0A1V9ZXD0 | MRPSSLFLGLFSLCALLSAVSGEIINKSVKRQWDLTRPIARSQVDITFTDEEASIKTYQVAIPLYLDERLALLTVKGDKNVVLDVVKGVRDEAKHVQLYTVKLNSPVAKGDEGNLKVFAHYTRVMNPYPAEIAQNEDQLVLFIAQHLFMSPYPTTTQSTRVKLPSPRVEQYSEVPPVNLKGSILTYGPYENTEAYGSISYPKSLQVHFKNHAPFMTMTNLVKEIEVSLWGRVSTEEVVDLANTGAVLKGGFSRYDYMMVQATSASFRQLTAVLPKDAVNVYYRDQIGNITTSRMRQTPSRTELELNARFPLFGGWKTQYY... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
Catalytic Activity: L-threonine = 2-oxobutanoate + NH4(+)
EC: 4.3.1.19
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 995
Sequence Mass (Da): 110552
Location Topology: Single-pass type I membra... |
A0A7C6W6Z5 | MKNKTTKKTLIGGQAVMEGVMMRGVSSMALAVRDPEGNLLLKTERLKKTKGVIRKIPIVRGAVMFFQTLIMGVKTLLKSAEVFSEEEGESELSASAAFFAMFLGLALSIVLFMFLPSLISDGVNYLTYKWWGYKSNVLTSVIEGVTRIIIFLAYLIMVSFVKDIKRTFMYHGAEHKTINCYEKGYELTIDNVKKCSRLHDRCGTTFLFLVMIVSIILFTASNALFAYLAGLNSRLGFFSAWYGKLIIRLFLLPLVAGLSYELLKLLALMPNYWFIKILKAPGLALQFLTTKEPDNDMIEVAIKAFDAVDRMDKDPNVPSV... | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A099KHJ9 | MATLNLDLGTRSYPIYIDSGLLSKTDLLSSHIRAKRVCIVSNDLVAPLYLASLKSKLTAFDVDEVILPDGEAEKSLANFDVIMSHLLNNEHGRDTTLIALGGGVIGDITGFAAACYQRGIDFIQIPTTLLSQVDSSVGGKTAINHPLGKNMVGAFYQPKAVFIDIDSLSTLPVREFNAGMAEVIKYGILGDKDFFEWLEANVKGIKSSDKQLLAVMIEKCCKCKADIVASDETEAGVRALLNLGHTFGHAIEAEQGYGNWLHGEAVATGMILAAKLAVAMNLLEVSELRRIEKLITVFDLPVVAPKNMGFDEFIRHMRRD... | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)... |
A0A927NJ97 | MPILYGRLLIKSKILTKTNKGDFMEKFVQKTFPHGVHFHDNKELSKEQAIEVMPLASDVFISVSQHIGAPSTPIVKAGDQVVKGQLIADAVGGLGSKVYASVCGEVVGIVKKVGAAGGLADHIHIKTSEQQDEVVGLPALEVKDKASVLNRIFEAGIVGMGGAGFPTNVKLKPAKPVDTLIINGAECEPYITCDYRLMLEKAKEVIAGANYLAMACGIDKVVFGIEANKMDCAELFASLGADVVVLKKKYPQGAEKDLIVAVNGRRVPCGGLPMDVGVVVQNIATAYAAYEAVELGKPCYERLMTVSGRAINSTKNIIVA... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 454
Sequence Mass (Da): 48735
Location Topology: Peripheral membrane protein
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A0A3C0PAX9 | MKSFSDYIIIKSAIRHNLRQCKRVLNGTKICAVVKANGYGVGIKNVVKQIDDLVDYYAVACFVEAKKLRQITQKPILVLNFVHMSTFDYCIKNNISITVSNLKQQKIIEQFEKRFLNKKHKLKNILESQDNEKKLKIHFAINTGMNRIGFSSQNDFYKSLVILKKCKYLKLEGIYTHFYNAENLKDTTNQNRIFMQYLDILKTNINQRDLIVHAANSEAALNYKIFNYDMIRLGIVLYGGLEINYDPVQYGESKGYREYKTKFMFKPSISIKSKIIAINNVKKGECVGYCKNYIAKKNMVVATIPLGYADGIFRNFSKKG... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 397
Sequence Mass (Da): 45710
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A0A1H2QFX4 | MVAGPGPGALDYPRGTVFQDLGDEGEGLDLKRYLAILLYRKWLLIFAVLLALIAGLFYTVREPPVYRATATVQATPPSGNQFGFTDLSAVASARNFTGDQLELLRSSVLAERAAQTLSLDLAPETKTDDAKPTFFDELQQQLTQWWHARQGRVEPTALDEQRDRLLDDPLASNQAAVAARIRSSLVATPVRDTNLIQLSMEGSDPRAITAMLNAVAKAFVNFQTERRSDDATSTQTFYEQQIEWTRVQLEDAERQLTAYARSKDLVHVDNLLEYSQSEYGALRDRLGEAERNLFQAEAKMRAMNEIDAQGSSDFLGSEVI... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 764
Sequence Mass (Da): 84030
Location Topology: Multi-pass membrane protein
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A0A3C1BXB4 | GGVLSDRKSMSFPNKVMSGPYLSEQDQSDILFGIRHGVDFIAASFVSTKQDVLDIQALLDANGGSDIEIISKIENRSGVDNVKEICSACGGVMIARGDLGVEIPYVEVPAVQKKLTRMCRMLGKRVITATEMLESMIQNPRPTRAEISDVANAVYDGTSCVMLSGESAAGKYPVEAVKAMAEIAEYTEQHTDYKQRFRKTEFVGKSNLDCISHAVCSMAIDVGAKAIVVCSVSGKTARLVSRFRTPVDIIGMTTDRKIWRRLSMSWGVTPVMADQFPGMEVMFYYAKKEATRVLNLQPGDNLVLTGGPVNGQQGNTNTIR... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 324
Sequence Mass (Da): 35306
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A0A8B6EIQ3 | MAAPSATTKMSKVEKKLKKKQIKFRDMLEKNEGIQITETPTKIICVHNGGLDNSVSREEISTALDKNGSLIDVIMLPKKPYSIVCFKTTEDATKCCEEFNGLALPPDGKRKHSVILYLSYVNKVPSNILPCKDLPPGLIILENFVSEAEENQLISSLHWQNDNQMKHREVLHYGYEFRYDINDVDADDPLPQSIPTECNAILQKALQTGYVKHLPDQLTVNKYVQGQGIPPHVDTPPAFEDGIMSLSLLFQIVMEFSHPGGQQISVLLPRRSLLIMTGESRYLWTHGITPRKSDIITTAEGLDLVMRETRVSFTFRKIIH... | Catalytic Activity: 5-(carboxymethyl)uridine(34) in tRNA + S-adenosyl-L-methionine = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.229
Subcellular Location: Cytoplasm
Sequence Length: 660
Sequence Mass (Da): 74853
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A0A970IQ65 | MKLLNVYTVEETRKKIDTYFCKEYNLYDEIHVTDAFNRIVFEDINSPIELPEFSKSVVDGYAVKSKDTIGASESMPVFLDVLGYVEMGKGADAMVQNDATVYVPTGAIIPKGADSVVMIEYIEKLDENTIAVYSSVAPGQGIIQKGEDVGKGELIISKGKKIQAQNIALMCAVGIEKIKVYKKLRISIISTGDEIVDSFGKVEIGQVRDINTHLLSAMALDSGAEVGLEILVKDSFDEIKVATEKALQVSDIVLLSGGSSVGAKDMTINVIEALDNGEIFIHGVAVK | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 287
Sequence Mass (Da):... |
A0A970TFS8 | MYRNDSNYKTNACSKALWRRYHEGIIPVIPDIKLFSAREGNLMRGRNPVDYALLMESCGAPVISVVTEEEHFGGSLKLLEKISEKISVPVLRKDFIKTKQQVKDSKQAGADAVLLIVSMLDRRLLAELVEFTLANGIEPLVEVHNEEEFNMLEGLDLSFIGINNRNILKYEVDNGDVATTELLGRYKRKDAFLLSESSITDKADVMRAISAGANGVLVGTAILQAEDSVCKYKQLAYSYGSKTESIEELSSFNLLNKISCRFKRSVNDYK | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 270
Sequence Mass (Da): 30255
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A0A8K1J2J5 | MLVREALAWGILELEDFTSKQLEARILLASVLKTTQEDLLIRYNEPISQEEESAFYQYIKRRKVLEPIAYIVGKKEFYGRDFVVNKQVLIPRPETELIIDRVVLEYQENFAGKEVTILDLGTGSGAIAVTLAALIPQAKIVATDISDEALMLAAENAKFNGTIIQIQFIKSDWYSNLPEKKFDFIISNPPYISPDNKTYMAQETILYEPESALFANENGLINYKKIISGLNNFLKSENKIFLEIGFNQSEAVINILKGYLFTEIVISKDLSGHSRVIEFRRA | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A8K1J3I7 | MEQLIIANWKMNLTFKEASNLTRFISEHNNCHKLIIASPAPYIAYLAQNYQQLSFCAQDVSVKNAFGSYTGESSAKFFKSCGVNYSLIGHSERRTLFGETNGIVRKKAEVCIENQITPIICIGESEELRNSGSYKEFLLTQLEESLPKTDKRMIVAYEPVWAIGTQITPTIDQISEVAELIKTKYQSIVAKTMQLVYGGSVNSENCKDIINIKDISGILVGGASLNKDKLFKILNS | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A1W0ABV6 | MIAPTLVAIFFANAVHAHSWLECTNYDASSTSNQEYWSAAACTGYARCGSYQQSHGFGIDTGFDYRPLLHNKPCQCSKDSPNAYSASAPMATYVPGQKVCLAYPAKNHVAAPCTNQYIPDTGVRIFRTQHPASNLTGDDPALHSWPVEYKHLNGPHQNGVVDYKGFQHCPKFCEDKGRALCSMCFNLEKDIAPGVYTFQWEWDFNSANDVYTSCWEARQFTMLTTHRRKSVIVQQMADIIQSQAMPEADNEHWWDARVKIIQEWLRANPLRIGVPEDGTIETIMQQISRGDKYVHVRVKAWNHIVTELQGIPGVCEKFAT... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
EC: 2.7.4.14
Catalytic Activity: ATP + CMP = ADP ... |
A0A947YZX6 | MTEYKTVHIECRSDYFDEIAGYAVTIGAIGSQVTDSTTLGASEGVCTWVAEGELEQFLFELDLWLKNLIPEHAYNVKVTDYVPEDWSTKWRENYYDVSAGRFRVMSSFSPPVVSSDEIQILIDPSMAFGTGHHETTQLCLEEIDMLKQEGGSYNAVLDMGCGSGILAIGSAKLWPDAKVTGIDNDPDVIPVALENSQINGVSVWASTDLPTDSKFDLILANINPAVLVGLRETLMNALIPGGIIILSGIIEEQAEFVKNAWGIEPILKREKNEWVLFRYQKQ | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 282
Sequence Mass (Da): 31229
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A0A927NBP9 | MKRKFKVTGMTCSACSAHVQKATEKVDGVQEAQVNLLDGSMVVECNENVTDNQIITAVTKAGYGASGYGEKTEYAQIEPEIKSEFVYSLKILIFSAVFTLMLMYVSMGEMLNIPVPDFIRGHHNSVTKALLQLVLALPVVYANRQYFINGFKKLFRLAPNMESLIAVGSLASIVYGLYVTFALSYALANGDVATLKALHMQLYFESSATILTLVRLGKTLEAKSKERTTDAIKSLVALAPDTAIKLVDGQEVSVNVKDIKLGDILVCKSGEIFAVDGTVINGECSVNQANITGESIPVYKKVGDGVISSTTNLNGVVRYK... | Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
EC: 7.2.2.8
Subcellular Location: Cell membrane
Sequence Length: 838
Sequence Mass (Da): 89589
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A0A927NVZ7 | MTKKTEKEKSTKGSRWWGLLVFGLLVFIDQLTKLFAEVYFLAGNEPITIIPEWISLRLAYNDGIAYGIGSDASAAVKIAVIAATAVMMALLAVAYCKMDKRRAFLRVAFIFVIAGGVGNLIDRVYFRVWETAEAGSFLIGVRDMVDISRFGFGVCNFADFFISAGAVMIVFALLFFDRDAIFPLGKKYKALAKEAEEKEEAKKAEKQAKKQAKNG | 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-, ... |
A0A316A414 | MITQIGFQKLSHQQNVDKDLVAQRFKSSTETYRNSAIVQEQMASHLSELLKDFSNKEFNRVLEVGCGTGFLTQKLPHEKMERFWANDLVAEVGKTVSEIRKDCTFLAGDIEKIAIPDQLDLIVSGATFQWVTAPRTFFCKLRDHLDVNGLLCFSTFGTRNFYEIRQLTNQGLNYIEKQDYSHLLYNFQILHLQEKTYTLYFESVKDLLRHIKDTGVNGVHQSPWSIREYRNFEKAYEEHFRSEKGLSLTYDALFIIAKKLN | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malony... |
I0AMP5 | MSNNRKIKVLVIDDSAFMRKTLSFMLESAGDIEVVATAKNGLEGFELIKTHQPDVVTLDFEMPGLNGLETLDKIMKDFPVPVLMVSSFTTEGADVTIKALSLGAVDFLPKEPSAVASGVMKIKNELIDKIRNIYKQTSIATRLKRISDITIGEKKTPKQKTQVRDWAPAFEIKAILIGISTGGPLSLQKVIPHLHAQLPVPIVIVQHMPPMFTLSLAERLNKLSELTVKEAADNDLLESSKVYFAPGGKHLFVYQNSGHLSIKVSENPDNTLYRPCVDVTLNSMIDVFGKTVLPIIMTGMGKDGMEAVKRLKQIGGYAIA... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
A0A2V2G756 | MKTQRQNKILEIIENNDVETQEQLAELLCKEGFVATQATVSRDIKELRLVKISSVGKDGKQGRSKYSQNSVKNEIDTRFTEKFKSILSEMVLRISYAGHMVVLKTYPGMAQAACAAIDSLDISDIIGSLAGDDTIFIVMSTENDAMDFVKKLSKSISR | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 158
Sequence Mass (Da): 17570
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A0A316RRY3 | MTNSEYVLSKEEISGLDRRTIESGIPSRTLMRNAAYAVYRRILALGADMSRTVIVCGGGNNGGDGYALALLMEKSGIPVSVLESSAPKSDDCVYYSSLLRAARADISALASATLIVDAMYGFSFRGSLLGRDAEIAAAVNSSEAFVLAVDLPSGVSADGDFCEGCVCADATCTFTAEKYATASYPSKAKCGRVFVEDIGVPSSMLEKLSPGALLVRSADGMIKPRSDTGHKGSFGTLAVLAGCADMPGAAALCAAGALCSGVGLVKIASEEKVLDILKIKLDEPVYLRASVDAITESGASALLVGCGIGRGYDGMLADLL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A316RAC4 | MNLPNKITVFRFACIPFLLAASLIQFPYHWSVALVIYFIACMSDKADGIIARKQGLVTDFGKLMDPLSDKSLVLAAYLVFVNMGWHTELVIMLMMAREFLVAGIRMAAAAEGEVIAANQFGKAKTFLQMSTTGLTYLLLAIGEGAADITTSTPWLNVYCTIAFWVVAVVTVLSGIVYAKDGWHLIRTK | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
A0A9E6ACH9 | MRPKLALAPTAQQTPAEFETRPMRLSEESVMDVGDAWAVIWRGRLRILACMMIMAAAAWTYIQKIATPTYQATATVVLETRSTQVIDMEGVISGLSGESVDIATQVQVLRARSLHARVVDELGLLAHPDFAKPPRFSELFSYVKAVVPIRVFSDIGDPSGPTHRDEAIDAVSDMISIRNIPNSLVFEITVEHASPTLSAQIADAMAAQYISDQLSVKSEATAQATNWLSERVVALETELEEAETNLKTFTTETDLISAEDLLEMQRQAKEQRLRITHAEEEITRLQGLEGQGNSEERRRNQEALSRTERLLANLNDARVD... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 675
Sequence Mass (Da): 74735
Location Topology: Multi-pass membrane protein
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A0A965YHP9 | MIIGVTGGIGSGKTYFCHLIEIAGFPIFYTDMESKKLLNSDPLIKAQIIDLFGASAYTEDVLDSKHIAQQVFSDDNLRTKLNNIVHPAIKKLFDLWLTEHKSSPIVLLESAILFESGFDNFMDKIIVITAPLETRIKRVIKRDNCEEKDVLSKIKSQMSDEIKINKANFVIQNGEHDDLNKQIFDLLGKIMFQK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A951S681 | MFKKRNSIVFFIIYCLLSCYTYAQSIDSLRAVWNNGTELQKLKSSVHLTKVLSIKKFSETIQITEQAIPIAINQKDTSSWASLLCSKGIAHYFSGEYDQAAACYFDAVALLENNVKSNQLAEVYELIARLYRKTNELTLALDYYQRAMLIYSKKNDKRGMATIYNESGVVYEYQKSYDIAIYNYKQSLSLTEQLNDEAASAYALSNLGTVYRLINQFSLGEQYLKHALSIRHQLQDTFAIALNLSDLGLIYQAWGKFEKSIEAFDESNTIAHQLNYKDLLSANYKNLALVYASIQKYDKAFQYQNLHKAISDSIFTEQRA... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A356ML10 | MIRSDDVNYLLTICYDGSNYKGWQVQPNMITVQGELEKALKQVFKTDIKTIASGRTDTGVSALGQTVNFYSDVVYKEYPLLTYLNTILPSDIRVMKVQYVPDDFNARFSSKRKTYAYNFYLSKLPNPYYDKFATRVWYQLDMELLEKELQSLIGVHDFTTLSSVDTQADSKVREIFDIKLVQSGDVYTVYFTGNGFLKNMIRIIMGTAFDIARGKIKANMLELLDKKDRRLGGKTASPIGLVLVEVNYV | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 249
Sequence Mass (Da): 28487
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A0A6A6P348 | MAAALRAALFKLTVWDHDASYGAALQGLRYVDARAPRGVEERKRPGGWQKGVYGLVSVGGRYAWSKWEDWLLDQESGYGEVGLVLCCCCSLTPSSAQLFIFLHNTRLLTLSVSARSRSLPSSAAPPASRTSPAPPTPSPPSPPSASSSSTAATGRCSTALSASA | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 164
Sequence Mass (Da): 17227
Location Topology: Multi-pass membrane protein
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A0A2V2ENW4 | MKMKLGFIGAGMMASALAHGVCKNNLLNGADIMMYDVNADKLTKLQAEVGIVPAKSAEEVFQNCASVIIAVKPQHLATVGYSAGENKPLIISIMAGVTIQALEEKFAASPIVRVMPNNPAQIGEAMSAYCINEAVTAQDKKWVEEILAAVGETAFVNETQMDAVCGLSGSAPAFMYAVIEALADGGVMMGLSRDIAYKLAAQTMKGSAEMALKTGKHPGELKDMVTSPGGTTIKGLYALEKMGLRAALMSAVEEATLQSKKLGEMK | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A354MXG1 | MNNETPVSDSSSLSRTEITLAVFLGCFNMLLLAVLTALSDVPLYFSAPAAVALYLCEIALLGFRKKIYARVAPDEGIAKLLEERGITVLKNTQYPVFIFNAGEKILWYNDAARNILPPDENFISREISEVISPSGENTEGENAATVTLGGRIYHAESFRVGDDLPLLILMLSDATLLSEAEKKYEDERIAVAYIAIDNVEDILQYVHEKFKDAVAAVDDRLKKWAQDLHGVIKSYENDKYIMFFESKYLDALIENRFDILDEIRDTRLGDGVSITVSIGVSRIRGTLADREAAAREAIDLALQRGGDQAVYKSEEGITYY... | Cofactor: For phosphodiesterase activity, probably binds 2 Mn(2+) per subunit.
Function: Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP).
EC: 3.1.4.-
Catalytic Activity: 3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H(+)
Subcellular Location: Cell membrane
Sequence Length: 663... |
A0A356M7D3 | MNLPNRLTLARILLIPLILLFMLPLPDIFAFASWNRFIIEYGQLVAFVLFAIASLTDLIDGRIARKLNLVTNLGKFLDPIADKMLVISVLSVLVQLHRLSALVVIVVIIREFTVTGVRLAASDKGVVIAASRLGKAKTVSQIIAVLIILGERTLIMLTGSFLAGSWIIGAGDAAMLISVILTLVSGIDYVRKNLSYLKE | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
E0WU05 | MALLFKSINFITLCRGHNVIRTRKNSLAKLVVQKKDYCYYSLPKMASFLGDIDRLPKSMKVLLENLLRHIDGKSVKENDLQAMVDWLSTGHSDREIAYRPVRVLMQDFTGVPAIVDLAAMREAVKRLVGEVKRVNPLSAVDLVIDHSVTVDNFGDENAFGENVRMEMARNCERYAFLRWGQQAFNRFRVVPPGTGICHQVNLEYLGKTVWHEQQGDQCFVYPDTLVGTDSHTTMINGLGVGGIEAEAAMLGQPISMLIPDVVGFKLTGKLNEGITATDLVLRVTEMLRKQGVVGKFVEFYGDGLADLPLADRATIANMSP... | Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
EC: 4.2.1.3
Catalytic Activity: citrate = D-threo-isocitrate
Sequence Length: 677
Sequence Mass (Da): 74375
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A0A1V5CUZ9 | MDEEIRRFIEEDLGSGDVTTNSTVPEDHLSLAEIFAKEDGILAGQPFAKKAFHVLDEGIRYEEIKEDGAPVKRGDLVARIQGRTRAILSGERVALNLLQRLSGIATVTKKFVDATGNTGVKILDTRKTSPGLRVMEKYAVRMGGGHNHRLNLSEMALIKENHIAVAGSLKEAVKRVRTASNVFIEVEVKNMNELRDAIEEGVDRIMLDNWAVEDIAQAVSFVQKRIPIEVSGNMTLERTQRISPMGIDFISVGAITHSFKSLDLSLLIKGGDT | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 273
Sequence Mass (Da): 30076
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C1A5M4 | MIGTGAVRGAATAALLADLGFGEPPDQLHPTVWMGRWLGRIRASQKSRSMMPGHSSRQAFWHGAAGLAGGVALTTAIAGAVAAIIAQLGNASTAGASTLPSTLGRISVEGVLLKPALAVRSLLRAADVVRVALERHDLDQARHLLSWHLVSRNTDALSADEVAGAAIASLAENLSDSVVGPLMAYRLGGLPAAYAYRFVNTADAMLGYRTPELEWFGKSAARSDDVLNLLPARVSAPLLALAAPCAMASPWKALRCGIRDASRTPSPNGGWPMATMAGALGIRLEKRGLYVLNAEGRAPTAHDITRARRMVFAASLAAVM... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 330
Sequence Mass (Da): 34367
Location Topology: Multi-pass membrane protein
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A0A2P1VPK4 | MASARRFGVSELLSLLLPVSTEQPIRWQCVALEPTSGALAQTPSQQGQFGHAELESVAALVTPNTTVQLLIPGEWVSLWSVTLPKGAQRQADKVLPALLEEELTQDIELLHCSLLQLQGDKASVAVIEHRRMQQIVDWLAQANITSARVLPDWAALPENSLLIAADRVQCHQQGWHGFSAEMALASVLLQADSNHDEMARGESRAPEWQVFSAQPLTDYPALLTALTGDELARDAHTLMVKDINTLALTTSSVAIARNATLLTGRWRLRTDVRRQWRRWRPLAFTAALLLSLLTVERAVALWSVAQQSAQARQAAEQQFR... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 443
Sequence Mass (Da): 48693
Location Topology: Single-pass membrane protei... |
A0A1J4VKC5 | MGQALVKGLVEKSVYPQNLSIFDLDKKKTEAVKKETHVKLSKSARQCASLSDVIILAVKPKDIQGVAEDISSVLTQSSLVISIAAGVPIAKIEAYFGKPVSVVRVMPNMPALVGVGMSAISLGKHATEKHRRIAEAIFNAIGEVLVIQEKFLDLVTAVSGSGPAYFFLLAEKLIEAAYEMGMKAETAKRLVYQTALGSGKVLVESGEDPEDLIERVASKGGTTESALKVFQKQGIGKIIQDAVKAAYQRSKEISKGE | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A101D342 | MQVLNMLTAAQLASETPNPPAFVHITTKAMAAEAALESLASVIPSTTPLVLWQNGFLAQPRISQAWPGPVLCATTTEGAYLTGDDGVVHAGRGHTFIGDLSNQHGELAETLAQTLTQAELPATAVSDIRQRLWQKLAVNAAINPLVALNGVRNGELRTAAHSPHVQSVVKEVAAIMLAEGIQPPNGGQGEQAWLALVWQVIASTANNKASMLQDVEAKRPTERGAILGPLIESAQRHKLPYGVLQALDTAIAALEAGY | 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: 258
Sequen... |
A0A0T6A5A8 | MTSQELLVLGRVLGPWGLRGAVKVQSHAESRSVLSPGNVVILRGPRGSSEALLTAIRPLRHLLVATFQGIDSRKAAEAVRGFEICISRTAAPALPEATYYHHDILGLTVQTEAGEGLGEIVDIWPSAAHDLYVVRRDAGEWLLPAVRAFILRVDLARRVMVVRPIEGLVDAETV | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A2V2EBL5 | MRTGIFGGTFNPPHLGHRKALENFIKNASLDKAIVTVTGTPPHKKLLRVVSDEDRLKMAEIAFGDISEVSDFEIQRGGKSYTIDTLEYFKQYDDDLYLYMGSDMILNIETVWHRFEDIFKICTVVVLSRTGDDLNKLNTHAKYLKDKYGANIKVFETSPFVVSSTQIREKIKNGADFSGYLPAAVEKYIKENNLYKC | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A352WXJ0 | MQSVVLLGSTGSIGKQTLEVLPCIHKHVEAISGNENVSLLENQIRAHSPRFCAVGNEKAARDLQLRVADTNCKLFVGNDGICEMISRSVSPLVVNALLGRCGIRPTLVAMEHKKNVAMANKEPIVAAGDFLLKRAKEEGVMIIPVDSEHSAIFQCLDTAHNHPRFIRRLILTASGGPFFGKNREDLVSITPAQAVTHPTWNMGKKISVDSATLMNKGLELIEAVRLFGVDADCVEVTVHRQSIVHSMVEFTDASVLAQLGHPDMRHCIQFALTYPERCESLCKPMDFTDSFSLTFQPVDENTFSLLPLARHAVKRGGTAP... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
I0AI48 | MNNFIVIILDGVGVGELPDADLYGDKGSNTLANISKALGSIQLPNLQKLGIGNIIPINGIEPVTKPLASFGKMTEVSKGKDSTTGHWEISGLQIDFNFDYFPNGFPDEIIKKFIELTGVKGVLGNKPASGTEIISELGDEHIRTGYPIVYTSADSVFQIAAHEEHFGLDNLYRICEITRNQILTSPLVVGRVIARPFIGKDGNYSRTTNRKDYSLNPPSDTILDYLQLNGINTIAIGKIDDLFNHRGINVSEHTKSNSEGMKTLLEYVSMVSTSFIFVNLVDFDVYFGHRNDPKGFYEALRKFDDFLPHLLSKLNENDRL... | Cofactor: Binds 1 or 2 manganese ions.
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 II): step 1/3.
Function: Phosphotransfer between the C1 and C5 carbon atoms of pentose.
EC: 5.4.2.7
Subcellula... |
A0A355V3W7 | AYKSLGKTFYYIMTADATIVIADDFTDAASAEARCEQFINSVGDKLAEINSSLSIGVEDSAVSLFNSAAAGAVIEVDKTAYDVFTLAEQMYGFTDGYYNPAVYYSVEAYGFNTNGSVPETAADLPSDAAIEKFRQLSSHFGDIQIFEEEGKFYVKKPSATVEIDGVTYSMKIDLGGIGKGYTVDVVNAMLDESGFKYGYFDFGSSSIVCKSHFKFGAYELEFRNPRAEFFGQQFLKTKIKNECISTSADDVKYYVLDGVRYCHVIDPTTGKPVNKGIMSATVIGGTAAEGDALTTALMAMGKDKALTFIENKLKDRKVVF... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 325
Sequence Mass (Da): 35490
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A0A969YFB8 | MPMDEQIENTVETVLRRANLLRSGATLLVALSGGADSVVLLRAVCALRPENGLNVTAAHVEHGLRGARALADAHFCERLCAELGVPLSLDHADLPGDMRAPGAETRAREARYRLLLSRARACRADALLLAHHQDDQAETVLARLIRGGGAQGLAGMREISRMEGVTLARPLLSLPKQALLKALGGLPYCEDETNAEPCCQRNRLRAEVLPLLAAENPRAAAHIARSAALLAMDEDCLQAQAEALLTVARVDRPPYYYVRRATLRAAPAAVAVRALRAFVLMGAARLQRADAPTSAGPPPSVTDASALA | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A971JZF4 | MNHDALLFQDLESVLYTREQLQTSIAEMGKRITRDYQGKSPVMVCILKGASLFFCDLIREIDLPLEIDFMATSSYGSSTISSGEVKLIKDLDRSIHGRDVLLVEDIVDTGMTLNYLKKILMGRGAASLRIVTLLDKPSRRVAPLTVDYICFEVPDAFVVGYGLDFDEKYRNLPEVGILSPRVYAAAEKEKGAEAPHS | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 197
Sequence Mass (Da): 21966
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A0A3D5MN96 | MGRSERWVELKVTVSAESADAVAERLVGLGAGGCAVKEEEDGRVRTLTAYFPADDRAGERLKDLRAFLERLPDWGLDPGPGDMTARPVEEAEWRDQWKAYFRPRRVGRRFVVHPPWEKPGADLLRPVPGRTAAGPVVTLEIDPTRAFGTGTHPTTVGALELLERAAGMLREAGRGQEPDSLEALDLGTGSGILAIAAARVGFSRVTAVDCDPAAVEAARENVRRNGVDAVVEVVEGDALAVAGRLAADGAPRRVHLVLANITTDTAAALAAPVASLLAEGGFFVCSGVSSGEGARRVLGLARRAGLVEVERRAAEGWTSF... | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 853
Sequence Mass (Da): 91383
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A0A3D5R7G8 | MFEIKILNKEKYINIIHRLETKIFTDPWSKKMIKTEFNNKLALILGVVNTKNKELVGYSFLFNIFDEIHINNIAVKKDFRNKGLGKKQLEYIIKYGIENNFSRITLEVRESNTPAINLYKTYDFKLLSKRKDYYTNPKEDALVLVKNLKENKKI | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 18311
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A0A970RRL5 | MKVIIIGAGGAIGSCLSGWLSEVSQDIYLFDKPSVSEVLKEKGITYYKQNEAKQNVKVKVIDSLSEVENPDLIAIVVKNYSLDGVSGLIKETVKGNPVILGLQNGVENQRILPKYFDRVVYGIIEFNAWLDEIGIVGYQNRGPFVIGTLDNGMQAELKAIAELFNKGVETIITDRITDAAYCKMVINLTNSFTTLVGMGYRDITNLHAFKEILTNSMYEGVKILKKMGVKEYKAHTMPTWAKIKASATLPNFITDGMFKKNLAKMVLSSMAQDIIQRKSGESELESLIGEFVSLGDRYGMDIPYNRAVYKLCKEKFNRHP... | 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: 339
Sequen... |
A0A7C6ITP9 | MERMTVQEIAEAVQGQIQFSIPGARVTGVSIDSRTVNKGDLFIAIKGQRYDGHDFIKNAVKNGAVCVLSEKEIQPLENCSGVTVEDTAHALKALAKHYRRKFDVKVVAVTGSTGKTTTKDMIAHVLSSHFNVMKTVGNYNNEIGLPLTVFNINPKHEILVLEMGMSGFGEIAALTDIAMPDIAVITNIGVAHIENLGSQDNILKAKTEIFNSFTDEGLAVLNGDDRYLLTLRDKYHFDKIYFSIKTKQAGFINAYDIKSTQGGISFKVDILGKGEQINIPVPGEHNIYNALAAIAVAIHLGVPAHKMKHALGSVTANKGR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A1F6SW40 | DYIGKNQFRGAVLGLSGGIDSALTLCLAVDAIGPGRVEAVMMPSRYTAAMSLEDARRLATALGVTCREIPIEPMFEAFLAALQEEFRDMQPDTTEENIQARVRGVLLMAISNKTGKIVLTTGNKSEMSVGYATLYGDMAGGFAAIKDV | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Length: 148
Sequence Mass (Da): 15796
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A0A2N6ATN3 | MEKKIAVMKFGGTSLMTSNQRDAATKRIIEMKNSGKFPVVVVSAMGRFGDCYATDTLIKMIKDENEACDNRNLDMIASCGETISAALLSETIRKTGHESVALSGAQAGIHTDSSFGDAKITSIDPENISKWMNKGHIVVVTGFQGVDHEGFATTLGRGGSDFSAVVLSKALKADIVYIIKDVPGVLTADPKITEKAHLIEKLSYDELYEMSKSGAKVVNFKAVSYAKDNDITLVVKSLYSPIEEKGTQISAREEKISVSAEEKLLTAIVSKEGVLQYALKERDSFKIIDLLNRLSENKISIDMINIGIENQYFAIDEKNQ... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to t... |
A0A2H0B0G1 | MIXXXLKIEEKQAKIKEIEEGMKSPDFWSDREGANEKTKELKNLKTEVEKFEGLEELSEMAGSEDLKAIEDEIKKLEIYTYFSAKYDDHSAILNFYAGAGGDDAQDWTEMLLRMYIRWAENNNYMTKILARSSGAIAGIKSATLEIDGPYAYGKLKKESGVHRLVRQSPFNAKALRQTSFSLVEVTPKIEKSEEIAISESDLKTETFHAGGHGGQSVNTTDSAVRITHIPTGIQATCQNERSQLQNKTSATAVLQARLAKMLEDQHKEKIAELRGQSAEPEWGSQIRSYVLHPYKQVKDHRTGFESKNPDAVLSGDLNEL... | PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Subcellular Location: Cytoplasm
Sequence Length: 330
Sequence Mass (Da): 36979
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A0A970Q6R1 | MASTIITAVASVIIFTLMVFSHELGHFIAAKKAGVEVEEFSIGMGPKVISWGRKETKYSIRIFPIGGYVKMLGEEDKAEGEGSFYKKSLGRRMSIILAGPIMNIVLAILLFSVIFFVIGTPTTVIDTVMEGYPADAAGIRPGDRVEYIDGERVDSWERLQYLVSVSKGEQMVVLVNRNGQTIALDVFPVTDPGTGQSIIGITPTSQKDPIGSIRLGITRSFEVIALMVTYLGQLVTGRASAEDVVGAVGVIQLVNQAAKTGVLNVMFLAAFLSLNLGVINLLPIPALDGGKMVFLLLEAVIGKPIDVEKEGLIHFIGFVF... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 339
Sequence Mass (Da): 36776
Location Topology: Multi-pass membrane protein
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A0A9E1AR58 | MSGGGLKYLLKEGVKNLWTNRLMTFASVGVLTACLLIVGFAMLFSQNVNSMVGYLEDQNEIVVYLEKENTEERNIEIESELKQISDLKEVTYFDRAEVFQLQKEKLGSASALLDDDDDNPYYAYYTVKEKDLEKITATVAAIKKIEGVKQVSFYKDFADAIVKVKNMVNLFGGAIIIALVLVSLVIIANTIRAAVFTRRKEINIMKYVGATDNFIRFPFMVEGLLLGLISAVLAFLMIWGGYSMLANAILENSTVTFLASMMQRMLPFKEVAVGLGLCFAGAGIVTGMLGSIISVRTHLKV | Function: Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation.
Subcellular Location: Cell membrane
Sequence Length: 301
Sequence Mass (Da): 33326
Location Topology: Multi-pass membrane protein
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A0A970XKB3 | MTSKVLVGKILTAHGIKGEIKVLPYTDSTGDFCQIKNLHIINSHYEVQNSRPMGKMALIKLKDIDNRDSALNLKGDIFAERIDLPDKVGRYYINDILGFSLICNGIDEGILSEIVNYGTIVDTYFVKSKNGNYSFPALQEVIEEIDLDKKRIVLNEKELKKVRVYEI | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A927SQ07 | MNIPEHIAIIMDGNRRWAKKKSLPIKLGHKNGAEALRKIVEYSKQIGVKYLTVYAFSTENWKRSKEEVDDLMNLLREYLGKIEEDIAGKNIRAKIIGDKKRLDLDIQEKIRELEEKTKDCTALTFQIALNYGGRDEIVNAVNSIINDNVKEISEEIFERYLYTVNAPDPDLIIRTAGEKRISGFLLWQCAYSEFVWTDVLWPDFNEKDLDIAIEEFNKRIRKFGAN | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 226
Sequence Mass (Da): 26301
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A0A149VUL4 | METTQANGLERSLNLTIPLNQLQEEVAKRLKHLSKTAKMQGFRPGKVPLSILEKQYGGQLHQEALGDLAQNQFFMAIKENNFKVAGYPSFDANPDHKEESTIGLVARFEVFPDITIGNLKEVTINRPVTEVTDADIDRTLDILRKQRVSYTIVDRQAQNDDQVVIDFKGFIGDEPFQGGEADNYQLVLGQNQFLPDFEANVIGMKQGESKSFDLTFPEDYQATNLAGKTVRFDVKVHEVKEPVLPPVDEEFARSVGIQDGDVSKLRAEMKKNLEREVKNRIKSQVKDQVMQALLDKTLIDVPQFSLSQEVQRLRQNTLAD... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A3C0P9W8 | MEITTELVNHLAELSRLKFNEKETENFKEEFAKTLNQIEALEKADTTNVEMQSTILNAETELKEDKPHQSLQKADAIKNAPETMGSSIAVPMMVD | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A7C6S4Q6 | MIRIILQSLIALIISFLVSALLTPLVIKIVGKLKARQTILHYVDNHLNKQGTPTMGGIGFILAVIIAMLFLGFSGSSLMSVAVMTAYGVVGGLDDFIKIKYKQNQGLKAYQKIIAQTLIAIIIAIYIFRNKNIGSYILIPFTSIEINLGFFIIPFIIFMFLAVTNSVNLTDGLDGLAGGVTLVFMLFFCLIQLIYVNHLYNEGYTDQIINEYIGQIIFAGAVMGGTLGYLIFNSYPAKIFMGDTGSLALGGAVACATVFTRLELLMPIIGVMFVLSSLSVIIQVLYFKATGGKRVFLMAPLHHHFERKGIHESKITVIYI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yield... |
A0A061E365 | MLQGRKQLKDLVKKVQAARDEMQWGEEGPPPLLVKIAPDLSKEDLEDIAAVALALRLDGLIISNTTISRPDPVNKNPVSAESGGLSGKPLFNLSTNVLKEMYILTRGKIPLIGCGGISSGEDAYNKIRAGATLVQLYTAFAYGGPALIPQMKAELAECLERDGFKSIHEAVGANCR | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
EC: 1.3.5.2
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Sequence Length: 176
Sequence Mass (Da): 18873
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A0A3D0Z1V6 | MSGPDRQGGQVRNLRLTVAYEGTAFHGFQAQRPGLRTVQVELERSVSALTGEAVRVTGASRTDSGVHARGQVVNFRTGSAIPVDRWPRALGSHLPPDLVVQDAVEAAADFHARYFALGKIYRYLVYESAVPSPFWDRYALRWPGPPLDTSAMHRAATALQGYHDFRAFHDTGSRVGDTRRHLFYAGLHQFTDEDRPAIVPPPAGPGKTRFLGITLIADGFLYHMARVMVGTLLEVGRAGLTADSLCERLADGRRDLTGPTAPAKGLWLERVLYCQAALHSLLPPI | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 285
Sequence Mass (Da): 31235
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A0A845MCA4 | MDQGLAQLLPLVLIGVVFYFLLIRPQQKRAKDHKAMIEAVRRGDNVVTAGGIIGKVTKVRDDNVVQIEVAPEVRIDVVKSTLSDVKSKADPAPAAKDAGDKTEGDKPAGGNPVSKLFKK | Function: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-Y... |
A0A928RNS1 | MKKIIGNFKMNQTPSQTKDYLINFLPRVDATKNEIILCFPATSLTTAKFLVEGRGVKLGGQNICDEEINHNMGEVNGVMIREAGAEYVVVGHSERRSKYKENTRTNNRKIKIALKNRLKVILCVGENLAERNTLKMLDSLKNQIEESLKGIYENELQHITIAYEPIWAIGTGKLPTNKELENAVKAIRKVICDDFSEKAGQSIDVVYGGSLDAKNIGQYLKLDTIDGFFVGGSCLDPAGFAQIIKLI | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 247
Sequence Mass (Da): 27495
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A0A3D5WRA8 | MKERIIQNVSEAAKNQRIAVGVSGGVDSMVLLRALIEAKKSTDFSFFIVNIEHGIRGRSSENDSRFVADFARSHGIECRTFKVDSLRRAKEFGETEEEAARALRYGVFQKLLIDGDCDKVFLAHHEDDQAETVLMRIIRGTGIKGLSGMQKETRGYVRPLLDVSKEEILDFQKKYDVPYVVDETNFENDKTRNLIRNEIMPLLNRAGDATGSLNRLSRIAADTEEFLSTLDLPLEISKDSVGIDVKNPPVFLLKRAIRNAFLALGVEKDVEEKHVLIILDLLQKENGASVDMPYGVVVTKEYDKIVFSKSKQKQAFTTPF... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A524NE94 | MSTGNYMNRDISWLSFNNRVLEEARDKHLPVYERLKFLAIYSSNLDEFYKVRVAAYRRILNQDPSFVLSEILRIVDHQQQEFGKIFWKELVPELKKNNITLKQNHRLSGLHREFVDRYFREELVPCLQPIVLLRDKVSPFLKDGFIYLAIKLFKRSKQADAVKNKKARYALVNIPTDQLPRFIELPAMKERHTIIFLDDIIKMNLEALFPGYVIDSSFSIKLSRDADLEIGDEFSGDLAEKISKSLVKRKTGVPSRFLYDNAIPDSFLKLLQCTFKLSPGDLVPGGRYHHFSDLFSFPNPLSPLLENLSLPPLVNKELAQ... | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n)... |
A0A151BW64 | MKPSPDAGSETDDVDEVPAAPDAAREYLGDQFELMSRYVGHLATSAISHGLIGPRERETLWTRHVLNCAVLGDIIDPGSSVIDVGSGAGLPGLVLGISRPDLEVTLVEPLLRRSTWLSMVVEDLDLTNVVVRRDRAEAVHDLQADVVTSRAVARLDRLTGWCAPLVAAHGRVIAIKGATAQEELDLTRDALATLGVIDARITQCGEGVVDPPTTAVELVFGDRSVADRARTKGAGRKTKSKAKNRRRAG | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 249
Sequence Mass (Da): 26596
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A0A947YTH5 | MDKKKEKSPVKSDSGTLDLFASAGISDSDSSTPPEKNIPSESKNRLPVPVRLPETPPVPERREPEETVKSTIPPEKSELVYTVSDFINSLNLVLEKNFSRVWIEGEIGNISSRNNVRYFSIKDSKSLIDCVLFVWKTKIDFNLEEGLKVRVRGYLNVFPSRGKLSFNVEIIEQTGAGSLNAAFELLKKKLEKEGLFDEKYKKKLPAFPRRVAVITSPEGAALRDILKVASGRIAAEIIIVPAVVQGKNAPDDIVRALGTVSRMEDIDVVICGRGGGSAEDLSCFNDEKVARAIFECRVPVVSAVGHQTDFTLADFTADRR... | 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... |
A0A352IJT6 | MSKEKKNSEINGNNADINKHDKKKSRARKKRKVIIRATLLLILVAAIIAGGAIFGMVMGIIRNAPKIDATNVLGTLTESSVIVDENGDVIEQIHDPNENREIVPLKQIPKYLQDAFIAIEDHRFQEHPGIDIRRIAGALMHNVKEGDPTAQGASTITQQLVKNLYLTDKKTWERKITEAYLAINVERVLSKEQILENYLNTIPLGQSAYGVQTAAYTYFSKDVSELTLAESALLAAAAKSTVSYAPFNRYNLEGINDIPEEDVVGYVFIGSVQYACVYNQNAIDRQHTILNRMLELEYINQEEYDGAMAEDMRAALTPGQ... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
EC: 2.4.1.129
Subcellular Location: Membrane
Sequence Length: 462
Sequence Mass (Da): 51619
Locati... |
A0A929XAV7 | MQAGKTSLSIKLAKKINADIISIDSMQVYKYMDIGTAKVTEEEKEGIMHHMIDVQEPDERFSVAEYIRKVKRIEQDILKRGKNIIIIGGTGLYVNSLIYGFTFEENDEKVLLDYRKSLEESIESGKETLDTLYEKAKKIDEKAADMISRTDKKRIFRILEIYYLSNTGKTEIDKIRKENNEVSDIRVGVYNYNKNLEYKLFYIDMDREILYNRINKRVEIMIELGLIEETKKVIEIIANKKKVNYEEILKHYDDITALQAIGYREVIVYLKNEIDYEEMKEKIKQNTRRYAKRQITWFKKNEKIMLDREKTDEELIEIIM... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
N0B681 | MNLRVSGISLKLGLLFSSVFLTLIFILELVLYGVFMHIFVDYVTQDLLERGSNHAKILSENYNQNTIDHVITMEKGGRTSVLITDSNNQIIASSVHPDKDMKSHLLKQGNMKVNKLLEKDWKHHDYLISVTTIGHNKGHLYMYYPTNIVREIVLVLKILILLTFIGMILLSFGLIGILSQKITRPLLIMKDATQKMAKGEYKQKITTKGNDEVAQLGQSIQGLGEKLQAFEDSRNDFLADVSHELRTPLTYIKGYSDILSKGMYKNSIEQAEYTAIINKEANRLSFLLNDLFEMSKLQVGKFELSMEMANINTIIEKVIM... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 455
Sequence Mass (Da): 51584
Location Topology: Multi-pass membrane protein
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A0A970N4J8 | MKDGFIRVAAATPKIKVADCVHNMQEILGIIKSAPEDTSLLVFPELCITGYTCGDLLFQPALLRAAEDAVAGILEQTTDIDTVVLVGLPVAVRSSIFNCAAVCQHGKLLGLVPKSYIPNYSEFYEMRYFAPADDEDYHICFAGQDTVLGRNQLFVCRSMPDFCLGVEICEDIWAIHQPSQNLAESGATVIANLSASTEGIGKPGYRHQLVKMQSARLVCAYLLADAGEGESTTDVVFSGHNMIAENGVMLAESKRYTNGIITAEIDIAHVSYDRRRISTIKNKGNMNVVWFDVPVKDISLTRVISPTPFIPSDINAQQRC... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Length: 431
Sequence Mass (Da): 46993
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A0A355JGT4 | MDKFYIITNRDKDQNLRFTEEIVQYLKEHGKKCQVQQAERRVEGEYHYTDPALIPEDTQCILVLGGDGTLLQAARDVVHREIPMLGINLGTLGFLAEIDKTSIYTALDKLFADDYEIEERMMLHAVLLDGKETTALNDIVVTRASSTLKILDLDIFIDDEYVDDFKADGIIVATPTGSTAYSLSAGGPIVDPSLNSMIVTPVCPHKMYSRTIIVPPEKTVTVKCKAAIDNEAVVAADSEILGKLSGNETVVIQIAQKNFKLIRFKGYKFFSVLHNKLVKKES | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A7L5C0A6 | MNWISVIASGVALLAALYHLGFAFDRPFTEGEHAIIHVGFAALIVGVDQARRRRGAFRFLAVACTVAALAASVYFVQISEELELRFGIGLTMPQTVAGIAIIVAVIILCWMEWGLIIASLAVIGLSYFFFGDNIPGAMRAASHPSFEYAMTFLISSGGTGLYGQVTPISANIVFLFMVFGALLASTGVTRLFMELGNWLGRLLKGGAAVTSVVSSALLGTVTGATVANVAITGVFTIPTMKRQGFRAEDAAAMESVASCGGQILPPVMGAGAFIMAAFLGVSYVDIALRALVPALLFFGSVLLVIAFIVRKSGHIEECDP... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 629
Sequence Mass (Da): 65899
Location Topology: Multi-pass membrane protein
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A0A937DZE9 | MKRFFIELSYKGTAYSGWQVQPNGPSVQQTLEEALALILRREVPVTGQGRTDAGVHALKSFAHFELEEVPMDNKTLTYKLNRLLPQDIAIHRILEVQPDAHARFSAEAREYRYFIHLGKSAFLKDTALQLYRIPDLEAMQKAAQYIPGEHDFSSFCSARAEVAHKRCTVSQAEWRQDGRMLTFTIRANRFVMNMVRSLTGTMLEIGAGKRRPEDMPLILAALDRTQAGENAAPEGLHLSDVIYPSSIFISPEK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 253
Sequence Mass (Da): 28622
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A0A943J1I3 | MDLIETGKIVNTHGVRGEVKIYPWTSDLSRLLEFEEFFIDGESYSVESIRVHKDMLIVKFKGIDSVKDSEKLRNKIVKVDASLFKLDDGEYFLRDLLGMVVYDADTGVCYGKITDIFQPGANDVYEISEIADGKSIKRYIPAIKDCIIKTDIDNKVMTVRPLEGLFDL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A9E2BLU4 | MLTRAEDAVRVLAPAKINLALAVGALQPEGYHRVATVMATVSLSDQVILAPSEDDSLAVEGPFAKGLPAGEDNLALKALRLFSDAFGRPQGWDGVALTLHKELPWEAGFGSGSSDAAAVLRGLAFLKGPQGPSTDELLDLAAELGSDVPGLLLGGLVEGLGRGEKVRPLKPPPPLPVVLVAPPFRLSARQVYDVWEERYGPRAGEPQDRREWQTFMEEVRRQSWEDVWPLCFNDLEPAVRSLLPDLDPYLALLENETVLAFGVAGSGPGLYALLEDGAAAGRLAARTRQMGAWAQTGQLLPGHRPPERRRGR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A8T4DRI1 | MDLTIEGKLYHDGAFEHGCIGIDKGKIVAIKKILKTDHHIDVGNSLLLPAGIDLHVHFRDPGFTHKEDFSTGSQAAAFGGISCVFDMPNTKPATTSIQALKEKIRVASEKSYVDFGFYAAVCDENIGRIAELSSLCNGFKIFLGSSTHALKLSSQHLRVALMEINRTGKLSLFHAEDEHCLKTHKDVEHTLIDHLRCRAAECEEAAIRHIQNSSQSLSSPLHICHLSSCDGFEMLRKKLGNMSVGVTPHHLFFDVNALKSNQTFYKVNPPIRSSFDRETLWYGVNHGLIDVLESDHAPHTKEEKLVDFDTAPSGVPGVET... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
EC: 3.5.2.3
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-car... |
A0A3D1WFV0 | MKVLFLGSPNFAKTVLDGILKAGHEVVAVICQPDRPASRGHKMQMPAVKEYALEKGLKVLQFEKVNRNLDEIAALDYDIFVTASFGQILSRDFLAIKMGLNVHPSLLPQFRGATPIQTALLNGCEKTGVTIQRMVYEVDAGDIIEQEEVEIKPDDDYVTLEKRLSEVSVKLLTKALESIENGTAKFVPQQGEPTFTRMIEKSDGKLDFLRTASENVNKVRALAHNPGCYFELGGQRVKVLKAALADQENGAQNQPKDIIKDKNHFLIKCLHSVIEIVSLVSPNGKTVDGKAFLNGLRNINKVD | 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 Acti... |
A0A965Z9R4 | MSPHTSHTIRNITQRITEALRPVYPTEECTEIVRLLLEEVTGLSRVQLLASPLHPLTENEEKNLTEALYRLQHHEPIQYILGKTWFYGFPLTVNRNVLIPRPETEELVTMAMQEFTKNHALPPVVLDAGTGSGCIAIAIKSLNPQMKVAAFDLSAAALEVARLNAASISAEIHFFRDNIVAFSGLPLSEKSGFLISNPPYIMEKEKEQMRPNVVKFEPGSALFVSDDDPLIYYRGLKAIAQKWVISGGFLFFEINESLEKEMRNLFNEPNFYDIAVEKDMRGKPRFFRCRKA | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A927S986 | MLRDFHIHTTFSFDGRSTVEDHLKKAKELGIGELCFTEHFNPNGPSGLLNRRIPDRDGYFAAIDAGIKNHPECIVRRGVELGLYDLPSCHMAKELLMGWDVDFILMGSHFNHAGRQYWIPEEWNGDSKQKVMEDAMENTLVFVENLENFDVVAHINFFSRACPYADKEIRYSDAPDAIDTVLKAMVERGKGLEVNTSSYGKFGFFMPGDTIVKRYLELGGEVITIGSDAHSADALGSGIKEAREMLKQVGCRYYATFAERKPIFHTL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 267
Sequence Mass (Da): 30164
|
A0A971WEM7 | MTNDLMGYFWIGVGNLASEGKRSNRKGLILAGAAIVALAGLFIYDVFFNIPEYTKSDFSMGTVVTQTLTGNDAEKAAGEIFEAFDNIEQKWLSWRLPNANIAKVNEAAGTGFPVADNTVEWLKKTLDVCASSSGALDITIGRITALWDFGGEYERLPKKDEISDMLGKVDYRGVEFTGNTVKIARGQSLDMGAVGKGIACDEALKILRENDIKSAIISVGGSILLYGGKEDFRVGIRDPEGRPTDYMGVLTLKSGCISTSGSYEKTLVRDGGTYHHILDPKTGYSAQSGLTSVTVVCDSGLLTDALSTACFVLGYENSLP... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 368
Sequence Mass (Da): 39419
|
A0A3D8SQF3 | MSADTTTSLSSKNAASKQDAALTGASKAFGKPPVKSKSKVNNTYSGNNGALAAAKRASPSRNASLSRPEQPVAEQRLLYQRSGSSIGSENDWEHSAFLQRRMGTGNGHLQPPLDSRDPSKSPSFIAATLAASRSVPVSPAHTGQALSPAALQKLAGSVRRSSASVRSGSSRGSSDHVLDTTSIPPTHSLIGMFERSAAQTPKKKTPKQQRAFTPEVQMSSMQPQPATPSPMPVQPRTPSPKSAKRPPEIQSPKPQFLRTHSALSSPKTFASPAKSQPAERPVTSSGMSAKPASKPAPKPKPAPLPRRSSTPGARSNLVPI... | Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma mem... |
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