ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A7X8LBG9 | MKIIKTLSNMDLKKQLIIAFIAFIIFPSLFIGIILMKFSTNKIKELAISSAIRNNEQVIKNIDGFLEMVIKLSEQPISDPQMNAILHKDYSSLSYPEYETSNDFDAAGRFIYQKIVSYSDLIDSVILYSAASNKVSGRVPVDYINIHYLETKFYQEPWIQKTMNKGGEYSIIGIHQECLLSPQKKHVISVGRNVIEPGTNNSLGIILINIDVEKLEKLWLDIETTENSRFYLIDEDNNIIFSKIKSEINKKTSSVFGQEILFNDKTAQSMMLLDQKVYLISSLSSLSKWKVVSIIPQNELFSFAQIMLKIIIFSIVGAIAFSIIIAVVIATGITKPLFKLNRKMREVAAGNLNVAIDIQGGQIGEISKTVDTMLKEIRRLIQQIYQEEEKKRKAEMLALQTQINPHFIYNTLNVIKLMASMQGVKSIENALTSFSNLMAFTVKGEASYINIKEEVRFIQDYLAILDLRYYNKFKVQYDIDEEVYQYKTLKFLLQPIVENAVFHGFDNIDRKGELQIQIYKEEKSIIFQVKDNGKGMKDNTIQSLFLQSQKKFSGVGISNVYERLKLHFGSPYGIFITSQLGEGSVVMIKIPLIRSEKNENIDC | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 603
Sequence Mass (Da): 68864
Location Topology: Multi-pass membrane protein
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A0A0S7X9M7 | MVRRAFLSVHEKSGLLEFASFLVQRGVELFATGGTASFLRESSVAVRPAEELTGFGELLSGKVKSLSPRLHGAILFDRSNAEEKGQTEREKIPSIDMVVVNFYPFYNVNTDTALTDALSLIDIGGPASLRAAAKNFRWVVPVPEPGAYERVMKEMSGDEPAVTVALSRDLAARVYEMTSSYDSIISAYLSTIPVTDEGQSSPFPRRLALSLNRLWELRYGENPHQAASFYVESSPQAETRSAGRKLHGKELSFNNLLDIDSAVAACREFEAPACVVVKHRTPCGVSTASDALEAYRTARDCDPLSAFGGVTAFNRPITGTLAREMSGLFLEVVAAPGFETEALEILSKKKNLRLMELPLDYFVKPESPGTLMRSGPGGLLFQEEDSRAESVAEWRTASKRAPTQEEAEGLFFLWKVVRHVVSNAIVIGRRGRTLGIGSGQTSRVDAVETALYKARRAGHDVKGAWLASDAFFPFRDSIDLAARAGITAIVEPGGSRRDEECIHAADEQGIALCFTGRRCFKH | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Length: 522
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Sequence Mass (Da): 57007
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A0A433U2L0 | MASKRREKSAGCICNRREKMKLLVLRMMFVMLACGTLFICIMVSLSIKNKNSSAPGLELTPMKRSGFSLQPEPTKRNGKFVGSNGQHLFYKAKARDWFVEPEIIKRYCRATNLTQCSPVFRTEQQKQADRASRGRPVRVTIYRPFTPDPTEPNFSECNYNNCVYAGHEVTPESDAIFIYGIKLNEDAKVPAVRLPHQVFIFSGYEPVGSGYSTALSNSNSKWRTFFNATMTYRLNSDVFKPYGVLDFQPKAEKDLPDYRAIARRKTRTAIWIVSNCRTQSMRMQYVKEMQKYMTIDIFGKCGEKCEVVDERCVADFNSTYRFYLAFESSFNTDYITEKFFKLFIDDTHIVPVVRGSLDYKRELPEKSLINAADFKSPKDLALFLKSLEVDEVEYSKYLEVKDRYRAIDTDRWCGLCEYMHKLWTSPHVFTHGRQVDLQKELLHGHVLSPSVIG | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 453
Sequence Mass (Da): 52376
Location Topology: Single-pass type II membrane protein
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A0A1N6LYA8 | MSSSQWLGTIRHIPGLIKIKLSSWVTLTSYSGYYISSDWDIQSAIALGLGVFCCSASSQAANQLIELKNDIKMSRTCNRPLVTGKITKKQAIAACITFATIGTTTLAYISPISAIIGLSNILAYTLIYTPLKYRTIYNTQIGAIVGAVPPLIGSTISNVQLSEISPWILFYTLYCWQMPHFYLIAWLNRKDCLKVGFRMVGITDDSGKTTGKACIRWHSLTTLLSALLLAANITNSTVPISYAFLLPLTINLSLLRQFILFMKTSTSISAIKLFKNGLWHILALLASTSYALDNSTRDFLKP | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Subcellular Location: Membrane
Sequence Length: 302
Sequence Mass (Da): 33283
Location Topology: Multi-pass membrane protein
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A0A1R4AAA0 | MILTLFANGNSYLVFNHSSQSNQFNELNDYLLKLSILRESVVTTKYKLNVARKLNKLFLKLGYPVSLKRSLYSINSDTANIIRKQLKQLKHNNSLEISDNTIKKSSFMKYPNVEGCFFEENAHDHHTPNILSLSKNINSRNYYHHLTIELKVKCGLDDFSDYPNLFTIRNTLRHLSSMNYVSHNPTKLFSNAITEIKQQLLMLSNEINHKYIKIFINGQVIGNNEINNTQLLDIVANTITSSNGLIGNILKLQASSAGQQFLAHVIYLLLDIFYQYSGHLTDSWKIYYLQRFKTFNISPCDIETNIHLSIQIGNFKKGIFLIKTLLSLLITMGHIELNGCLIFFSKKFNQYNKLDTGITYHPLVKLRDYLERYSRKGYPNISLHRTNSFKSLFVKYNIVRDSIRWLQNFFIGRTMMDCSLIYNIQNAKDNHPSTDNSMEKHHIYNELMPRYGYTMSNNQLIKISLVDLDIKPYRRVGKWANDTYIAIKRYRSTLTNHQQLIVK | Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
EC: 2.7.1.158
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Length: 503
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence Mass (Da): 58651
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A0A7C3L4D2 | GSQFFITDVPTTHLNNRHTIFGQCIEGMDVVSKIARVPKGPMDRPATDVVINKLTILRKK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 60
Sequence Mass (Da): 6706
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A0A497IIG2 | MLLISMTIAKAFAPSHITGFFVPVMRERAVESGSLGAGVCLEDGVVAEVALQDETRVTMEGEPFRSAPLVDALLELTSEPLWVDLHLDAPLGAGFGASGASILAALSAANHMLGLSLTCNEIATMAHRAEVVGRTGLGDVAAQVTGGVVLRIKEGIPPHGRVVHIPTKSVPVSWACFGEISTAAVLENVAVRKRILRAGRSCLKKLLDRPTLENFMLESRRFTEEVGLAGESVVDAIETAEASGVVAAQAMLGDTVFAIGENLFSEFENSGTSQINHTGVVLLK | 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: 284
Sequence Mass (Da): 29839
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A0A662R2D6 | MEEIIKTTEKRVRILKTERILGGELPYRPSHRGFLNSLKKGKKKYGYALIAEIKPASPTTTNRLITSQDAVKIAKDMERGGASAISVITEPYFFKGSIGNLKLVRRNVRLPILRKDFIISSLQLTECYQDGVLLITSILGNELEDMIKECKKLSLEPLVEVRDIEEAEMAIDAGARVIGVNNRDLRTFEVDVNTSVELIPSIKEGDNNVFVISESGIQNVDDVRRVVEAGADGVLVGNAIMKSSSIYEKTHVLAHAMEVNK | 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: 261
Sequence Mass (Da): 28984
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A0A1V4K4G1 | MRAPALGCISLVLCLLELPACLPLPDGRAPKRREPPDRRPSPASLLGEQPGPQPPAPPQPAGPRHKPLLPSRRPSGPRHKLLLPKLSPKLSPRHRPKLSPRHRPPLPRHSPKLGPRHEPPFSPRHGSGPADPARPLSPQDPDPCEGPEPSKAKAEYRNYTDGKLLDRVYNTYLQMHTHQTVDFVRKKNAQYGSCSLRTMGAMEALDLLDQLVDESDPDVDFPNSFHAYQTAEGIRRAHPDKDWFHLVGLLHDLGKVLALFGEPQWAVVGDTFPVGCKVQKSVVFGDSTFHNNPDTRDPRYSTEFGMYQPHCGLENVLMSWGHDEYMYKVMKFNRFALPKEAFYMVRFHSFYPWHAHGDYRHLCSEQDLQMLPWVQELNKFDLYTKQEELPDVQQLRSYYQGLIDKYCPGQLCW | Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
EC: 1.13.99.1
Subcellular Location: Cytoplasm
Sequence Length: 413
Sequence Mass (Da): 47138
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A0A1V4J585 | MKESSLPVGALHVEFSRPVNLEEVARINPEVKAGGRFAPKDCIAVQKVAVIIPFRNREEHLKYWLYYLHPILQRQQLDYGVYVINQTCCGGSGLARDQSITGMATSVVTLAYSNSDVDLIPMDDRNTYKCYSQPRHLSVSMDKFGFRLPYNQYFGGVSALSKEQFRKINGFPNNYWGWGGEDDDIYNRLVFKGMEISRPDAVIGKCRMIRHSRDRKNEPNPERFDRIAHTRETMSSDGLNTLFYKGSLKIRKR | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 253
Sequence Mass (Da): 29083
Location Topology: Single-pass type II membrane protein
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A0A522CB75 | MPEIRVLIVDDSPFIRKALLRIFETDPSIAVVGVARNGKEALTKLIESAPDVITLDIMMPELDGIETLKIIMETKPTPVLMLSQYTHEGAELTLNALEFGAMDFIDKSTTGLMDFFGLAKEIISKVKELTGKKPLRIVSQATALKDYKSNGFVDVVAIGTSTGGPPALQALLPKFPKDISFGILIVQHMPQGFTGPLASRLDSMCQIHVKEAEEGDKIEPGLALVAPSGLHMKVTPPFNSPLNKGGHRGVKIQDSNKKIKLDMEPLNAIHRPSVDVLFQSVAESYGSRSIGVILTGMGSDGAKGIRLMKEQGAVTLAQDEATSTIFGMPKVAIESGVIDKIAPITSMAEEIMKRA | 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 residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
EC: 3.1.1.61
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Subcellular Location: Cytoplasm
Sequence Length: 355
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Sequence Mass (Da): 38214
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A0A061NGZ3 | MTEQLQKVSIMEPQNPVRPTAIIGGKSSGILNWNDIPYPSFYRTYRELVGNYWIPQEVSMAPDARSLTTLTPAELNAYKLTIGLLATLDTPQARLIHAVSEYVTDDSVHAIAAVIAQQEVVHNESYSYALSSLFSYEEQRKIFDDARQNRTIIARNQRVMAAYDAFLAEPTPERLVKVIVFSMILEGLFFYSGFAFFYNLARQQKMSATSQIISFINRDELVHGKFMSELLRAVLGENNTLLTFELTEFIYEEFRIATESEIAWADEVLTDIIGIDNDEMAQFVKYRANKMLKMIGLDALYPEATANAMPWITAFVDNFDGTKTDFFEARNRSYEKVDADNGFDEL | Cofactor: Binds 2 iron ions per subunit.
Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 346
Sequence Mass (Da): 39435
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T0P8Q5 | MCYVAGSSNEPLCEATMFELIKSMAFSLVMVPVVMVGILGLIYALGELFNIISRIGHSEK | Function: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with a broad substrate specificity. This protein binds to AcrB and is required for efflux of some but not all substrates, suggesting it may influence the specificity of drug export.
Subcellular Location: Cell membrane
Sequence Length: 60
Sequence Mass (Da): 6525
Location Topology: Single-pass membrane protein
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A0A3M1SBS2 | MKFSFTNRRPDRIKTDILLLPVFKGQTPEPYGGLPEIKTLIEKPIKDGFFKGEFLELLLLPSPSGISASFLLMLGMGEAQEVNAEKIRKAGGKTASHLRGKRISRLTVFSQPLMVISDAEAAFTEGFLLGNYTYSEFKKEKNPLKIRELQFTGRETKSKSNSLREVTLSAGATNYARDLINTPANHLDPLGLAEKARELASSRIKVQVIRKRALERLGMEAFLSVSRGSSKEPCLIILKYRGNPSFKKEYVLIGKSVTFDSGGLSLKPSEGMEKMKYDMSGGAAVLGVFQYLKKAGLPVNVTGILPATENLPGGTASKPGDIVRTITGKTVEILNTDAEGRLTLADAIGYSRRLKPLAIIDIATLTGACSIALGNEAIGLMGNNKDLLQGIKNASSVTGEKVWEMPLFDEYKEYIKGEFGDLKNTGGRSGAFVTAGYFLKEFAEDTPWAHLDIASTAWTDKEKPCYPVGATGVGTRLLISFLKGTKR | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Subcellular Location: Cytoplasm
Sequence Length: 487
Sequence Mass (Da): 53048
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A0A533Y402 | KLAKVELIRPKTVIGTDTAGSIQSGLLFGYAGLVETVVRRMEHELGRSTYVIGTGGLSSILAAETTSIQKIEPLLTLEGLELLYRRAQGAPPTTMQV | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 97
Sequence Mass (Da): 10383
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A0A922WQ71 | MSAFRILMSASRRTTLARLSTSGPAATWMSRASEMSVANPRSSRPSGFAKTAFGNSSAWFAKTPSTTVQSNSCARRLLDNVLPSGRWPCELILASLPRRDTFSLPFHPWHASGPRSSDREAALHRGCQTECSAGRRRMSQVLIVGADTMVGANWIRLAGENGKEHSHGQLVGLPVATPADHLRQIVGHTASAAKTTASPVRRVVHCGAAGANGWNIRRAENTANSSEVEKWARLCAEHHIPMTLISSDAIFTGPWMFHSESSESFCESFEAQTLRQMEAAVLAASASHLIIRTHPFGWHTRDGGMEECLETIRSQSCCQIDGTRHASPIFVNDLISIVQRAWSSGLSGTYHVAGAERVSHAQFIQRLAQTFGLNLRRMSSGGPLEARATGFASGETSLQTRKIRRAIGIPMPMLHEGLAQFARQPTAVSYVSREFAAA | 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: 438
Sequence Mass (Da): 47571
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A0A0G0JYH1 | MTLLNSIILAIVQGITEFLPVSSSGHLTLFQYILNTTPSLSFDIFLNTSSLLTVFVYFAASWRLFIKDFKYIIIGSIPAAIVGLLFKPQLESLFSSPKYLPLFFGISALILFASRYLVRQDKKLTYQKALIIGLFQSLAILPGVTRSGSTIVAGLLLGLPATMAFQFSFFLFIPASFGALLLELRDNQFSQFFNLNYFIAFLITFFVGLLSLKILKKSIQSQHLWYFSIYLVILAVILFLSLQT | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 244
Sequence Mass (Da): 27422
Location Topology: Multi-pass membrane protein
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H0ADH5 | MEFSEDIEQRLSKYFDRIYEDSEKYFLIPLGLIILGLGILSYNFAATGEFLDKGTDFAGGTEITYEVDGGFSSTEVEALFADAGRSGTNAMTQNTGERELLLVEVPPPDMDRDEALQIMEDSGYNVTVDGFNSISASVSGTFFQQAIFAFILAFTTMSMVIFYAFKNFTPSVAVVFAAAGDIIIAAAGMTVLGVPLTLGSLAALLMLIGYSVDTDIVLSTRVLKMNRGSVKSRMWSSAKTGITMSAGGIAGFTLLYLVSTSIVGPSELSNIAAVMVVGLVADIPLTWLGNTAILKKYVEGDFEGLEKVMIPWK | Function: Involved in protein export.
Subcellular Location: Cell membrane
Sequence Length: 313
Sequence Mass (Da): 33646
Location Topology: Multi-pass membrane protein
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A0A522UQP5 | MIRSGNWRAGLHSSKGKSSPDRMNRKSIQMSVLLGTVAVIVVTGLMMILLVKFMLPGKLLGILEEKTIAQARLVASEIANPLLTEQFFDLRIRLNDLKRSDDSIAYVFVIDAHDKVVAHTFESGFPSELRTANKMASGAKQSVKQLTTGSEHYLDVALPVLNGGIGDLHIGTFLAPVKLGVNRIVAVIVWIIIVTSAAGGIIAVILARRELRPLRELGQAIESFGRGDVVQQVLPADDNNEIGQLITVFNKMAEDIRRSHEEREHTKNFLVSLINGVNERIMVVRPDYTVLMSNKAMAQGDTSDFCYALSHQRSSPCDEEGLVCPLREILRTRQSLTVTHTHTRADGSQYVEEIAASPFMDERGELLYVIEVCRDITEKQRLHEMQAALDKRIAQQQKEESISTLAGGIAHDFNNILMGILGNAEILGMTLESRENEKMLVNNIVSSSERMADLTNQLLAYAKGGMYQPGKLSMNDAVKMALTMTQTDKYRHIETSLLLEEDLWPVHADREQIKQVMINLLTNAFEAMEHSGGCLTVQTLNEPDRPSWECVSFKHRHPAGDYVHVIVSDTGPGIPQEALQRIFEPFFTTKFIGRGLGLAAAAGIIQNHQGCISVRAGAECGAFFDLYLPKYVNKNGV | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 637
Sequence Mass (Da): 70526
Location Topology: Multi-pass membrane protein
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A0A7V1N084 | MLVRRHAYRASRLRRCRYSISILRNSPVKKPPAEIIQAFPPEILEKLIVVRDRLVAWNQKFALTSVPDDEIFDLLIAPSAWLGSRYVIEEIGAIADFGSGPGVPGLAMALADTRNKYILIDSNQKKIGFIKHCLTVKDLYQANNVEARLLRVEPGVYKEKFDRVITRGAGSILSTIKLWKGKVKEGGAFDFFKGREVDAEIEELEAAIPGARVEELKAPGWFGHLRVLRVYFT | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 26279
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A0A3S1A0X3 | MNSSATVTSPYFKRNTRSVSSGKLSNVQIHEPIVKKSKIRSKAKSNCGSLSSSKVTAKSDNESSITEGTSSNAGVVKTSELAQKLEPGSHEDSCNSKSEVGKPIPLPNRESANDNHSTRKAASKRTCTRSALKSDNTSIDSSYLPKTESLEEGKEKLGRKHTQAKKSKRNHIKIEFDKDSKNSSNDQNESLALEKVKLEPVDSPANIIKEACLSPVKVSKNDVKLVKSSPVKGEDGYFHVYSSPEKSGSSSWEPPLWREQYANILQMRKFRDAPVDSMGCDVISDVLARPQDYRYQVLVSLMLSSQTKDQVTSAAMSRLRQHGCSVGNILATSDEQLGKLIYPVGFWKKKIDYIKRASAILKEKYNEDIPDTIQGLCSLPGVGPKMAHLAMKCAWHTITGIGVDTHVHRISNRLRWFRKPTKDPEETRKALEEWLPRELWSEVNHLLVGFGQTTCLPVYPKCNGCLNKSICPVGRTAKASPVKKELSQKIKEEDAAGCSEITPMT | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
EC: 3.2.2.-
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Subcellular Location: Nucleus
Sequence Length: 505
Sequence Mass (Da): 55851
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A0A1V4K7T1 | MAVLSENNACSLLATTFNLNTALFKGLVPTIALSYLPACLVVLNLVATSPPAVSLNADRCILQITGCVDVFAVLPNSTTQYIFTGNLTASTRANLTITKQKLIISLLLKRLQFSLLRSTLGFSDQISLVENFLSYALRSAVIPVINDKLGKGFPLPNLADTTLTGPVIKMNQGHLVISTDVHYKHEKGGDEDLHSCS | Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular Location: Secreted
Sequence Length: 197
Domain: The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues.
Sequence Mass (Da): 21189
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U3MBW5 | MAARLHCELDAARDVVLLRPLGVEPRGRPFPRPPRDPPRAATAAVPPFHRSDLPVRRLPACAFSSAGPCVLRFTCADLQRHMETPLNFVTWQGARQRGHFLRTLDYWDWYIKQSLMNQWEELGLGERLNTYVLGGCRHKLK | PTM: A fraction may be phosphorylated in insect cells and HepG2 cells, a human hepatoblastoma cell line. Phosphorylated in vitro by host protein kinase C or mitogen-activated protein kinase. N-acetylated in insect cells.
Function: Multifunctional protein that may modulate protein degradation pathways, apoptosis, transcription, signal transduction, cell cycle progress, and genetic stability by directly or indirectly interacting with host factors.
Subcellular Location: Host cytoplasm
Sequence Length: 141
Sequence Mass (Da): 16185
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A0A932KRJ9 | MKVRDLHPWTLTPRQAIALQEKLARKVVHRGGPRKVRFVAGVDVSTSRFSRTAWGGVVVLSFPGLSVVETRGGAAEARFPYIPGLLAFREVPLLLDLFARLRHAPDLLFVDGQGAAHPRGFGIACHLGLLLDIPTIGCAKSRLYGTHADPGFLRGRSAPLFDGKGKIIGRVVRTKDGTRPVYVSVGHKIGLAAAVRWTLACSGGYRIPEPTRQAHLFVTRLRRESGNRGRGEEEKRGIGESETVNR | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.
EC: 3.1.21.7
Subcellular Location: Cytoplasm
Sequence Length: 246
Sequence Mass (Da): 26866
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A0A3S1AZK0 | MAVTSKVYDRIWLAEYFHSFPHRNLNFKKVNSTFNPENEDYQESLVFLLLVPFTVSLVLWLVYIIYFIARCQKQTIHQRPKQRGSCCFSSFVFLFVLFAYCLIGFGLFQNEHVDDGVNGVKDALTNINNTISVAKEDLRNLEATADTVTGPLALTLEAAAGAIPDATFRRDVVDMIEQMRQQAAKAKGYMKVIDHIDTGQDYLTDVHDSVKEYEYYRWLGTVCVFVIYTSVFVCVLIGVMKHWKKMLIITAVFGALLAVLFWAFLGTYLGLSVGLGDFCMDPTQFFVKQLTGSESAGELLVYMKCEDTSQPYQQVITEAQNSLTQASNTLDAVAQYTRPYQLPGLFSLFEATVRLVSADILQAQRSLSSILTNVGTCTVLHNFYINGVNSACHKILESVSLLLLVAGLLALLSATMVFFVSCLWRTYDKRPTTQSMDADDTDPFLPRPPPYEHDYGSFARSSPAAWSDRGPLRAQHPSVNEEQVMFMRHQPTPLREDSPPPAMIALHKITPQIQVYSALYSGTHLQSHIAYTP | Function: Probable chloride channel.
Subcellular Location: Cell membrane
Sequence Length: 533
Sequence Mass (Da): 59953
Location Topology: Multi-pass membrane protein
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A0A1R4AAV5 | MLYQIKCLFYEHTFALALVLRFLLVAYGRIHDSLFKLKYTDIDYKVFTDAASFVYKGESPYLRETYRYTPLIAFLLIPNVTLCKDFGKILFSIFDILTGYFVHKILKFSKVPLSRSRILTAIYLFNPISIAISTRGNADCLICFVVMSAIYFHMKNRTILSSICLGFAIHLKLYPVIYLIPFFISLYKIPVTNNFVAKIRSNYSLYNILNSCMSLIWDSIYHLNINHVKFQVTLITTLTYLTLLFYNTYGYSFLYETYLYHFKRLDHRHNLSLYFYHIYHLVDKHQKLNFLVYPFFQLLCVVTCGLIVDDLILSMCLQTIMFIALNKVCTCQYFIWWISLLPLALAKAKLTQDDIKNLFYSGLLFILSLGLWLFFAYLLEFVGISTYIHLFASSIFFTYSQFNLAWKIYSICNNYSTVNNSTNNVEKGKLND | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 432
Sequence Mass (Da): 50723
Location Topology: Multi-pass membrane protein
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A0A660ZE44 | MRLAFFALFSYVLGSFPTAYLIGKWFKGIDIRKVGSKNMGTVNTFKNVGPIAGVIVAIVDVSKGLIPAILVGTLGFPKVAYPIAGAAVVAGHNWSIFMKFNGGQGLATAAGFLFALMPYEVLIAIALGAVGVVLLKMLGIGGWFKSPKNRFGFFTFSGLTCFIALRPHESFSRIAYLVIVVVLTIRQIECALKGWGYLRNTIVECLKGKKEAKKRDQ | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 217
Sequence Mass (Da): 23472
Location Topology: Multi-pass membrane protein
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A0A7M5VH26 | MVFKYTKAVCRRIPRSIVDGGIRMDLNKPLVDYERAVKQHEHMVQSLEKLGIKVTVLETDESTPDCVFVEDPAVIIGDTVLITNPGRESRKAETKIMKDYFKTNEPHLKIVEMESPATLDGGDVMFTGREIFVGQSRRTNEAGFLKVKETFPNYPVHAIPIPENTLHLISCMSPVDEDTILCGGSPDASAALKVVLEKATHMYSVVRTPEDDGANLVSANGTILWRSDLPATSNIVSKLNIPKVDLDGSELNKVDGSLTCCSLLYN | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
EC: 3.5.3.18
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Length: 266
Sequence Mass (Da): 29334
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A0A3M1G2Z4 | RERMGHIELAAPVAHIWFLRSVPSRIGTLLDMTIRQLERVLYFEAYVVIDPGDTPLQYKQLLTEEEYKQYRAEYGNAFKAGMGAEAIRELLKSLDLEALSKELKEKIAETSSQGQKRKYAKRLKIVDAFLRSGNKPEWMIMDVIPVLPPELRPLVHLDGGRFATSDLNDLYRRVINRNNRLKRLMALKAPSVIVRNEMRMLQEAVDALFDNSKRTKAMRMSQRRPLKSLSDMIKGKQGRFRQNLLGKRVDYSGRSVIVVGPHLKLHQCGLPKVMALELFKPFVYNKLEEKGYATTIKQAKRLVEEERPEVWEALEEVIKEHPVLLNRAPTLHRLGIQAFDPVLIEGKAIQIHPLVCVAYNADFDGDQMAVHVPLSVEAQIEARVLMMSVHNLLSPANGTPIVYPTQDMVLGLYYLTKERTGARGEGKVFSSPEEVRIAYDTGQVDEHARIKVRLNGKTIDTTVGRVIFSEIVPEEVPFEMCNKVMTKKELQKLIGYIYRHSGRRKTVE | 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: 508
Sequence Mass (Da): 58094
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B2L4S2 | IEKEDGLXGETIFMYLFLGGLGLLVXVGLHQL | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 32
Domain: Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.
Sequence Mass (Da): 3499
Location Topology: Single-pass type I membrane protein
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C5KBV9 | MPSRRSLKRSVANATTAVTQLGVSSGVDIGDIFSQFAGGSDGYAQPSGRNAAATVAVVYCGPDPSIGLLFRKFGKKDSLTRMKAYEELRGRVEDSDDANSSALVSILEPFAAHYMRSALLDPDWRCRAALHNIVGLLVSKLKRHAVRYLPDILPSLYLAGLYDTHIEVCRSASAALAVIFPHQNKREMAIYDKFRDSVREEIWWLLSSECTMQELDERFGCSGGGSKVDASDESEERYDRAVCAALAAVPKFAKVWNSDGSSVDPAIATMDFMKFALPPYRSSVRTAALSRCLLPLFSEDILRSKIEQEVDVEKILLLLSATQGDLTVGAATAQFVQVLAEESDLCGKLESSRKLRQRICTTVASGSKIIKSIPAIMRGIASSDDKVALKWSIEELTPSILRALGAPQPAPPPRVVYQVFSECLGIAAANSKFLEYKDEITDLFIELARHFINSGENRLPVGANQDLAYIDDQQEW | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 476
Sequence Mass (Da): 52184
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A0A1A9NPT8 | MKQFALIFCLLSSSLSCQAVDWEDPFEAGKLPKPVVSGSIATSGNDVCGAELALPAALSLADVVDRVLCRNPKSHEAWANARVQAAEVGVARAAFLPNVDATAGVEHNWSNGGSRGGLGGTSGTTGSTFGSSSSGNTDYNQLSAGVSLSYLLYDFGGRDAALENARQLFEAASATQDNVVQGLFFSAIQGYYQLNAAQAALESALEAERSSKASLDAATARYQVGVGTPADRLQAQTAYSQAVLDRIRAEGALRNAHGTLANLMGMDANQNYTLQPVADAPATGQFQANVGELIAEARRRRPDLAAAEAQIAAAEAGIASARAAGKPSISVSTDLAYLNRESSDSSRSGGIGLNVTIPLFTGFANTYRIRSATEQAEARKAARDQISLQIALDVWQAYQNLQTETQSVQSSADLVASAIQNADVALGRYKAGVGNIIDVITAQSALASARAQRIQARFNWDIARASLAYSMGRLDDVAADTQHPLSSESQQ | Function: CyaE is necessary for transport of calmodulin-sensitive adenylate cyclase-hemolysin (cyclolysin).
Subcellular Location: Cell outer membrane
Sequence Length: 491
Sequence Mass (Da): 51404
Location Topology: Peripheral membrane protein
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C5LRE3 | MAFENFAPTLARIFHSLQTWLMPFKLPLNEDVHMLGRTYPPPVVDAKCSTAPPPEDSPLYRAYVDIILFTYRCAFEPIEGCVGPTSVSDKGWGCAIRATQMLLAQAVKMAGKGEAGCLFSSDIILQMLTIASC | 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: 133
Sequence Mass (Da): 14574
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A0A1Y6K4D4 | MSSFPLLTLKILSPDGINFEKKGLKEVVVPLADGGSIGIKPGHATLIAETVRGAIRYRSELEQDSIEVLPGILDIRDNTVIILSAGKVSQQTSMVSEAEPMNFERLMQTLISKIQSEEESISLQS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 125
Sequence Mass (Da): 13596
Location Topology: Peripheral membrane protein
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A0A1Y6K6F6 | MKAIGAYLGVVWQILRKDIQVEWRGRQGLPVMLMFALMIVFLFNFALQLAPDVQAGLTSGLLWVSLAFASTLGLNRSISLERENNALDGLLLAPVDRSAIFFGKTLGNFCFTTLVGLLLLPVFSLFYGQNLLRAPLFLVMLLGLAAYTSLGTLLSALSIQARTRDVLLPVLLYPLALPILIAAVEASRGVLAEQPLSEMSSWIYLLLAGVLIFNAAGLLFFETILED | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 227
Sequence Mass (Da): 24791
Location Topology: Multi-pass membrane protein
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A0A3P7TVK0 | MTTFDLGGICSGMATCFRWREYYKVIEGDRRDVEHYTPHELALRITKLPFNVRLNRQVPPLLTEVDSQIHLKLRVVISEDEFTYKTDIWELLKWAATQYIVTFIVLNHLINSFLSCLFGNRLIEVVPCCKRL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: Cell projection
Sequence Length: 132
Sequence Mass (Da): 15535
Location Topology: Multi-pass membrane protein
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A0A0E3ZXS0 | MQALTGEIEIVSIATIFLLFITGAPIAFFMMHQRQYLRYLQDKEQIKNLYQRELLQSQLEIQNQTLQQVGSDLHDNVGQLLTVVVMRLNELEDEIMEPARQEGVQQTRELVRTVISDVRALSKTLDHDTVRRFGLLPSLTLELERIQRTKRILAELTTIGEPYSLGEQTEMVLLRMTQESLNNALKHAQARNLHVLTDFKSDSFALTISDDGRGFSVTEATTRQLEASGAGLSNLYRRAGLLGGTCVIHSTPGAGTRVEIRIPYPQIKQG | 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 transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 270
Sequence Mass (Da): 30432
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A0A533YM19 | GRGVRTVTGRIGVWLDTPLLDLEHGPGTLEKHFPAMVRQFKRYGLDITKDPVLVYPTLHYQNGGVQIDVNGESGVRHLFVAGEASGGLHGRNRLMGNSLLDLMVFGKRAGTTAAERAEAMRQGKLTLEHLARFRAEARKHSGALAVRSPMLFPDYVRKE | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Length: 159
Sequence Mass (Da): 17557
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A0A847WAJ0 | MYTLKNSRGLSVTMLEYGGIIQSILVPDRKGVLGDVVLGYDREEDYYNDMASLGATVGRYANRIGGASFKLNGTEYRLPNNEGQNCLHGGKGFQKRRWKGQATDSEVLLTIESPDGEEGFPGNLKVELRVRLSDENELILDYTAVSDKDTVINLTNHSYFNLACEGNILEQELMLNSDYYLEVDKALIPTGELIPVEGTDYDFRQLRPIKNGYYDNCYVLHSGEGVKAQAYDPKSGRGLKMYTDMPGVQLYCAAWLGGVKGKGGRVYKPYEGFCLETQFYPDSPNKPQFPSAVLKAGEVFKSRTVYQFYVK | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 311
Sequence Mass (Da): 34819
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K4J1L4 | IKIFSWLATLHGAQISYSPALLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWFPLFTGLSLNNSLLKIQFIIMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYTSWNIISSIGSTISFIGVLLLIYIIWESFISQRLVIFSNQMSTSIEWFQNTPPAEHSYSELPMLSNF | 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: 197
Sequence Mass (Da): 22245
Location Topology: Multi-pass membrane protein
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Q1G7J2 | MYFVLLVSIAFFVGVVGVVSNPSPCFGSLFLVLASGIGCVIVAEMGSSFPALILFMVYLGGMLVVFAYSVSLCVDLYPGVFVGRFVLVFIVFFVIVAQFELGNTYFGDGGFWLNCHFGSDFLGVPLLYTSGGYNLLFVGFGLLLTLIVVLELVRGISFVSQKTK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 164
Sequence Mass (Da): 17682
Location Topology: Multi-pass membrane protein
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A0A521QYC0 | MERLWRGASALALWGAWAGGAMILLAAVVVTVEVISRKLLAFAFSGSDEIAAYLFAVGTSWSLAHVLVTRGHVRIDVLYGALGPRMRAAFDLVAIAGLAILVLAIVDRAGEIFLDNLSGGNRSNTPLRIPLAWPQAPWFAGFVLFLAVTGLAFLRSLLALLRGDVGTVAATIGVPSQDEEVKGELGSLGIGTGSGAGR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 198
Sequence Mass (Da): 20638
Location Topology: Multi-pass membrane protein
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A0A7E4WAI5 | MISQEVYCVAPPSTTMPNSSQVAPESPGSATGGHRPPHVERQPTLNSLQKLRSLHRRTSLDVSHSEAVQEACKPLELSDDNLRTIMDRMEKSYQKGLSKEGAPTAAVKMLPSFVRSVPNGSENGNFLALDLGGTNFRVLLIRIDNTECEMTSKIFRVPESIMRGSGTKLFDHIAECLAKFIEEHDLVNKEKLPLGFTFSFPCQQYGLTCAKLVNWTKGFKCSGVEGNDVVQMLREACHRRGDIDIDVVAVLNDTTGTMMACAFKENSCNIGVICGTGSNACYMERLDRIPKIEGECNPAEDGLPAEMCVNTEWGGFGDDGALSEFFTEFDKILDEATINKGHQLFEKMVSGMYLGEIVRIILEHLAREGHLFGGDVDAIAQRGCFPTKFLSEIEGVYRFHPTFPAALDKKIDELLDENIEFQLMLSEDGSGRGAALVAAVATRMKQESAAHQLKMQNLKI | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4.
EC: 2.7.1.-
Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Length: 460
Sequence Mass (Da): 50681
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A0A0G0JQ56 | MDLRQLINQQPVIGLSPMDGITDEPFRLIQTEIAQPDVIFTEFVSAEGISRGGFKLYDQLLYKPQERPIIGQLFGKDPQSFYAGAIILAELGFDGIDINMGCPAKTVTANGSGAALIENPQLASEIIKSVANGINDWHTDKNALKKLKLKSKLDQVILRNQKYSQLKISSKIKPTLSVKTRLGINESIIDQWIPHLLKHPIDFLTIHGRTLKQGYAGQADWQQIGRVVRLAKGSGIKIWGNGDVQNRTQAQDYLKEFGVDGILIGRSAMGNPWVFSDHLPTVSEKYRCLLYHAQIYQATFPLRRFDSLRKNFLSYAVGLPNAKQLRQKLVHINNISDIIDIETDFLSSTDSQ | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 352
Sequence Mass (Da): 39413
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A0A7E5A0X7 | MPLVNGLLNAEMPVAPVPEIVEQEKLKVEKEQSLRSEVFKAVSSLTETVTEAELKEVLSSLDTNSWDSVVEERFLSGVCGWPLCGHAITVGKLRQFKFDRHQGKVYQNYSAKEKFCSLRCMDFSDFLRPQLSEVPLYLTGERNERSYNIYPSNEDLNAKTKSTATTANASSKSKDSERQVEFVPDKLIAQMKNLFIAENAESGSDSEGNDDEDDDGKKKKKRDPEDVKFLNEVRSFVTAKTATSLSTDPGICKTPNPKPAKKPIGPTPEEAEAKLAKLREKYGKGRNEKTKKPPLIVEPHNEASLKPKTPQRDAKKHAEAAIDLLSAWITPSTVNFLATDQHPRKPIENELLYEQFIASILDPRHATKIYDREQETDAVKLPLVDKVDQHFRRVDIVMNAVKNPWTAYISRLKIAANFTQCKNLIATFNLTRDNIVVEPKIADVLAIALFHLITHNNAELRALAEQDEAVQKHKAVMESFQLEVDFFSNRLKAIIEKISATEDDADVAEKEEAKSEEMNTSEA | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 523
Sequence Mass (Da): 58828
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A0A7E4ZSL7 | MADNLERLCTLRGFNKTNSTPVSPLEREFLDDFALDRQRNVTLGRDNHQYLVEKYLDPRERFAFDLSEGYETFDPKPEGEGINSILKYILLRAKDGDDLKTAVNGADIVCWRGLITKLATSFYEQGGVGWKVVVTKLGDTLFMSEVSTEAKIKSMAAETAYQKKCTYWGHKFETFIFAKKDQNPTPNEPVSTWEEKGVFFTVKLPGKADEPPIKLLCGAEIDGLDSDGNLVEVKTQVRDLFVGRFFPQKAMKWWIQSTLVGIQDIVVGFKLDSGIVNRLTKVQLNWLRNRLSKHWDPNVCLRTAGYIFNAIKTAYNEKIKPGQVLIVERQPDSLNIWFTIAPAESQEPILTEEFIARFGGGTEAGKVSSDDGPSEPKRTRF | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 381
Sequence Mass (Da): 43108
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A0A0P9D418 | AKAPLEATKRFREALNFLCAYSKDQGYNLKFALEPKPNEPRGDIYLATVGHALAFIQTLDDPAMVGVNPEVAHETMAGLNFLHGVAQAWDAGKLFHIDLNDQAPGRYDQDFRFGAVNLKSAFFLVKFLEDVGYTGSRHFDAHAYRTEGVEGVKDFARGCMRTYLILKEKAQQWNADSEIQALLADVQQAEGGAAVPAWGGGYSAAAASALKEHAFDRKALGARNLAYERLDQLTVDLLLGVR | Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose
EC: 5.3.1.5
Subcellular Location: Cytoplasm
Sequence Length: 242
Sequence Mass (Da): 26579
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A0A7E4W1I5 | MAPVTVDNKSKGKVLLNVATFGFSHMQYALTIGEWLIKDGFEVHLMVVKTKPNEAVSLPNCFPKRHIIEPTKTSAELFPLFGLFNNMISTVKESNRIFLANPVLEDIRKEKYDMLVGELLSPCQILKFRDMGIPKFIYISALPFDHLTADKMGLPSPSSYLPIMNECVLCGDEMGFWDRARNLYTALYLKLYLLPKFDESEKDQLREMGYDADAAFIRAKQSYDLRVFNSNILLDYPRPTVHNVLHVGGSMTKEPKALEEPVASVFAKPSNGVILISFGTLAESSNFPKTFXXXXGVRRPVLQCHTPTQKEGRSTCRIEDHHTGQAYLRL | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 330
Sequence Mass (Da): 37300
Location Topology: Single-pass membrane protein
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A0A851JNN7 | VMRRNPFGMDICCRKGSRSPFQELYNPTQVSLSNTAILHQIRRDQVTDTCRANSVSSRKRRVLTPNDLKHLVVDEDHEMIYCYVPKVACTNWKRVMMVLTGRGKYSDPMEIPANEAHVSSNLKTLNQYSIPEINHRLKNYMKFLFVREPFERLVSAYRNKFTQKYNTSFHKRYGTKIVRRQRKNATQEALRKGDDVKFEEFVAYLIDPHTQREEPFNEHWQTVYSLCHPCHIHYDLIGKYETLEEDSNYVLQLAGVGNYLKFPTYAKSTRTTDEMTTEFFQNISSLHQTQLYEVYKLDFLMFNYSVPSYLKLE | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 313
Sequence Mass (Da): 37080
Location Topology: Single-pass type II membrane protein
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B7XK28 | MGKIKGLISKIPKKKMIDVNKSLKDIYSSKPLVKLYQQFLFKKFKKYKLLYEESLVCDRNIEFTEMENTWGYKNIKILLKEKNDYIFELEQELIKLKKSISLSNDIDNVKKQKQTPTLVKVEFPEQLNTLFNKIKETEHLLCSQSEQFKNIEIKWEKKECEYKKTISELESKISHYQSIETKLIPYEIFINVEAMQKLELESINLKTVIGKLEQKIFFLEKEIKHQSQEKNDLLVAHKLLKDLLNTTENNQNTLQGDQYIIEEIKSMSQAFEKTQLENKKLRNQIEYLHKRNRDFEIKLVEIQTKAKITEKMLNLIEEHNRKYLALKETVELEKQNHQKKYGTIEHELETKTTQLQELNTTLKTYKQDLLNMQALLEKKTSEYFDQLNQIKILKDTIIENEKKIIEFKSIIKIYEESQNENTAIIDLQIQIQNLKEYVYCPLCKSNIKNHIINKCMHCFCEECLEHRLKTRNRNCPKCNQEYSKNDIKKIYL | 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: 492
Sequence Mass (Da): 58890
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B7XRD1 | MVVVDEFDRILEERSLRERFERMVEGYEGQRVYFSATLPNEPIKDIETIIRLESRIPEAIEHFFYYVPSESKENALLSVLDRSLKTIIFASTKYGVVLLLEILNDMGFGALGIYSGMDEDARKCHFDAFVEGRTMILIVTDVAARGLDIPHLDVSISYDLCDEKTFVHRVGRVREIGKNISFVTYSDVFHFFNIRETHLPEVEIGLMPQDLLTS | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 214
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 24634
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A0A8J3FCU9 | MQPALSGWTDDAAVLAWGLLFGSFLNVVAYRVPRGISVIWPPSACPHCGGRLAPRDLVPLFSYLWLRGRCRRCRAPISPLYPLGEALTALTFWLVWHRVGPTPELAVGWGLASLLVAATMADLRDRLIPNRIVLAAAMFLGGCRLLTHPLPLEAYALGAAAGFGVLYALNGLSLLVYRQEGIGGGDMKLMAAVGLAVGWKTVLLALLIGSLLGGAVAILLLATGKAHRRQYLPFGPMLAAGSLIAYLWGDALIAWYLGWSIS | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
EC: 2.1.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 262
Sequence Mass (Da): 27996
Location Topology: Multi-pass membrane protein
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A0A318XPH0 | MKLNNISIIGLGLIGGSLAKAFRQENKAFKIFAVDNCSEALKLAEADGVIDMGFNECCSEIWNSDIIFICTPIRKTMQFISQLADNVKDDCIITDVASTKHEICNYVDGLKNPPIFIGGHPMAGTEKSGYLNTFSHLFQNAYYVLTPSKTASKAALGTLEALLTGIGAIPIIVSPEKHDIVAGCISHVPHIIASALVTLAKNENDSELIKLLAAGGFRDITRIASSNPTMWENVVLSNSPVIVELLDKFKKIIDETADNISSFNNSEIYNFFDKAKSFRDSFSTTSVGLIPKSFELILDIEDEPGIIGKIATLLGDNEINLKNINVSNSREYEQGCLKITLSDQSNTDRAYKILSGYSYKVFRKE | Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Length: 365
Sequence Mass (Da): 39994
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A0A0K3AQN7 | MRLEYKVNPNNVAILKTPEEFYGTLCGLYRNAKYRIVASCLYIGIGDLEARLVKSICSSCQSRPDLTVDILLDFNRAQRRIKTKNGVKSSLTMLNPIVQASNRARISLFYNPSLNNILYNITKSPLSEAFGVMHLKVFIADEFVIISGANLSDEYFVSRQDRYYLIQNETLSDALHTLVGSIQNISFTYVNGSVQWDSNFSHPRHQALVYRRQIGYYLRETLVTCQEILNEGLSGPKSEQIIIKKGLGVGNKSCISLASPQIIPKNGLFCTILLSLQCPFAYPPITDDYDMVYELIQEALRTDHSLLISSPYLNFTNEYIESFGQFLLKDSDAKLRIINASPSANSFSKGSGVAKLIPDLFTIASATCFDKMYSVLKKIKNENEEEVESMDDFYTQINPDFYEEYHREHWTFHVKGVWLYKCPKNDTDICTPCTTVIGSSNLGMRSRYLDMELSACIQTNDPELCASIYEEIDTAFKYTKPVSLSELYSRCSMVTKILYKHIGLRQFL | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
EC: 2.7.8.5
Subcellular Location: Mitochondrion
Sequence Length: 508
Sequence Mass (Da): 57777
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A0A7M5ULL0 | MFRRKRLVFTFLPLLACLFVLWQMTTRSEDDPLMRRLNKGMAESLLLSENIQSFFPSKELFTANKNARNFKRRRKMRKRSIPSDEIFDKLYRDFLDCMLKSQRSLALFLNDQYQKQFRRDFRRRPSVESPILEPECKADLDLVIVVTTRPGNFLERTSIRYSWGRPGAYINRFLIKQKSFTYKTIFTLGRDQNNVIEDVVSKENSRYRDILRLDYQDTYENLAKKTILTLKWVNEACAPRFVLKTDDDCYVNLHNLSPWLLRLSPYVNYVGKKNDLMPVIRDPTHRNYVPFDLFSEEYYKVYCSGGGYILRGTVLGNITSKAKEIPEIINEDAYLGMITNALDIIPYDDERFLPFIFGDINLRKRHMCDWGDKFLMHGASPRRQLLMHWQKLAMVKYSVLCDL | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 403
Sequence Mass (Da): 47807
Location Topology: Single-pass type II membrane protein
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A0A7M5UXI6 | MVKYMMLAMTFMVGFIMTAFMTVNLNLFITGAGNSNPTKHVYIHNNKQNEERQNLSRHFEKFETYLKEIRKEMTSVKEGVYGMKAWEKIQIDRMELWKTLDEKSPPKADLRNPHIVLDDVKLDCSTRYDLIILISSHAAHFERREKIRRTWGNASMWITQNKKWKVVFVLGVIDNKNTMLKIKKESKTHGDVILEDVPESFYQLSFKVMVGLHWAFFALKFDFVLKGDDDVFVHVDRVLAKLDGDFRNEHYIGSVMSGQPVERKGRYGLTAEEHKNDRFDPYCSGGGFILSNVAISRMISLFDWLTPLKIDDAYIGHLVFRSGYKAKSVRGFYMWNNWCEYNEHLMVTHPVKQDRCLRFLEQRALIENGMMVDKQNLTSQLYGLPSSKKT | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 390
Sequence Mass (Da): 45585
Location Topology: Single-pass type II membrane protein
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A0A7M5V8R4 | SFFNRSDKNTKEIKMMKASILLALVAVCAAASWDYTDPNKLWSGDCSSGKKQSPINIVKANVEKDTNLYKLQAPNYNETRTGSTYTISNNGHGLVVTPVIDTTDLFDALPYMVSQHVAYELAQFHFHWGINDTQGSEHTVDGKEYPLEVHFVHYNRKYGNISAAVEKSDGLLVLGYLFEISSAENEDLKPIIDAVKDVLYLGNSTSIPFFPPQKLFPTEWYKFFHYEGSLTTPGCYESVKWFVDQAPLKVSSAQVAELRKMYEGSNQDKPMTHNFRPPQGLNGRKVKSIEVDKTYIYISPSKWDYESTEIGASAWPKLFPICVDNTETSRQSPINIVSANATHDDDLKPLKMTSYDSANQNMMQLSNNGHSITVSLGGSRFDSSVEHLGVEYELAQFHFHWSDQPLGGGSEHTHDGKQYFAEVHFVHFNKKYDSLGAAAAKSDGLLVWGHFIQAGNGSSNHTGYKTIFDAFENVKYKESTHNIDYVKPADLIPPMHNHYYTYPGSLTTPRCFESVTWIVNRDIIDISVDQAHQMLGVLENKNGDAEKKMYNNWRPVQDLNNRVVRKNFGADSTDPTDSASTTIQISFVSMLFALVCYLAL | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 600
Sequence Mass (Da): 67466
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A0A7M5VB59 | MSKVIVWEYETDMHGLFAPYEDNISNSIEDAYVKNPQDQNVDLGKIDHLLNNYEIEFNAMMQTNTKSGRQRQIQRQTYSTNSTIGSGVSWQWMTEKGWVVYDIEAIEAIERAYNQGSKTCDLGLLSFGLPNLVCIDKGYQKNKQSGFVRPIQRKVVDYKAVSGTRMKSSGTSSSTLTSAHAATNNLPSLNQPNSTTSHYQSLNGGAGSNTRPYSTQQPKSLPVSSGSSKSKSAGSISLGASSSTASHKSVGRRSSSDDKASHKKRKSNSAKPINPILDPFCSLSQPDDKNEQCAICLSELEDDNMTSLPENVLQLKICKHKFHESCLEALYKSSHNQQHCLRCPICKQIHGVLKGDQPPGRMTHRMDRHQDCEGYRGDGLIIITYNINHGIQGPEHPNPGHPYYTGNFPRTAYLPANKKGTKCLKLLEVAFERRLIFTVGTSATTGHDNCVTWTNIHHKTSSRNDGSGHGYPDPGYMDNLIEELKNVGVTDADIKP | 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: Cytoplasm
Sequence Length: 496
Sequence Mass (Da): 54860
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A0A840QNZ9 | MLRKHIYLIGFMGAGKTTIGKQLAQKFNLPFVDVDQFVEEREGISIADIFEREGEASFRLRETKSLQQLSDCSPSIISTGGGIVERQENIDEMKHHGQVIYLSASFATLYERVADDTTRPLTSAGKSTLHERFQMREAYYENAADLVVDTEGRSISETCDFIVEQLGNNS | 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
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 170
Sequence Mass (Da): 19103
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A0A520JU33 | MKHRIISSGEQAVFEAGIKLGALYHQFTGAPISPTSVDSMEKAIEESIALQPYVINITVKIDRDIINARLNKFGYCEIEGRMLDITLITRVGCSTATVRLSYDSKLEYPLMKILQIEEN | Pathway: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.
Function: Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD).
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 119
Sequence Mass (Da): 13335
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F3NTQ5 | MPSTRSGSPVTVRPSSTVRSYRGVAASRPGSERHPSGPRTLTPSLATSRGFTRCPRWRTPSSSSQSKTNTRSGSPTWWAARPTPRAAYMVANMSSTSAASSGPNAVTSAPGARSTGSPSRVRGRTRPRTPGRERCRMAVSVRFPLHPAGSAEDRSARAVPVRDSGVRMDLDRLTSITLPTGFRAARTREDRELMAGNSDPLSPRAKLAVTAGKAVAAASRAAGRGSGSVIGGKVALRLDPDLLARLAQNLDVVLVSATNGKTTTTRLIAEALRAAGPVVSNALGANMPAGITSALAGGSESKYGVIEVDEKYLAGVARDTDPKCIALLNLSRDQLDRAAETRMLAENWREGLAGSKAVIVANADDPLVVWAASSSPNVIWVAAGQMWKDDAWSCPSCGGVMQRPGDDWFCGECGFRRPVPSWALSGDHVLDPHGSAWPIHLQLPGRANKANAASSAAVAAVFGVPPQVALERMYQVQAVAGRYDVVQFQGRDLRLLLAKNPAGWLETFSLIDPPPTPVILSVNARGADGTDTSWLWDVDYTRLTGHPIFVLGDRKLDLAVRLEVANQSFQVCDSLDQAVQAAPPGRIEVIANYTAFQDLRRRVGN | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue.
EC: 6.3.5.13
Catalytic Activity: ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosphate
Sequence Length: 605
Sequence Mass (Da): 64259
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A0A522URB9 | MTPIHTPDALKVYLQPGELYVGEEPTKVVTVLGSCVSVTLFCKRLQIGAICHGVLPHCRKVKKCHELCRDSFKYVDCSLHYMIGRMRSSGCMDSELEVKLFGGADTLPSQKENTIGSMNVKMALEMIRQEHLRIIAADVGDSFGRKIIFLTHTGDVYLKRLKDAAALVQKPGVTFKTRGK | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 180
Sequence Mass (Da): 20013
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A0A7E4ZVD9 | MPEAIRTRRAGIADYFVTYDSAVLSLAAGFCFLTNVISSVFITLINRFIFMFHPDSRRYLENKYTITGIVIFHFVMYSFAFGIMISTMTSHDQTRFEATRDHPGAMDEYFKYNSFAYISGGELRYFLLRIGLCVAGALVLSLLISVTFFIVNVFIYKKTATVISKTSKFLIVNNHPTMDVSTDLSPILGESPIARLDQTRFKWLTPRKYPAFVKAIDSIGALSAKAQNLKKPLTSYDRILDNDDEQHVYIAWEQSPNGITSRILGFLKMSRRKLYLRDNAETQFIISPPCVLDFYVHESVQHQGYGTALFTAMLTSEDCEASKVAFDKPTDALMNFLATKFGLVNPVWQSTNFLVFEEFFSDLKPEHVPDQLLSARSQRESFNSQQASVNHNRVPYRTRDAASDIIHGAEPQPIKELPGADTPRGRKYYRDYGHSDIFG | Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
EC: 2.3.1.108
Catalytic Activity: acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-acetyl-L-lysyl-[alpha-tubulin]
Sequence Length: 439
Sequence Mass (Da): 49924
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A0A7V1HZR8 | MKQEITAKDVKIMAELQRTLPMTKRPFKSIAEKIGLAEKEVIEKTREYGQKQYYRRFGATLRHQKAGFKANGMGIWAVPAEEDRQGVGETLSAYHEVSHAYERPSFEDWPYHIFTMIHGESEDEVRRIAKGMSEQVGITDYDVLFSTREFKKTSMQYFDHWPLEEND | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 167
Sequence Mass (Da): 19557
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A0A3M1SMK6 | MISFLMMEIAGVVLAGGSNRRFPILKGLMEVEGERVIDRNLRLLRRFFSQVLISTNRPDAYFYTGAQLVGDLYPSIGPLVGICSSLITSEADALCVMACDMPFVRPELIDILIKSIGSGDAVIFEHSGRLHPLLGIYRASLIPLMEQLINQKDTEMIGFIRQIECRIIGEAEFPKLSGLEKSFVNINTPEEYRRYKGG | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 198
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 22116
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A0A533XNK4 | ADNLPVATGIALAFRLRGESRVVVTNTGDGGTSRGDFHEAMNFAAVRKLPVVFFCNNNQYSYSTPLHLQMAIKDVVERAKAYGMPGEIVDGNDVAAVYLAARRAIQKARAGEGPTFIECKTMRMHGHSEHDSAKYVPRELLEEWKKKDPILKAEQMLKQLGYADEATFREVGERVTKEVEAGVEFAEKSPLPEGPETLNGVFATDEEVKP | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2.4.4
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Length: 210
Sequence Mass (Da): 23169
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A0A433TXQ2 | MTTCSLSFLQDSQYEKTVRLGDFNGHSPTRAYRIWKNIEELYGATNLAVIQESNSLATILQKAHATLGNTGPTLPYAHLTLKTPVQALYKLTGGGRSGPGVEHWLQTQKSVGNDQFALKVNHNYARMDLVKDKIVEFKEFYDWAFTVADKRVADWPLMWGYTPTLVITALYLLAVYVGPRIMEHREPIKLKYTLVVYNFICVAINFNIFYELAVSSTMLGYSYSCQPVSYTYNPYEMRIAKAIWWFYFSKCVEMLDTVFFIMRKKNNQVSFLHVYHHATMFPIWYIGVKWVAGGQSFFGAMINSFIHVIMYSYYAIAALGPEYQKYLWWKRYLTRLQLIQFVTGIAHALQSLAFNGCGFPDWMHIALIIYAFTILLLFLNFYFHAYLKAQKNKGKKQDTNGSAVSNGHANGKSTISDSEPKKNK | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 424
Sequence Mass (Da): 48740
Location Topology: Multi-pass membrane protein
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A0A1B8P025 | MLALETARRAIGWPLPLVAAVALLYAFFGQYVPGEFGHPGLPAASLVGSLTIAEGGLWGKLTGVSVGVVAIFVIFGAVLNAGEAGKGFMNLAGLVAGRLTGGGAKVSVVSSALMGSISGSASANVASTGAITIPSMTRLGYPRALAAAVEAVASSGGQIMPPLMGAGAFVMVELTGTPYTDIMAAAMLPALLYFATVWMGINAYATRHDLRPVADEDRPALREVWMTGLFFAVPFAVLLERIFHAGNTPQYAASLAIFVGAALLWLDSRLVPSWRGLFARLAEAMVLAGRQVATIGAIIVCASLVIGVLAMTGLGVKVTSAILSLSGAPCGRRCCSPPWHAWCWAWRCPPPRPM | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 354
Sequence Mass (Da): 36596
Location Topology: Multi-pass membrane protein
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A0A522C3P1 | MDLLNDALKNIKAVNGEWHDIAQKHLDNLTKPQGSLGRLEEFARRLVAITESKKPILDKKVIFTFAGDHGVAEEGVSAFPKEVTRQMVFNFLNGGAGINVLSRHAGAEVIVVDIGVDFDFGNVSGL | Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Length: 126
Sequence Mass (Da): 13700
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A0A1J1GT14 | MQTKNEKNMKNKYKNDLNENNADINYNENNKNKYLDVEKKNMNNIKRKSKSVDEQYLKNEYLDLENRNISSIHRRSKYIDEENFKNECKNNERKSSCIYKKKKSLDEQNFKNDLLEDENKNNLKSEYKKRKSSKDIKYYKELKHLKELVNCKENNKLSNIIKLYGYNKGNSINKFKSGINSTINDTLLNSENFESKIRTFKIRALWTFILISLYFLILAAGHFYCSLLVLILVTIVYREIISLKSIENKDKRLPQIFYIRWYWFFLTIITLGIPWIIPKLKHQIWFFNYLLAYHSIIMFILAFIGFAWFILSLRKYSLKYQFSQIGIILLSSLFIVTQSLMHIANIYSGMIWFIVPVSSVIVNDIFAYVFGILFGKTRLIELSPKKTVEGYVGSSIITILWGIFITYILQRYKFFICPQAYISFMPFSTWNTIDCEENSIFQQNVYTLPKHVSSVLFINKIYYTKMIFHGLVLSLFAAFLAPFGGFFASGFKRALKIKDFGQYIPGHGGVTDRFDCQIFVGMFTYIYMKTFVKKKNKINSYDFLIESIQRLDNKDILRLFNQLKTILDNKEMLKNNTNNKKKDDFILKDDKCLDDKCVDDKCVDDKCLDDNYVEL | Pathway: Lipid metabolism.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 615
Sequence Mass (Da): 72809
Location Topology: Multi-pass membrane protein
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A0A1F6WZI3 | MAVITYLGPSGSTFSALAYYKLATLFKIPLGEGEEILAGNNEEVLPLIINHGGYGAIAMETEAEGRVDGPVNTFIKLLERYPTTADCPITVVGAIRMPLNFALMVRPGVRKSEVQILIAHPKSLGACKNLVQGLTLDGKANVVESDSNGKAAEDVATKPEFALAAALGPRVAAEKYGLEVLDEACEDMPAATTFFLLGPKSHSVKPGSRAVLVFRIKHECGALVDALLPFKEEGLSLRQIHSCYTQEGQYDFFIEIEIECDRHEPDKLSRAMKKASQHMTRHILFGSFPVS | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 291
Sequence Mass (Da): 31546
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I7IHF4 | MSHIFRELCYGTKLSLKRNNNYVYKEKIENDISGKSNSDLSSSSNGTDHVKSIGSSHFSDEPPSESYLKTQRITITNPQNSEIPAKWPLLLNFSHLNSLLTSLGNLDSKSNYKLPNSAPKWLFNNIRNNMNLSLTTPIQQIGIPAALLGSDILGISPTGSGKTLAYLIPLLIKLQAFNISNWNPQKLSIRSLIIAHTRELAHQIDKIILLLTGFGIKCSVLRKKNTELTRLDICISTPLTLIKLLRDGNINLNYCKILIMDEADKLFDLGFESQIDEILSFLPKENVQRLLFSATMHGKVRKLVNSIMIDYYKILVGTENAACTNIAQELICVTNEAGKLYTLRQMFLDGKLPPPVLVFISSREKVDKVFKQLANDGIQVAKLSAMLSKKERDATIQALRTGMIWILLCTDILARGVDFPQVSCVVNFDIPTKTQVYIHRVGRTGRAGRKGRALTFYTIADIPKLRPLTRIMKLSECELPDFILEF | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 486
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 54540
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W7HRW9 | MVAFSKLAAVVALAGSASAHTVFQRLWVNGVTPGQNVGIRVPLYDGPITDVSHNGIICNGAGINPMRQPPPGAIIDVPISSTLTMEWHHGTEGPNPLDSSDPVDPTHKGPIMVYLAKVDDALTPTVTGLKWFKIYEDGLDVATNTWAVDKFVAAKGYVDFKLPSCIPPGNYLLRGELLALHGASGTGGAQFYMSCAQINVIGGGNANPPTVNFPGAYSATDPGILVNIYYPPLSTYVIPGPRPFTCGGTQPTSSPTTLRTSTTSSRTTTTSSRTTTTTSSRTTTTSSSSSRTTTTPNWTGPTTCAQGTCKFSGDYYSQCLP | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 321
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 33699
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A0A144IVS7 | XLLLSSAFVEQGAGTGWTVYPPLXSIQAHSGGSVDMVIFSLHLAGISSILGAMXFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDR | 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: 104
Sequence Mass (Da): 11128
Location Topology: Multi-pass membrane protein
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A0A7E4VKY2 | MDKKCIENWSLQSYTYTVWTRGSPDDSRCHDGSEQRWNSHSRRPHCTTLDRDRYRDNTAAGCVTSNTHFESSATTLGKTSLTWHCTLRPDSPHPTPHLLLHVTMITDVHLGVMANVLGIAIFILIIAYHYITANQKKQ | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 138
Sequence Mass (Da): 15752
Location Topology: Single-pass type III membrane protein
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A0A3S0ZUG4 | MDFSLDINKLFREPITLIDNRLQPCRQHGIDRYGFQQLQKMLYEVVDKMGDASARAQGLHGPITTGKKLELANHHLYLMTDSNGNNGKGSALGILKVGRKKLFVYDNLKVQHELEPLCVLDFYVHESRQRMGCGRRLFDFMLSRENICAEHLAVDRPSPKFLSFLKKHYGLDHTIPQVNNFVIFENFFNNRKDSRKGRRNMESGGFIDRASPVQPNSGKRVAALGYNSHSQIQPHPYENGRQQHNLSVERSWTPSMARQSPSHLGAGEMMYSRHRTTPPQSGHGTPNRNRHGSRTPTQGFYPQPQQQQRQNHFDQQQQKGYQNYQQQQQQQDYNPYQQQQHHRQLNNTNKGTPDNSVSFYKQLNAQSSPSTYYNMGTSLGGYQHGGLGQGLNTLEHLPPKAPTPNQRQVQTVSLVSSPGLTNRGKVEGSVPPTPPDHSLHTNRNPSPSHGAAGRAGSGNHYTSPQSQPCNPVISAGSRTEPPLKLPAPSSASQQENIAHRPPSGKKSGSSLHRASQQPPLLPREGPPANYKDMLNMHQAYQGRNGRLNVPLGPSAGQGNSSAFARADAQNSSWTVGGVLREQRLNAPVSNRYYNPTRLW | Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
EC: 2.3.1.108
Catalytic Activity: acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-acetyl-L-lysyl-[alpha-tubulin]
Sequence Length: 599
Sequence Mass (Da): 67017
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A0A662RQ67 | MIAELAAKLSMNTCMLVGKRFQSESDTGWGIGALFIKSCTLRGYLIALTYSLLLASIPLISRTYPLRVFSLFSLFIGVSVAIIISYIGGTKFGTVSGDVIGASNEIARTAVLLIWSSQISGLST | 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: Membrane
Sequence Length: 124
Sequence Mass (Da): 13217
Location Topology: Multi-pass membrane protein
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C5LBY2 | MEIEELMGVLDKTLILALDFYEEPNAFHPSVVEAQAEFTRGLMAGVCTEGKKCVLVGHSMGGVVAAIAVSKSSEDIVKNVVSLVTVSTPLKTHPAMLDFGWSRVYREVGVGLDKVAVVSVTGGAADWQVPMEDTMVDGKARLQWAQMPTSDGVFAQGDHIAVMYSYEVLTYQVVPAIARALGWRTGAVVGDNDDLKAWMMSLDRPVRRHVPYDRKIEVDGSRVVEVKPLGLGKIRQVWNKGLIIDVERKSGAMLILRREGSYSRCPSVEVVDFNDKEYFSVEAPEVCDYCMRAGNNSAVVTVGAREMPLTSVHIRGDTWCVSPPISSDMKTILVPPGRGGFVVALSSPTVMKLKSRSAYEQYEMGVQLSGIGDAPYLACLVGGDHEVLSATSSSSGGRALMAPSRPLRARRARVMRGAVDTLVVVSTADDVGLVGSPGIHTFHRGHPHYGVPYTLLQYAVGDCDTVFDVNSLAHVGGYFCAGGAYRGVCSPWG | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 493
Sequence Mass (Da): 53162
Location Topology: Multi-pass membrane protein
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A0A1F6MG35 | MNKLLSSNRETLRRLLREQAPATGIDSHAVSRCGQGFVLIGILGTGEMIFQGWDEQAKAVGGLETAADPVASAIMAYRIRHGFPLNTFMVRKAPHDGKLVEGQIKPGDHVVIVDGVLITGDSVLRAIRAVKELGAKVLGVLVVVDREEGGREKLEDLGYTVVSLYTASEILAE | 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: 173
Sequence Mass (Da): 18603
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C5K834 | MHSSIPTLIVLVAVWSLVYSTIGAATATSATGQKQQQNQQTHLRTLVIVDEGEEDNDKRIYSQLYADLEDAGHHLTFAVYNDRALKLDDYGEWLYDNIIINANKINAFPVIEDRGRKYKSVDDEKREAASAGKPHKGISMFDLVDFVDKGNRSIVINVGRDFNGNGLRKLVNEFGFDVYDQDSTLVDHFHYEGNDHTTVWSRNFVAPRVTHFNPTAASKDKVLFGRGVGHSLSPSNDRVFPVIKSSPSAYSEDANMQMMREGAANTLSGLNLVSALQARNGARVLLVGSKDMCADKIFNKKGYDNRNVCKSMYTWAFNQRRVIRAVNMRHHKVGETEAPYMYTEGDDITFEIQLEELTMKGWVPYTARDIQLEYTMLDPHIRAFLLPDTSNNGLHTLTFKAPDVYGIFKFVVNYNRLGLNPLHIEEVAPLRNYKHNDYPRFLFCAYPYYASVFVAAFGLFVIAFLMM | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER).
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 467
Sequence Mass (Da): 52965
Location Topology: Single-pass type I membrane protein
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A0A7E4V453 | MASPSESAVKPASPAGTSANAAPAEEPEGYFVPKRHVFAIFDMAKWYRSEAYDKYLNFLHRINDSVIGVSNNANVEISDRVKSVIKLIDTLSSWTSDFPPVDMQEQRFGNKAYRLWHTRLTEQATDLIKDLLPEEHKAAVVELRPYLLDSFGNATRIDYGSGHEAAFLFFLLCCYETNVLIAPDDDQATVLRLFAHYLRFCRKLQTTYRMEPAGSRGVHAIDDYQFVPFIFGSAQLIGNKKRLIPDSYLNANTVEANRDDNLFFEAIQYINETKYGPFYEHSNQLYNISSVAKWEKVNSGMFKMYEGECLKKFPVAQHFVFGSILSIKQRPRFELEAAAVREAAIAHEKAEKEKAEQAEKEKHPITANVDHMNAIAEDVEASQ | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 383
Sequence Mass (Da): 43516
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A0A822J1H9 | MRIGVYICHCGSNIAGTIDVEEVRKHASMLKDVVIARDIQFACGDSGQEQVKKDILEEKLDRIVMAACSPRLHEVTFRRVLEQSGLNKHFLEMVNIREQGSWVHANKNALATQKAKELVAMGVARVALLSPLEKRTVPANKDVLVIGAGVAGIEAALALANMGVKVHLVEREPTIGGKMALMNEVFPNNDCSLCVLAPKMSDVQNHPNITLYTNSEITGVRGRAGNYLITGVTKPRYVDPRKCKGCIDICAKVCPIDVP | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.-.-
Sequence Length: 259
Sequence Mass (Da): 28237
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A0A5C0UF36 | MHLIPNLITVSRLVLGVLFFMLYPKHASPLILLGALSDVLDGFIARAFHMTSKLGEILDPIVDKIFWILVILKLYLNDIIPAWFISIILIRDMIFFAAFLYMLYKKIDRFKATWSGKLTAVVVGSTIFISLHETCPFCMYRLYVLCVGMIIVNILDYYKRVFR | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 163
Sequence Mass (Da): 18872
Location Topology: Multi-pass membrane protein
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A0A7X8QPP0 | FGLNNIIQLSLPVLMFLYPLAITLILLSLLTPFIHKQSDIYKWTTALTIIAAFFDLCKALPKPLLENEVIQQIIHFAHLYLPGFDYGFGWILPAFCGFFIGFISWSIRAKRHRFKYKTNE | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell membrane
Sequence Length: 120
Sequence Mass (Da): 13938
Location Topology: Multi-pass membrane protein
|
A0A2N1V1Y6 | MKIETKYSLLTFYKFVDIPDPKAEVAKLYRYTRDIGLRGRIFIGEEGINAQISGNIGQLHALLLYLDNSEYFKDIPDIDTKATRVDEHKFPKMIVRYKNEIVALGEIYSAADIEKVRSKMSVEEFKQVMDEENDDYLILDMRNNYEYKLGHFKKAIPAGTVSFRDLQSIIDHYKEQFNNKKIIMYCTGGIRCEKVAVYLDNQGFKDVKQLDGGVVKYVNKYNDGNWLGNLYTFDDRVSTDIGDENTNVIISECHYTGEKAKNYYNCRYGPCNAQIIAKPKEYRKHMGFCSEECSHKAKEDILIRDANFDPIQYKVLRSEIKQDNSKREQIVNGIEKHVTEWLAGVEFNHKTPVKEQIILPVLS | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
EC: 1.14.-.-
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Length: 363
Sequence Mass (Da): 42119
|
A0A5E4Q657 | MKGNVYLCEKRNKILTIVKDIELNIRIPAHDQEILLYYSQVLLGVNYIHSLDIIHRDIKAENILLTGKNGVIVKIGDFGISKMLASVKKTSTVIGTPYYLAPELCEVGLVKAITSGSVHPIDLNVYDRGIQDVIDSMLSVLPAKRPSIKQLMGRNILLFMSYTIMGSYKARDVDLYMGDNPTFNHQAGFNIERQQREMKSSEVDLVSAKIPPQHRDYCAHHLLEYQVCRYKNMPLLYKCAHEKHDYLNCEHQDYVVRMKEFERERRLRIRENRLVGVA | 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: 278
Sequence Mass (Da): 32051
Location Topology: Peripheral membrane protein
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G8DLS5 | TSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMXMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAXXXXTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRINNMSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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: 205
Sequence Mass (Da): 22173
Location Topology: Multi-pass membrane protein
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A0A7E4W837 | MAPARRRRVPVGERPPSVDEPTVSLESEAHRYERRLDRDAGNGRWDVLRGKLFHLLPSFDDAEPFADSFMLKLLSSVRIASAFYTVINDCDETYNYWEALHLMVYGRGFQTWEYSPVFAIRSWFYISLHYFPTLFLSFLLADSKVAVFYTLRVLLGFFHGAAEFMLTKAIAARLGNTISKFYFIITLTSVGTFYAGSAFLPSTFAMIMNMFALAFWLQERWFWSILSVATGALVGWPFAAVLGLPIVLEMVVLRRHQLFWTFVKYAAVAGSLVLSALYTVDSHYYGKHVIAPLNIVLYNVISGNGPELYGVEPFTYYLKNLVLNWSIALPFALVALPLALYVYIPSSIRPVVDEGKTKEIVERPTMTLAYWYRFMPIVLIGLAAFVWAFIFFSQPHKEERFLTPIYPHIAVLFAVALYALRTIIKDKFYVIPLSILLVFAVISTMRGAAVFRNYNGVVETHKQFYDHFVVFSEKKRDFTRFSDPIRVCTGKEWHRFPSSFFLPENSIDKHGNKRKVELEFIKSAFKGILPKHYPIAKRLSDVTRAIPDAMNDKNEEEPERYVPVETCDYILDFDDGTSGGPDEPNYAQRC | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 590
Sequence Mass (Da): 67727
Location Topology: Multi-pass membrane protein
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A0A851JY94 | RKAMLFLGFLVVFLGLALPGTQGRRIPRCEMVKILRQNGFEGFQGKTVADWMCLVKHESDYNTKAYNDNGSSRDYGIFQINSKYWCNDGRTAGSVNSCRISCSKFQDDNIADDIQCAKKIAREARGLTPW | Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
EC: 3.2.1.17
Subcellular Location: Secreted
Sequence Length: 130
Sequence Mass (Da): 14695
|
A0A3S1A2X3 | GANYVDSGALSGLGTKALVPGADCPDSATLIPSTVWNQHGGEPGRYDAALCMFEINNAYPLRRDLKYRKRNGFYGGMLDSVLTLRAILAVGSYDYVIDFIFHQNGVMETRLMSTGFIMGNVFRAVERQYGFRIEETLTANLHHHMFHLKVDLDVSGTSNRYETLNVEPMETKLCWDKSRDYAQTKFTTHLKRTEQEALYKYDFNHPKYHIVHNDARRNQWGEKRAFR | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 227
Sequence Mass (Da): 26082
|
A0A1G2P839 | MDKKEYKTESINLKTSKLPGSIVEIEGELPAAAVEKRRAAAIKMLGKNLNVPGFRAGHLPENIIIKTVGEMAVYEEAAEAALRDEVVAVLTNSEVNPITIPEISILKIAPGAPVAFKIKTNVMPVIVLPDYKKIALEKSKEPAEKIEVSDEEVNKVLDKVRNMRKAKTQNAENASDANTETARDETPAPELDDNFVKQLGDFKDVADFKNKIKSNLELDKTHKAKQKKRAAIAAELLKGEPFDAPEVLVGNELIRLTGRIKGDVQSMGMKFEDYLKEVEKTEEDIRKDLRPDAIQNAKLQLILNKIAAEEKISPDEHLVEHEARHLVEHYPGADLERAKDYVANLMRNEEVFKMLEGNPTSITSI | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 365
Sequence Mass (Da): 40644
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A0A3S1H0B8 | MSRFSGVFNWTSFYRRWAKISRESLTGRHSIADDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDYTDDDLYGSCHEDTDSDVPVAYGGFTEYPRPPSLKVSQSAGPNWFLENNRFSAWMSSNCHDYNRRQVLVNRLKILLGDDLDLYGTCGERKCPETICQDSLSNYKFFFTFENSNCRDYISEKFWAALQRRQVPVVMGGASVQDYVKIAPPRSFIHVDDFRGAEELVKYLRAVGRNETAYNQYLAWSLQADVYSELPARRKWLCELCAALHNTSRPGQVYTDIQGWVEDDICPVCRQEGGDVSTVSPKGRSHPRNPELGFEIFLHCSNLRGQQKC | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 352
Sequence Mass (Da): 40439
Location Topology: Single-pass type II membrane protein
|
A0A7X8JTK9 | MKKWYEENLDTDIIVSSRIRLARNYKKYPFSVRLSSSGAEKMIEETKRILLEGNTILSKEFEYIPVFGRNPIDKRALMESHVISPELVKKTIPCGVLLKNDESISIMINEEDHIRIQSVALGMNMSKAWDLADKIDNVLEESIEYAFNEKLGYLTSCPTNVGTGMRASYMMHLPALEWSGQLQNILYAIGKLGITVRGLYGEGTQAEGSLYQISNQITLGQSEKEIIENLNNIALQIAEQEKQIREQILKEKKEVLRDKIYRSYGTLRYARMLTTKEAMTLLSDIKMGFDMGILGEARPMISFYEFIMYVQPAILQKRVGTDLSSQDRDMQRAEFVRSQFER | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
EC: 2.7.14.1
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Length: 342
Sequence Mass (Da): 39270
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A0A1F9X0R1 | MLYNIYMLFIYNVITTCAFLLFIPFILVQLLTKKNRGQWLYRLGFLGPLPQGRYAWIHCASVGEVKVASLFISEFCKRMPQYKVILSVVTVSGFKVAVNSVPEATKVIFVPMDIAFLVKRAMKRVSPEMLILVETELWPNLIKYADKLNAKIITINGRISDRTFALYKVYRFIIKRIVRRVDLFLMREQYDYDRIIMLGADASKVNIMGNIKYDIIVSDNIKKYSVEKEYFGFSGADRIFVAGSIREGEEELVIDAYVDILKKHKDVKLIFSPRHLDRLELAEQLMDERNILHVRKTLNSEMKDFQCLLIDTYGELMKAYFVADIVFVGGSLIPLGGQNMIEPASLGKMVLFGPHTESFKEPAQMLVANYAAIRVQDAEQMKKTVIDYFSSPLKYEQYPVNAKNSIGKLQGVTARTVDKIEQFLKN | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 426
Sequence Mass (Da): 48939
|
C5KKG8 | MLSARESTSCTALQESLSAMKRDRDVWRDRAAKLETDHNSKIELLQQKLNESQRIGNSCSETMRERLMRSASEVGSLRAEVTKLKADCDASVAVNKAREERYKVMEEFFSTYQTDLDARQEECRNLHDAEKEATAKMLKMEEERREDVRKAERLEEERAVLKEQKQCRCLASNESLKSVCHKMASSLVKTQVDLEYKSAELARIQQLLDAEQRHSTKLKERMASLRKQVDTVVSGVDDHKSEFSRLSQAAKVQELQNARVVDNYWDALRQKNESLGIIQRLTEERDALQKHVQALESAHRQANGASMQENQLAQQSNNNSLAAMGQCRMQLETIVAEQKEKMESFKSTITMLKGVADKCQADCREKNKRILEVEKTNIRLTRQLEKARSLGSGHVVGVEGSGQSPSPGAVVDDKAQAMSIIEQEEVRAYRLKVKCSICQQNDKQVALQKCMHCFCRTCVNETMIQARNRKCPLCGQRFSESDVRTSLCITSKDDDSSLGEEDEHRRFLND | 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: 510
Sequence Mass (Da): 58123
|
A0A428PCY5 | MRDLDASKQAHDSSDVSAELLSDAKSVQNAGGVAVVLEAVASRAAAETTNTLEIPTIGIGSGSKCSGQLMLQTEMLGFQKSLFPEQVTTLISR | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
EC: 2.1.2.11
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Length: 93
Sequence Mass (Da): 9681
|
A0A1R4ABA0 | MSEIKWPVPQEQESLPQLDKEFVESTQNFISELSSSIVGYQTPTMDYCHDSNGIIALLNLLENVRSMTIQFEPIRDTLQRFGNKAFKHLINHLEQNVEALLAPIIKLSDNISESTLREDLRRYLIKCFGNKTRLDYGTGHELSFACLVKTLYQHGILGGDDRRDVVLFVFQRYFKLVRHLIELYNLEPAGSKGVWGLDDYQFLPFIFGAAQLQIQSSITPEQAIERPIIEMYKDAYIYIEALGYITACKRSVPFYECSPMLYDISGIKSWKKIYVGLLNMYRDHVLSRNIVINEINSGKD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 34609
|
A0A934AZK4 | MTSVKYWPGLCKIKISLLSAFSAATGAILSGAGLDVNFTIMVTGVFLLASGASALNQYQEREIDALMERTKSRPLPSGNISPREALYLSAALILSGTLLLLARSYFTAAALGVFAVVWYNGVYTDLKRLSAFAPVPGALVGAIPPAIGWSSAGGDLLDPMLPALCVFFFIWQVPHFLFLSLSNAKDYKKAGLPTISGIFSNGQIARINSVWILSMAVAGLALQLYIISSYHIFNSGLFAACLFLFIGGFTCISRHSTRIPFRTAFNRINMYMLLSMLILTGERLFLL | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Cell membrane
Sequence Length: 287
Sequence Mass (Da): 31058
Location Topology: Multi-pass membrane protein
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B2L4D3 | ELNEYLEQFVGDQEAWHELGLYISSVHIASNPKASAKMKKDNVKYATWAASQIKKAYQLAGRTMTDTQTSLKAVEDMLETLQITQS | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 86
Sequence Mass (Da): 9694
Location Topology: Peripheral membrane protein
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A0A7E4URR3 | MFGIPSVFGGFKKLNSDPLDDPSDRLSSAVSVALLVSFCALASGRIYVGDPIECLVDRSATSSWSRYYMQYCFVQPHLYLRSGTGLTAEATFSRPQVAFYPWIPYAMFLQACIFYLPKLLWDFFNCRLGIDLKSVLEEAKQLADKPIADRRDQVRELAAYMTAALDFVFDGHRVSWFLLSSPTAVCYILKKWLYVVLALAQFRWLIGFIGSGNLGWGFSAAMAYSNYGFHQASTVLPITTTCRIPTTIDGDARSTALPCILGMNVVFERLYIVLYFWLIAIIAISLTSAIRATMLFVFPAFRFTAINARLKLSRHSYLGQQNVISFLHSVLRADGLLAVSLIQESYGTALAEQLLRELWVMSESGRVRPRQPKLYDSLPTDLKLPSFSQSPNDLPKVPLMTSFTYDTPLKPHFK | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 414
Sequence Mass (Da): 46581
Location Topology: Multi-pass membrane protein
|
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