ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
B4L3S7 | MEQNEPQNCAETLRSMRQQIALANAQQMLGKITVNCFRKCIDRPGTSLARAEERCLVQCMDRFMDSLKVVSLTYSKRLMRETK | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
A0A6P6LY19 | MNSVKNVRSNPAHSTQKRKCAFGLGGTGDWRHVRARAIRRKGYAQCERERMEAAEQQRSSSDGAPARGAGVPGSGGGAGPGGGAEGERDRDRATFECNICLDTARDAVISLCGHLFCWPCLHQWLETRPSRQQCPVCKAGISRDKVIPLYGRGSTSQEDPRLKTPPRPQGQRTEPESRGPFQGFGDAGFHMSFGVGAFPFGFFTTVFNTNDNFHRRDPHYGGDHQADGNGNNWQDSLFLFLAVIFFFWLLSV | Pathway: Protein modification; protein ubiquitination.
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: 252
Sequence Mass (Da): 27751
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A0A3L8Q3U5 | MRAFGAHAATDVTGFGLLGHARALAAQQRLDVAFVIHNLPVLAGMAAVSRAGGGRGGLLQGTAPETS | Function: Synthesizes selenophosphate from selenide and ATP.
EC: 2.7.9.3
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Length: 67
Sequence Mass (Da): 6682
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A0A2I0PK47 | MKICSKNSVIIFISIIFILLVGIFIRLDSVGLTGVPLENKGYYQDSNGQNYMYDMDSYYNYRLTENLLKTGHIYESINNNQTIDTLSYYPPGVPFDYPPLIAYISVLFYKLINYFISVSLITVCFWIPSIIGPLSGVIAFLFIYRIKRDSIGILGGLVAGLLIVLSPFYFMRTVPGFFDTDMFIILFSLLTVWLLFESIRSSGPLKQIILILCTSLSMLLFSLAWAGWQLLYFIIFAAAMVYYLSTQFPKILVNQIHASEIDNSEIKYNKKKKTKNQNINKWNSKLLDFSNIEGKNRIKTGILIFVFLVVSIILIILING... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
C7Z3E2 | MAADPDDPYSCSEAKPCSNGACCAKTGVCGYGPDSCGTNDESPNDKCWSNCDAHAECGRYAEEPGKTCPLNVCCSRHGFCGMTSEYCDESDNEDESCQSNCSQPGSGGSGGDVQKRVIGYYEAWNWKKKCIGMSMEDIPVNSLTHIYYSFAYIKPETYEIVPMQDEKDGTLTTETFSQFTSLKRKNPSLKAVVALGGWTFNDNNTIWQPVFSDLSSTKEKRATFLDELLKFMNRYGFDGVDIDWEYPGAPDRGGKPDDGENLTKLFKEMRTTFDKTPGKRKEISFTAPTSYWYMRHFDITGSAEAVDYVNVMSYDLHGIW... | 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: 570
Sequence Mass (Da): 63000
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A0A8J5P7K2 | MWLIHWALGVAFYAVISLAVWIEGSSAILSCWDSPNQSLEIPRRLLSAVLFYFVAYFKQNQCHRHLASLKKYTLPTEGWFKYLVCPHYTAECILYLAIAWIAAPPGELFNKSILTAVAFVAVNLGATAKDTKAWYENKFGSDKVADRWIMIPPVY | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-gly... |
A0A7Y7IR19 | MKIDQSMIDVGPVDFLRSDHTGSFEGLPVANIGDAMDRMGMCDSGLHAMWSGAACVGTAFPVTVRSGDNAGLHVALEHVRPGDVLVVNGGGDLSRALLGDLLATKLRTLGVVGAVIDGCIRDRSTLEQMRFPVWARGANPSGPYKNGPARLAREAAVGGVVVRPGDIIAADDDGVAVIPADSAADVYRLTLEVMAHEAELSREFSRPIGR | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A940I9N3 | MKSTPSLQGKTVVITRAKKQSKEMKQLIEQHGGTAIEMPMIDFRLRKEGYEISSLFDYDWIFFTSVNSVRFFWELLQQHEIPISSLRCRFGAVGEKTKRALEKKGVSVDFFPTKFTGEEFGTQFVHSAFTGKRILIPKGQLASDVLAATLRKFDYHVDEWIIYETFLPTESNHLMDPSVLKDVDVITFTSPSTVRHFFQLLEQQHLLHFVKKWLIACIGPVTASEVKNHGYDVHICPETYTVPDLIKSINEWYKMRRN | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A0H3LW71 | MLLPILADLHDSNRNWITFLCSCAMTTMLATLILLATKGATCRFSARLGFMLTVCLWLTGSVVGALPLYLSHLPISLAGAIFESVSGITTTGSTVITGLDNLSRSILLWRSIICWIGGIGFIGLALLLLPSLRVGGVRLFHMESSDKSEKILPRINQIANGIIIAYVGLTLACMLSYFASGMSLFDAINHAMSTIATAGFSTHDASFGYFSDKPAILIISTIFMLLSALPFVLYVKLVLPGHSKRFIDPQVIVFLNIVFLFSFALAAWLRFHDHRAFHWIFLDVIFHLSSIISTTGYSAEDYQLWGPFALGIFFIVSFTG... | Function: Low-affinity potassium transport system. Interacts with Trk system potassium uptake protein TrkA.
Subcellular Location: Cell inner membrane
Sequence Length: 464
Sequence Mass (Da): 50719
Location Topology: Multi-pass membrane protein
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G3I857 | MSLLVLVLSWGSLGLEAATAVGLSDFCSNPDAYVLNLTQEETGLSSDFIKYYFLCNQEVSNPFQQRLTLSQPALASIHSQLQGLEREAVPQFPALWDAGPSPGKGPVGWVR | Function: Probable chloride channel.
Subcellular Location: Cell membrane
Sequence Length: 111
Sequence Mass (Da): 12041
Location Topology: Multi-pass membrane protein
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A0A2C5YW20 | MPFHDARSAPSPYRPTPASAVSMAFPFSPAQSSADVKSPGQRHQYPPGPYQHHHLQQQPPQPHPHPPLVPPSLPQQATQRPQHHPPPVFAHQQSPQQQQYLHHHQHQRSLSTHSSASASASASAPTPTPTSAHPSGLSLPGSSPATASRPSPDFGRQHQPSVAAPSSAWSAAGSFARPASPPQPPRTAQQSTTPDSHYPQSLVAAAGQRVSSAHGQHDSSPVSDVPGRPISRPDREHSVSVSPHTRVASLSSNPPSELERKSSRIVMTTDGAVTPAKRKLQDRSLSPHELEHQREPRQPPAETNGGHKSVSPAIAPRKRR... | Function: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Catalytic Activity: a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate
EC: 3.6.1.74
Subcellular Location: Nucleus
Sequence Length: 716
Seque... |
A0A1Y1S6M3 | MENKKTFVVVGMAGCGKTTFVQRLTSWIMQHESKEQANPIKSIELVNLDPAVLNTKVPPTIDIRDYVDYKDILIQNNLGSNGAISACLNLFMLKGIKLDTKKYTIIDTPGQIESFIYSAPGDIVFSSLTSQLTILFLIDLSVDSLYSVVSNLIFAGSLASKYNTIIVFTKNDESKIHAISDLFDYDKMRNVTATDDLSEIGTLVTYFEEFYKDIEYVSISSVTGDGKHELIKKLKLF | Function: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import.
EC: 3.6.5.-
Subcellular Location: Cytoplasm
Sequence Length: 237
Sequence Mass (Da): 26481
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A0A1Y1S5Q0 | MNIRTKLTCQKLFAEFLCSLIFGFAVYSAVLNTKASENPAPSTAVGLTVAFSSIALIYTFCDHCASHFNPAITIAALVTGKLDLALGIGYVIAQLLGFFIASLLAVLCFPYGYSKTLDLITPGAVVYSAVLNTKASENPAPSTAVGLTVAFSSIALIYTFCDHCASHFNPAITIAALVTGKLDLALGIGYVIAQLLGFFIASLLAVLCFPYGYSKTLDLITPGAVSDEISDHNIFWAEFILSFILVFVAFEVGINAVREPGVTLFVGETQIDRSKFAPLTIGSTLGFLAFLASSTSGGAFNPGIVFGPSIAGGNFEYFWQ... | Function: Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance.
Subcellular Location: Cell membrane
Sequence Length: 342
Sequence Mass (Da): 36140
Location Topology: Multi-pass membrane protein
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A0A7C9HJN3 | MGLRVRLRDRHRLPVLRHRADARTGLPRRAEGGRHGGCGIHLGLAGRHVRHDGDRPVPARSALVRRDDPGAHPGILVRHAGRDDRGLLHELPRELAAHPRRGQGADVTATRRAGQAPPATPTGAAAIGALGVVFGDIGTSPLYALSAALAPAGSIDSTTVYGVTSMVVWSITLVVTVLYVGVLMRFDNDGEGGLLALLAQLRRAHPTATVRTLATVVAILGAAMFLGDSMITPAISVLSAVEGLTTFDPDLGAVVVPITVAILVGLFVVQRFGAARIGRVFGPIMLAWFGLLAVLGFVAIAGRPDVLVALSPHWIVLLVA... | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 732
Sequence Mass (Da): 76707
Location Topology: Multi-pass membrane protein
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A0A6F8PY34 | MEFSWTTFILEIINFVLLMWILKHFLYRPVLNALQKRRETVDNTLQEALDKSAQAEELKTQYQQRLQAWEKEKNQLRQDLQQDLDSMRSEQQQRLREELQAQQEKFEINQQQTQEQTQQHYQSVAHRQGAEFAAKLLRTLSGVETEERLFDALMEQLDALDSQQIKNLQKTCDSDSGQVDVCSAYPLSEKNRQALQTKLEQLCPQPLKIHYQQDPELISGVRIHLGVWSLRMNLLDELNRFMELNRDRLNHQ | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 252
Sequence Mass (Da): 29939
Location Topology: Single-pass membr... |
A0A7Y2DT84 | MTRQIVITGLMGVGKTTTATAVAKRLSLPYRDSDDDIHRLLGRSGRQVAEQLGVDELHRLEAAVLLGALASPQQQVITAAASTVEDPLCRATMGHTAVTVVLTAPLDTVIERMRDGRHRRSIDRAELERIASRRDPLFNEVADMIVAVDRPADEVADDIVLFLQRD | 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... |
A0A7L2CG34 | MGAALQVTAFGLALLSTLFLLLATCTDCWMVNADDSLEVSHKCRGLWRECVTNMQDGVRTCDQYDSILAEHPVKIVVTRTLMITADLLAGLALATLLLGLDCITFLREDPCVKLKMCFGAGVTLGAGSILGLTGSLWYAVDVYVERAMLVSHNVFLGVHYDFGWSCWLGMAGSSGCFVASVLLTCCLY | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 188
Sequence Mass (Da): 20305
Location Topology: Multi-pass membrane protein
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A0A932R6W6 | MAWILHEQGHSVSGSDCRETARTRELRAAGISVHHGHDAAYLRDSEAVIYSSAIESENVELKMARELNLNILHRQQLLAMIYNSHSSIGIAGTHGKTTTSSMISLLLRRAGYDPTFLVGASSNSLGHYARSGKGRWLVSEVDESDGHFVHLHSDIAVITNVGEDHLNHYGSSEALLEGFKTFIKQSRRAVLFADDPHYELLASSARQSLSFGLKNQADLMAKNIRQDQMNTRADLVFQGASLGEIHLPAPGRHNIMNALTAMLAAHMAGIDFRKSMNILKSFSLPSRRFQILEDNGLVVVDDYAHLPEQVELNLEAIRQG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 433
Sequence Mass (Da): 48142
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S0G3F9 | MNLSYLFKNLPIRYKILCVFSVTFVVIMGLSSLTIYSIVKQNVEKNIETMLENATAAMVNNVRTAASVSIRNYLRATAEKNLEIVTHLYQRQADGSLTLEQAQKQAADIMLAQKIGTHGYICILDGTGRVVRHPKKLLEGLDISDHAFVQEMVAQKKGYIEYDWQNPDDDFPQPKALYLEYFAPWDWMITVSSYRKKFSELMEISDFEKSIQGQRFGKTGYACVLDAENNLIIPPAHQHANIFSNPEHADRFFKTISEQKDGIHTVSWPEKSGNFAGKNRIFFNHIPEYQWTVASAIHMDDFFSPLTTIKNFIMIVGLTS... | 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... |
F4N1N4 | MKNTYNLRSIAAKAISQVLDQGQSLSTVLPGLQKSISDKDRALLQELCFGTLRVLPQLEWCIQQLMARPMTGKQRVFHYLIMVGLYQLIYTRIPPHAALAETVEGATALKRPQLKGLINGVLRQFQRQQVELLERAANNDSHYLHPSWLLARIKLAYPDQWQQILDANNQKPPMWLRVSRLHHSRIEYLGLLKQANIEALPHDFYPDAVRLITPCAVSDLPGFELGWVTVQDASAQGCVDLLDPQEGEQILDLCAAPGGKTTHILEAAPKAHVLAVDIDEQRLSRVKETYNA | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 292
Sequence Mass (Da): 32849... |
A0A834J834 | MKLLERVIKETLLLYAVVAIIARKVTQDAEGQKAGVHKKVLFNYNFHRNEKHWAQPLVLDPDRFLPGRHSSSNFFPFSCGCRNCIGQKLEMIIIEMTIIIAILIRKFIIKMDKPIEIAEIGVELNLSLKLTESIKLKFEKEGNVAENHANDMIFCETSKQQRKSKFHDTLSRSEEFQMDFYHTNTLQKINIDPEENDSSDILVVVSSLPPETNKKTKKPHR | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 221
Sequence Mass (Da): 25536
Location Topology: Peripheral membrane protein
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A0A416D583 | MYVKSRGENLAGVLVDKGIRARFIGDDANKANFNKGETVIIKGELNKGFEYPEINFVLVSDREIFETKKSRSRRKVENANRIKNYTDISVGDYVVHQTHGIGQYMGTKKMVVGGITKDYLKIQYQGTDSLYIPIDQLNLLYKYVGNTDKKLKLNKLGSNEWNKTKQRVKQSTEELAKKLVALYAERERAKGFAYSEDTPWQRDFEDTFPYQETDDQLRSIEEVKGDMESQKPMDRLLCGDVGFGKTEIALRAAFKAVGDSKQVAYLCPTTILAMQHYETFLKRMESFPIKVEMLSRFRTASEQKRILKKLKTGEIDIIIG... | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
EC: 3.6.4.-
Subcellular Location: Cytoplasm
Sequence ... |
A0A3M7QQJ0 | MANQQKTIFICALPGTGHLNPILRVSAELVGRKHRVIVFCDDMFQKIIEKSGAEYRPYSVKFTLPSQINHQDVDDTHGMLLFFFRSVQVAYEDVGYMLEQVNTERPDLIIYDQFSFTTKYLFKLMEKNYQDKASHLRPPKSICFYTCFAMRPSIYPDHCHSKRLLVTDYWSNSLSYSVFNEQVKLCHKYKIEAENPFELAYNYTTNINIISCFPELQPESEKFDSSFKFVGCCLSNESQNFETSDKQLGDILQSFEPINPNYQMSKFSKQLVYASLGTLFNHKVCVFEKIIESVKILNNSSVEIMVLISCGKTSLEYLAE... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 451
Sequence Mass (Da): 51617
Location Topology: Single-pass membrane protein
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A0A3M7QJ11 | MFTLKAENIKADSAVIHFKQWNVKINSVLSVGSVIFTYEYEQDGKTKTEKYKSTLNGITVKEIFSFTSGQLINTETDLLTYEKCTHPVMSNDMCAVCGEDLRIKEIQKTKKITPKNESFRMVSIDPTLKVDQSVAHDIAKKDLIHLVKNRRLVLLADLDHTLIHTTHEHVNPDIKDVHHYELQRNFWYHTKFRPGCLHFLQEMSKLYELHIVTFGERNYAHKIASLMDPERRFFHDRILSRNEIFNRISKSDNLRSLFPRGDLMVCIIDDREEVWNYARNLICVQPYVFFKNTGDINDPALFNVAKKRKIEESGTSSEQT... | Function: This promotes the activity of RNA polymerase II.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 658
Sequence Mass (Da): 76256
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E3S314 | MSTIPLHTVALLPLLSGLRNAHAFITKASLHCTTTSTSPESLLTASLHPTMKDLRYQVYRFTDAAKFLPIRLNPALADRELKIPDVEQSFEELLERIQKTIRHLEEYKASDFDGVGSEDVIEVKFPGGKGFRMGVADHVARYSHPNFWFHVTTTYAILRMKGVDVGKLDFLNGAGEIEILDMEASLKDVTRIARLVADNTVSIGSSLAHVHVPGRREPEGDELKDGQVEIGMGIHNEAGSERKSTDLPGLVKTMLSHCLDVADQDRSFSRITDKDEVVLLVNNLGGVSPLELSGITHEVVEQLAGSFKIKPVRILAGTFM... | Pathway: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 2/2.
Function: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Catalytic Activity: ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+)
Sequence Length: 598
Sequence M... |
A0A0E9NMF1 | MADLDKYLLLTKFYAQDAFSSIDWSQPSLYISVASILFNPIWWNVVARMEYHNKTLTKLAGGNAKYGCYGLAVAIFSLGIIRDFLYERALNAQPLYAPLAAYPYTKPLAVALFLTGNILVLTSMYALGVTGTYLGDYFGILMDARVTGFPFNVTDNPMYWGSAMSFLGTALWYGRPAGVVLSVVVVVMYKIALAFEEPFTGWCEGPVSFLPLGSIVGALLLQSTWRTDVAASSGVAGERRNSTFCLLWIIIFGSFTGSSGVIHLFNKGSSCFFDTIPNIRKEIYDTCIATHFITSQTTHSMMNENDRISGTAQVTKLHVK... | Pathway: Lipid metabolism.
Function: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
Catalytic Activity: 1,2-diacy... |
A0A0E9NLI4 | MDPSAPYESDEKRISQNDSLCNVDRATARAELSNIQAGAESPNGSDARRPSLRKFHTAAHGMRSRSPQLGPHYGTNRISDGMDLEEVPMGITRQAIDLASYKFPDHRLRRVMADETKVPLVIVACGSFSPITYLHLRIFEMALDNIRERTDFEVMGGYYSPVSDHYMKAGLAPASYRVRMCELASERTSSWLMVDAWESLQDSYTRTAVVLDHFHREINEVRGGVRTKSGKHRKVKVMLLAGGDLIETMAEPNVWADADLHHILGKHGALVVERTGADVWKFLLSHDILYEHRKNIIVIKQLIYNDISSTKVRLFLRRGM... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
EC: 2.7.7.1
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 401
Sequence Mass (Da): 45683
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A0A672V0L2 | MASSAVQLLGFSLSLLGLIGTLIATILPHWWRTAHVGTNIITAVAYMKGLWMECVWHSTGIYQCQVHHSQLALPRDLQVARAMMVISCVLSALACVIAVIGMKCTQCAKGTSAKASIAVFGGIVFILAGLVCLVPVSWTTNDVVTDFYNPMLPSGMKYEIGQALYLGFVSASLTILGGALLCTSSQCRGNETPYQTQPSSVRRTAPSYRPPTVYKGNHASSLTSASHSGYRLNDYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 236
Sequence Mass (Da): 25295
Location Topology: Multi-pass membrane protein
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A0A160T487 | MHRFFILPSQIGHQTVRFDADQAHQMRRVLRLRPGDRVLALDGRGRQYEVVLEEVSNARATGRVATQSEAGGEPGARLTLFQSLLPRDKFEWVLQKGTEVGVSTFAPVITRRSLVRGDDVTAEKMTRWERIIREAAEQCGRGLLPRLLPPAPFSAAIVAAAALDRAVIAWEGESRRALGEALSQSGERPEVGLFIGPEGGFEMEEIEEAAAQGIVAVTLGRRILRTETAAVVGAALLLYELGEL | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A161KD71 | MTNPPDPFASGTFFAHIFHASPVAMIVTTPDDDRYVDVNDAYAALVGIPRLALRGQRNVHLLQPEGATATGARQLVEEPLCLRAADGRLHDVVASTQFEEWDGRPYRITLVQDLTDYNRTGAALRSSEARFRLFFDSIPLPIFVFDLETWRILDVNPIAVELYGYSRDELLTMTMLDIRPPETVASYIATIRALPADSRFVDVWRHRKKDGGLMDMELISYAFDLDGRAVRLHILRDVSEKLALQEALRRNQERLKIVADVTTDVIWEYDMARGAVDTVGLFELFGYAGDSSRPWEWWFEQVHPDERDAVEKATRDALAG... | 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... |
A0A2N7X9H1 | MSSRADVIWAVVPVKDFAMAKSRLAATLSSAARAELARAMSEDVISALQSAKVAEHVCVLSDSPAVQQLAARNGAVWLDERTVAGAPGLNAAIAGAARVAAARGATALLVVHADLPLLTASALTHVLDTWSNLSGKGRVVLARSRDGGTNICLAERPDAFTYHYGTNSHALHVDECVRQHRVVANVEMPATALDVDTVDDLEILRAAARTNACSSHTAAFLAKIATPVFGNEIEAAP | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor co... |
A7ST50 | FFLEEMATSASRRLEDEVTCSICIEHFNDPRVLPCLHSFCRHCLEELAVHSEGRGKLVCPLCKAEFQISPADVLSLKVNFMINSIISVLPLLTSEDSKKKTVCQMCDSGEPAQGRCNECDHFVCEQCISAHKRLRPLQHHTILSLDEIKSGKLLAMSKTSYCTKHKGKKLKLFCESCKEVICRDCTVVDHKNHDYRFTSDVIAREKEEILERAKKVTSKLTDIEQAMALVEKAQQHLDENKRAARRDLDQFIDKQIGALEKMRSDLRGEIESACQKQEKQLTAQRENLSMRLASARSSLEFAERMCREANDVDVLSIRNE... | 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: 374
Sequence Mass (Da): 42486
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K9J8V3 | QCIIWYTLLLFLFEYRGAKLLIMEQFPETAASIVSFKVDSDVVSLDGRDFLETDAEIGDDGKLHVKVRKSNASRRSLSAMTPRPSNLTGAEIYSLSSSRNPTPRGSNFNPSDFYSMMGVQGFNTRHSNFGPADLYSVQSSRGPTPRPSNFEENCAAQTVTSPRFGSYPAQTVPASYPAPNPEFSAPIAKSNSKNQQPPPQPQVEAPPVSNSAIAKTNSHHDAKELHMFVWSSSASPVSDGGGLHVFGGNDSSAAEQSGRSDQGAKEIRMIVADHPQNGENKAAVPESAPTAEGYGREAFSFGGRGGEGEEAERERAGPTG... | Function: May act as a component of the auxin efflux carrier.
Subcellular Location: Membrane
Sequence Length: 518
Sequence Mass (Da): 55448
Location Topology: Multi-pass membrane protein
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B9XHE8 | MQATRIALVGDFNSKVIAHQAINASFALWNSSTAKPIAPIWTGTDTILPGNDSLFTDFQGIWCVPASPYKSIDGALWAIQFARTRSHPFLGTCGGFQHALLEYARNALNLATANHTELDPSTEFPLLHRMQCSLVEKSQIISATGHGRFTSMYGATEGTEAFHCSYGLNPAYENLFQNTPLQITARSEDNEIRAIELTNHPFFLATLFQPERKALTGQLHPLVHSFFSAAASCALKNA | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 238
Sequence Mass (Da): 26087
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A0A498J374 | MIDWDRWLVKWHIEFWGRQWNFVDIATLAGLSYLHYLALLAPFHFNWTAFWLAVALYFITGVGVTLSFHRNLSHRSFILPKWLEYFFAYCGVLSLQRSPLEWVSIHRAHHQFTDTLKDPHSPIKGFWFSHIGWAIDYRNRFGSYEARLKNVGDLKSQPYYRFLHYTYPLHSIALGVVLYAIGGMPFLVWGMGVRTVIFLHAIFGLNSVCHTWGQAVWDSGLLTHGEGWHNNHHAFEFSARHGFEWWQIDVTWYVIRFLQAVGLATDSFVASPMGEWVTQWRVEFLGREWNVVDIGSVVVVSALHLLTLLAPFHFNWPAFW... | Pathway: Lipid metabolism.
Subcellular Location: Membrane
Sequence Length: 519
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 60599
Location Topology: Multi-pass membrane protein
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A0A953CFW9 | MTAPVSLRAPQFWWRKPGALAALLYPAAAIYGAVAGARLARKGYRANIPVLCIGNPTLGGAGKTPAAITIAKLLQAEGRKVFFLMRGYGGSEAGPLLVDLRKHSATEIGDEAPLLAKVAPTVVARDRAAGAKFAEANGAEILLLDDGFQNPSLEKDFSLLVIDGAKGLGNGLVFPAGPLRAPLKPQFTRAQAVVVVGDGNAGEKAARFAAEAGIAVLRAKLTADAESARQFSGKPVLAFAGIGAPEKFFASLEAAGAEIVSRKPFGDHHRYSEDDAKALLREAAEKNLLLATTAKDLARMSADANLSSLRANALALNVSL... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A1R4A6E9 | MKSVTGRVYCSSANIGSGFDSFGICHSAFFSDGNLSITEEQGPLKIDFRSNLNDFDMLENSALAVIRKIAEDFEIISHLSLELNSTIPVGMGLGSSGAASVSSSVLMNELFSLDLPVNEIIKYASYGENFASGSFHLDNVTASTIGNFSAVFSESPLRIRKFDIPENIGFISIVPQIIARNKTQENRKLLPEMIPFKKVVRNINFSNSLLAGIITGDRDLMEYGLDDQIVEQARMIKYDFLVDVRSICKRNNAIGLILSGAGPAMLCFTDDRTDKGQIRKDLTHYFQSRELDFIMADSYPSAGAYERN | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
EC: 2.7.1.39
Subcellular Location: Cytoplasm
S... |
A0A2K5QRA9 | MINGLGRENHYRKRSASRGRSGSRSRSRSPSDKRSKRGDDRRSRSRDRDRRRERSRSRDKRRSRSRDRKRLRRSRSRERERSRERRRSRSRDRRRSRSRSRGRRSRSSSPGNKSKKTENSGFAFYFPPSLSFFYFPKNFDQNKLEEEMRKRKERVEKWREEQRKKAMENIGELKKEIEEMKQGKKWSLEDDDDDEDDPAEAEKEGNEMEGEELDPLDAYMEEVKEEVKKFNMRSVKGGGGNEKKSGPTVTKVVTVVTTKKAVVDSDKKKGELMENDQDAMEYSSEEEEVDLQTALTGYQTKQRKLLEPVDHGKIEYEPFR... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 1009
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): 114904
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A0A1J4VAM0 | MIAYLKGKLVSKSPTEVIVEVNNVGYRLGISLFTFEQLGKVGETIEIFTYTYVREDALRLYGFTAKKEKEIFLMLINISGIGPKLALTILSGVSPDKLKTAIVNEDVGLLTAIAGIGKKTAQRLIVELKERLTAILPKAADWEKKDYLLRNEAANALVTLGYKRNQSIKAVDRVLPKLEKDVTLEELIKKALERI | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A7S0WTM9 | GIVRCMNDTGRMLKELQATSLGQYILRQAAEVSTPLAAALVDNLQRSFKVALADTATRDNADVHFMCKAQLLVAQLYRRFQGAEGQEQFRFSDADQFTVFSDSVLPAVLWSAGVLRVGDGLAAKIDGGEALSAGAEEEVALRAAAVRAGDMIVKEADHAFTAMDLSFYIWGRMSKEEGMKRIPRHIVKDTVMY | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
EC: 3.2.2.-
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-pho... |
S0FX73 | MTSHSGINSLQQEFHLKTDVLMAAHTRLNVGGPADLLAQPRTRQELVALLGAAKNASVPVTIVGGGCNLLVSDQGIRGLVMVTTHLKSGIQVRPHSGNHVHLFMEAGQPLSTVCKYAVNQGLAGLEFCAGIPGTVGGAVIMNAGTADQGIGNRVYSLEVLNLNTLSIQTLKKDALTFSYRRLHLDNHLILGITLALSPGDPARIKQTYEDIFLRKQHTQPMDLPSAGCFFKNPGPDRPAGKLIEEAGLKGKTIQDAQVSLIHANYIVNLGHATCKDILALKQHIQQQVLDRYNIVLETEVITTGDGMKNE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 310
Sequence Mass (Da): 33340
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A0A3S4XSV5 | MFEDDCLIVLNKPSGIAVHGGSGLNFGVIEALRALRPEARFLELVHRLDRDTSGILLIAKKRSALRNLHEQLRLKTVQKDYLALVRGQWQSHVKVVKAPLLKNELAGGERIVRVSEQGKPSETRFSIEERYSNATLIKASPVTGRTHQIRVHTQYVGHPIALDNKYGDKDFDTQIQTFGLNRLFLHAFSIRFEHPKTSETLRFNAPLDEKIKAVLKKLRESK | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 222
Sequence Mass (Da): 25238
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A0A3M7TA22 | MFKFQISIYFLLVSIFLVYNAVFFNLFSYKQANFDTENNKFEPPVAQNSAIINGRLILVLIDALRYDFIFESNVAKEKLRMPFVNRVIREQKAIPFKLIANPPTVTLPRLKALVSGIIPEFIDILWNFNTTYLAEDNIIRQFNLQNSPVIFYGDDTWLKLFRPNESFVRYEGTTSFMASDYDQVDFNVTRHLAFELEQTDWKVMILHYLGLDHVGHIEGPYAPFNIRRKLHEMDEIIKKIYSNLNRNDLMLVLSDHGMANEGGHGGSSHMEITTPLLLLSKGLFGSKFTYADDQKFNSLIENIKEKKQIDLVSTLSCLFG... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 462
Sequence Mass (Da): 53670
Location Topology: Multi-pass membrane protein
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A0A160SXU6 | MGSIGWPELLIVLAVVLLIFGVGRIARVGGELGKGVSAFREGLKDEKQTTAEKEAAEKQNDLTGGPTL | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 68
Sequenc... |
A0A662F6S1 | MNDERIYKVSELNRAAKRLLEEGIGSIWLRGEVSNLRRAASGHLYFTLKDESSEISAVRFRGRTDLLPTPPLSDGMEVIAFGRLTIYAPRGRYQFVASIIQPAGLGALQAEFERLKRKLNSEGLFSPEHKRPLPRFPERIGVITSPTGAAVRDIISVISRRWPLAEIYLFPSQVQGEQAPEEIISGIEAAQRFSTTVARLDLLIVGRGGGSIEDLAPFNDERVARAAFKCEVPIISAVGHEIDFTIIDFVADRRAPTPSAAAELAVPNRAEIAASVAEAVARALRGINQRLERSSRLLDSTLRGYIFRIPIRRLETAAQG... | 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... |
A0A949SI78 | MIHPTAIIDPSAQIGTGCHIGPYCIIGPDVVLGDDCRLQHHVTIMGPSRIGRGNQFYAFTSIGQQTQDLKYKGEPTWLEVGDHNTFREFCTVHRATSPGDRTVIGSHNNFLSYVHIAHDCVVGSHVIFSNNGTLAGHVTVEDHVILGGLSAIHQFCRIGTRAIIGGCSKIVQDVPPFCTADGNPARARGLNIVGLQRAGFSREQMRALRQAFRKVYREGLNNAQAVEALRAGELTPEAAHFADFVATTKRGIVAGGKNQADDED | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6.
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the ... |
A0A662EUU2 | MPVTPLLIACILLIPTSAFISTAFASFMRSCSLGQQIRAIGPEGHLNKVGTPTMGGIVVLAIWILGTAALGSVYPLTLRSGFILASGFLFGAIGAADDLISIRKHRSLGLSPLQKIFISSLAAVVLFFGFSAVLKTPLRVPFSSLTVALPPIGSFFLAWFVFLATTNGMNLTDGLDGLATGVTILILIGAALLLPTLENLALTLPLIAALIGFLWINAHPARLFLGDVGSFALGGIVASLAMASGTTLILPILGGIAVLETGSVILQVIWLKATGRRLFKMSPLHHHFERETKPIGDYVLPAPEWSETTITTRFLILEAL... | 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... |
A1WMN7 | MYLGIDLGTSGVKLLLLDEQQQVLATADAAVPQHRPQPTWSEQHPADWMAAVESAVAQLRAQAPAAWRQLRGIGLSGQMHGAVVLDAQGQVLRPAILWNDGRASAECAALEQIEPAARQITGNLAMPGFTAPKLLWLRTHEPAVFAQIRRVLLPKDWLRLQLTGDAVSDLSDASGTLWLDVGARAWSQAMLQACGLNLSHMPALAEGSAPTGVLRADIARRWGLATGVPAGVQKGVVLAAGAGDNAASAVGVGARIAGQGLVSLGTSGVVFRVTDAFAPATGRAVHAFAHALPQRWHQMSVMLSAASAFGWVTRLTGQRD... | Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
EC: 2.7.1.17
Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+)
Sequence Length: 526
Sequence Mass (Da): 54442
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E0UR55 | MKTITFIGNGNMALSIAEGLKENYKIEVVGRDSKKLDAFEQKLGLHVEKSLLDNYNIEQKTVMLCVKPANVEEVSAKLQGKAEILYSVLAGTSIEKLKNNFNTSAVVRAMPNLAASVGKSMTTLTGDTAYKEESQTLFSSIGTTRWLGSEKEIDIATALAGSGPAYLALIAESLTDGAVKQGLKRDDAMAIMRGLFDGFGTLIQDIHPALLKDGVMSPGGTTAAGYAALEQGNVRNACIEAIEKAYKKAVEL | 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... |
A0A2H5VQT3 | MASNTPSRPTTLADVVAEVRRLAAENLRLFRQLEENERRFRSLAQAAWRAEEEQRRRLAQELHDGLGQLLTALKVQLELLRPAGPDELERGLQAARELAERALREARELSHLLRPQVLDDLGLPAALRWLARTLGESTGLEVRLSCPEGLVQLHPDVQTLVFRVVQEALTNVLKHASSKVAWVELAETEREVLLAIRDQGRGFAVEELFSGKLSGSGLRGMRDRVELFGGHLQVEASPGRGTTLSVRLPKQPGGASS | 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... |
A0A7S0WFY7 | MHSTLRAQNVAVPTKVVAGRSRSAQASSRGMVAKANDYKVLSLAHAAGKFMGNRSALARSASVRGNKRAQSVQTVASNAVEISKQPKPVFPFVKIIGQEDMKLGLILNIIDPTLGGVLIMGDRGTAKSMAVRSLAAILPEIQVVKGDAYQSNPESPGEMGPESKAKFLAGESLDSEPRQITVVELPLGATEDRICGTIDIEKALTDGVKAYEPGLLAKANRGILYVDEVNLLEDGLVDVVLDSAASGWNTVEREGVSISHPAKFIMVGSGSEEEGELRPQLLDRFGLNVQVRTIMNVDERTELATARMMFDRNKFEYIAS... | Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Function: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + p... |
A0A917M356 | MSAVTVMSFRSIAGKWDLRQRVLVIIGQIAGGTLAIALLTVASFSLHFELSSAGYLYLLIIVLIALAWGFWQATVISFVAVLCLNYFFTQPIFSFYIANTQDWIAFGVFEVSALIVSSQSARNTLHMRENFLQQQSIERLYELSRGTLLLNLHQTPGPQIVQLIQHIFNLEAVALYDPLLGRVDKAGDCSETEEHLARGAYLQDLSYDDRLTQTSQRSLRLRGRPTGGLALRGNITPAIANALTSLTAIALERYRSFERESHAKAAHQSEELRAAVLDALAHAFKTPLTTIRTASSGLLEIGSLNGTEYELAQLIDQQSI... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 494
Sequence Mass (Da): 54450
Location Topology: Multi-pass membrane protein
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A0A171KP19 | MSIADLRQTYSRDTLLEQDLAPTPLEQFERWFQQAQQGEVAEPNAMTLATADAQGRPDARIVLVKGVDERGFTFFTNRESRKGQELAAQQRACLLFFWQPLQRQVRIEGTIEWLPDAESDAYYHSRPLDSRLGAWASQQSSTTTRDALEAAFEAARAKYGDEPPRPPHWGGYLVRPEAVEFWQGRPSRLHDRLRYERQADGQWAVRRLAP | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Ca... |
A0A0E9NLK9 | MSSSSSSKREREVGGYRIGNEIGRGSFATVYKGYRIKDREPVAIKSVLRSKLTKKLLENLDSEIAILKSLGHPHIVALIACFNHQPSPTPQYDLSSSPSPANFEAGGSSTSKYIHLIMEFCALGDLSFFIKKREHWKEIPEIRHLSTRYPYPPAGGLNEYVVKHFLRQLSSALAFLRERNLIHRDVKPQNLLLQPPPNPNAPAFCSSGEDLPVLKIADFGFARSLPGGGLAETLCGSPLYMAPEILRYEKYDAKADLWSVGAVLFETLTGRPPFRAQNHVELLRRIERAGSAGVRWPEEALSNVSGEMREFVGRLLKKEP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 822
Sequence Mass (Da): 89479
Location Topology: Peripheral membrane protein
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B9XS05 | MSGRLLLLNRQHTRLIDRRWLRWATKELISDLLHFEDFDVTIHLVGEREMTRINEKHLQHAGSTDVITFDYSDSPGSEPLIGELFICVDEALVQAIRFKTTWQSETMRYIVHGLLHLKGYDDLETTARRKMKREENKLLKELRVRFRLSKIEGKSKLRA | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 159
Sequence Mass (Da): 18817
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A1WJ64 | MALVDIQVPDIGDFDEVGVIELLVKPGDTIKVEQSLITVESDKASMEIPSSHAGQVKELRVQVGDKVKEGSVLLTLEVAGAAGAANAAGATEPATPTAAAAAPVAAPASPSTAAAPAGATPPAIPAQQPSPAMASLPHASPSVRKFARELGVPIAQVKGTGPKGRITLDDVQAFTRQVMSGAMQTQAQAARAPAAGSAVGLDLLPWPKIDFAKFGPVERKELGRIKKISGANLHRNWVLIPHVTNHDDADITELEAFRVQFNKENDKSGIKVTMLAFMIRAAVAALRKFPEFNASIDGEQLVLKNYFHIGFAADTPNGLM... | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3... |
A0A8B7NYK2 | MEVLSSNKEKLKIGFIGAGNMASAIIAALLKKGAVAPEQLIVSARTDTRLAELRQRGIATTTDNVALLKQCSDGVVFLCVKPHVWPAIAPALMYGGRRALFISVMAGVSIQKLSQQAFGERIDLFSLVRAMPNTPARVGEGCCVYAVESVLSAERKALAAALLGCLGLVREVPEQQIDAVTALAGSGPAYIYVAIEALADGAVKMGLPRDLALALAAQTVRGAATMVQETGKHPAQLKDEVCSPGGTTIAGIHKLEEHGFRNALICAVEGAALRAKELGQE | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
EC: 1.5.1.2
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
Sequence Length: 281
Sequence Mass (Da): 29396
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A0A1F6QQH1 | MSALARYCHANGYYVSGSDKEQSGSIKDLRSEGIKNIWTPHSTNNIQGIFPDLIIYSTAIENSNEELIWAKENKKEILHRSDLLDQITSSKKLISVSGTHGKTTTSGIISEMLIHSELNPSVIIGGILESRNTNSVIGSGDYFVIEADESDKSFLKGNPEISIITNIEPDHLENYPGGLEEIKAAFLEFAKKAITKKGLVVCLQDKITGELIRKNFDLNSPNLISYGINTNSPEITLRANFNNKTNSWDVYLKQNLLFTFRLKNSGNHNVLNALAAIAVGNLMGINLKKIKTAIENYQGVKRRFQVITKTNEITIVDDYA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 456
Sequence Mass (Da): 50862
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A0A1H6NY72 | MRIAVIGSGGVGGFYGLKLLEAGHDVTFVARGPHLKAMQESGLHIENDLGSNGSAKVKATDDITSLAQPDLIIIAVKLWDLEGIAHDLKKIAGPNTAVLSLQNGVIKDYVLRRVFGEDNVIGGVGYVATSIGRPGVIKQVGALQRIKLGEYDGQKRARTEELVRSFADSGIEATLSDDIARVLWEKYVFLVGLSSMTCLTHLTIGPIRESEGSRGVLRSIIAEGTSVGRAHGISLPEDYADQCMDLVDNLPYTMTSSMFHDLEKGNRIELPWLGGGVVSLAREVDVAVPVNTLITNALSPYIDGRKRS | 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: 308
Sequen... |
A0A522GZC6 | MTNETTRAEGMDAVFMDSIRPAQEMRKDRRHFLISAAGVLGAGAVGLFADVLIDNMNPGKAVEALGAPIDVDVSKMEPGQLILAEWKKKPIWILKREAWMLKTLSEPSLLRRLKDPESKQNQQPASKFINGNYRALQPEMFIAVALCTHMQCIPDYRPAPHTVTPWWPGGFHCACHGSMYDFSARVIEGSPAPLNIPVPPYYWKTPMVAHIGEMNGSGLDKNWTPDIW | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
EC: 7.1.1.8
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrom... |
A7RMQ9 | MASGSSISSQSSIEKVREELTCSVCLEQFREPKMLPCFHTFCKECLEKTKQSFRGNLLCPTCRTKTSVTEHEMIQKLPNNFIVNRVLDALGAENSGELKYPNLGPNLKSFCINHKEKELDLYCRDCQICVCTICFATAHQGHHLQNVELAMEEGKAKIKKQLLESQNRAELIGEARGVLEYKQDKFEKRFQDCKQQINKTLSQVIKAVSQKAEEMIEQLEKAHKTRQKALDCQQEDLRLQELKLNGAQTFAEQIIASSSGVEVLSSQKQVTEKLKDLNTSNGLGFIDKVNDFFEVHFDVSDALECISNARVEESSISPGE... | 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: 636
Sequence Mass (Da): 70947
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A0A932VUK3 | MNILIAGGGTGGHVYPALALIEELRRSQEKIRIGYVGTAKGIESRIVRHESGIEFFEIEASGVERKLTSKTIREAWSNLKGLSLSLNIIAHFDPHVIVGTGGYVSFGPLLWGTLLGIPTLIHEQNRIPGLVNTLLAPLVDSVLVSFPETANEIRAKRAVHTGLPLRSSITALREKLDQTSAREYLKLDPNRPVVLVTGGTHGAQCIHDQLLSGSSELQECGVQLVILAGRDAVRLQSLTRQRNSDSIRVLGHTHEVGQWMKAADLMVCRAGGATLAEMTTLGVPAIVIPWPGAAHNHQEENAAWLSERGACHLLRESECQ... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A1I6IPU1 | MNWKQSKNSESETSMKGGRTDLALEVRESFTEDNVEIKGVILKKEENEQKDIRVTTVEITDKQGEKVMGKPIGTYITIEAPHLNEKDENFYKPLSEEIAKYVERLAGGLKNKQVLVVGLGNREVTPDALGPDVVDNLFVTRHLINEYGKEFKEKHNMESMSAISPGVMAQTGMETGEIIAGVIHETKPDLVIVIDALAARSVERLNRTVQITDTGISPGAGVGNNRKELNRKNLGVDVIALGVPTVVDAATIVSEHLERLLSRQGFSEKEVECFIQEMNDPSMRNMFVTPKNIDESIKQISYTISEALNQCFFKGIGA | PTM: Autoproteolytically processed. The inactive tetrameric zymogen termed p46 autoprocesses to a smaller form termed p41, which is active only during spore germination.
Function: Initiates the rapid degradation of small, acid-soluble proteins during spore germination.
EC: 3.4.24.78
Catalytic Activity: Endopeptidase ac... |
A0A095WY08 | MARTLFVASPEPRTGKPMVTIGLASFFIEKGMKVGLLRPIVRDRSTDAMLNIFNNGTVISGPAVGALTYDEYIADPDSALESIVRTHRKLSENVDIVIVSGSDFEGVVGFDEFEFNCRVSANIGAHMAVVLSGIDRTPEDVMDAGRLAVTTARQEFAHVAGVVITRVPEENADDYRRKVEKIPTYVIPEDPLLTAPRVIDIMNSTNATLVNGDRANLLREAENVLICGMNSTHVLERLQDGQIIIAAADRPELLMTVAAAHAVEGKPSLAGLILNGGFELSEQVMDLVGKLVPDLPIMTVSTGTFETADRVSRTRGPVHL... | Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Function: Involved in acetate metabolism.
Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
EC: 2.3.1.8
Subcellular Location: Cytoplasm
Sequence Length: 686
Domain: The N-terminal region seems to ... |
A0A3M7QN87 | MSSDSLPIPDDLVQPVPISSTTFFLTAALIWSTLFYTKNPLQYYLKYVTYALIVIVVATFTIFLCLLRPCDARNVAVVAKVLSFFFQIFQIDIQLENSKYFQSKEPFILVCNHQSSLDFLTMMKVWPGGNCTPLAKKELFYSGPFGLAIWLCGITFIDRLNPQKARGTIDKLAKKINDENLRVWIYPEGTRSPSTNLLPFKKGAFHLAIQAQIPIICVVTSSYSNFYHKREKKFDFGGKVKVRVLPPFNTTGMTLDSVAQLTKHLQDLMQREFDLLNKEIGLDQKYYIKAKSNEETNEKTHDVTRTFVQDLDYTQISDVT... | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 354
Domain: The HXXXXD motif is essential for acyltran... |
A0A1S9CDV5 | MRKTKIIATVGPKTRDEESLKKIIKAGASAIRLNFSHDNQDTHKKTALRVMKIREELGTPTALVLDTKGPEIRTGVLTGDNEIELQTGQTFILTTDEMEGTSEKVSITYKELPHDLSEGNRVLLDDGLIELIVDEIKGNDIICTVKNGSHLGSRKGINIPNVRLNLPSLTEKDISDIQLGAELGFDFIAASFIRKASDIIKIRNILEEHGGRGIQIIAKIENQEGVDNIDAILQVADAIMVARGDLGVEIPAEEVPMIQKSLIKKANLAGKPVVTATQMLESMVVNPRPTRAEVSDVANAVFDGTSAIMLSGETAKGDYP... | 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: 586
Sequence Mass (Da): 63136
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A0A938Z7U0 | MITIREMQIDDLEQVMPIEEANFSIPWTETGFFTFLIRDDALFLVAEEDGEILGYLGILISFDESEITNVCVAEKARRRGIGRALMEELFHRMQERKVRVIHLDVRLSNTPARNLYESLGFVQDGLRKGYYDLPKEDAVLMSRTDESVPKR | 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: 151
Sequence Mass (Da): 17501
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A0A1J0I1U9 | PLSANLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYHHLF | 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-cytoc... |
A0A0E9NFX7 | MLVVSIQELHIGLDGKTPIDLNVRSRQQFVQAVPILRFLQLYLHVLWCPSSIEPRQSYTPARPLALIMSSGARLAPPTILHRTASGTDTSPPRDRLLYAPPSDEFIPRGRLPSRGSSSFQRPNFNFCSPRRPPPQGTDPGDAVRKPWRKLLWIKQDYPDNFTHHTFLHSLQRNVSVRPYDFWPLVNESTVITQHLSSIIIFAAAFVAIYTDLVRAGSIATLGTVGTILGYGYLDWKLKPQQDNPYRRKRTRTQTAKSSLLIFFTLLGLSPILTSLTKSTTSDSIWALSTWLFLANLLFHDYASSPPSTGKMDAALDLRFP... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Membrane
Sequence Length: 454
Sequence Mass (Da): 51006
Location Topology: Multi-pass membrane protein
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A0A6I1EDC3 | MLHLSSPEALALVFLLGGIGALTRYAVLVVSAHAAGPFPAGILVVNTLAAFIGSALVSARAPEELLLIIGGGFVGSLGTLSSLCSEIIALERLGKYGSIVLFVVLTLVTGIAATLLGNAAGASFHG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 12541
Location Topology: Multi-pass membrane protein
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A0A949WFK5 | MNAYVTFFVGTAILLLLLFYIGTVVHKTKRWVGSSLIMLMTLFAVLTVKNIGIPLGIDLKGGSEFVVRLKESTDKDGKTQSVTSADVQQAINILEKRLNPNGEKDLAMQPQGADRILIQMPGVKPEDFADVRTKIQQVAKLEFRIVHQDSSSKIAEINSGGLTEPGWQKMSYKKQKDEQGNDLPDRGAELVRNRADMEGDGVSDAFATMDAEGWKVFLNLNGDGSRKFDEIASVNKGRQLAIIVDGEIISAPVLQTDHFGGTAVISGNFTRESSVQLATLLKNPLKNPMTIESENAVSASYGQSSIDQGKWICVAGLVMT... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 799
Sequence Mass (Da): 85458
Location... |
A0A950WEI1 | MNQLPASPVQAKLRELAAQRILVLDGAMGTMIQALRLDEAGFRGARFDAWNRELRGNNDLLNLTRPQAIHDLHLTYLRAGADIIATNTFSSTSIAQSDYGMESIAYELNLKGARLARAAADMAEADDAKPRFVAGAIGPTNRTASISPDVANPGFRAITFDQLRTAYAEQVRGLLDGGADILLVETIFDTLNAKAALYAISEVCDARGVRVPVMVSGTITDKSGRLLSGQTPTAFWHSVEHAQPLSIGFNCALGAKELRAHVAELAQVADTLICAYPNAGLPNAFGRYDESAPVMGALIEEFAAAGLVNIVGGCCGTTPA... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor u... |
A0A2K5QWV5 | LLCCSLLLKKKMEDQKTEQDGIKPEDKAHKAATKIQASFHGHITRKKLKGEKKDDAGASKKKDEAPVADGVEKKGEGPTTTEAAPGTGSKPDETDKAGETPSEEEKGEGDAATEQATPQAPESSEEKASSAETENATKASTDNLPSSKAEDAPAKEEPKQADVPAVVTAAAAATTPAAEDAAAKATAQTPTETGESSQAKEKVEAVDETKPKESAWQDEGKEEEPKADQEHA | PTM: Palmitoylated. Palmitoylation is essential for plasma membrane association.
Function: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.
Subcellular Location: Cell membr... |
S0FYA1 | MKIGIAGVGGIGSNVARHLAQAGMPHLKVVDFDGVVPDNLNRQFYSMDQVGCPKVDSLKQNLQNIHPAIRVETLNLRLGPDNMARIFSDCDGVVEGLDDPGTKKQLMEALADAGIPVVSASGIAGQDMDGIAVRTMGNCHIVGDFSTDIAHALLFPPKIAMIAARMAQIVLKLKQTIFPKGIYGILGEAFSLGRSNVTMAEQLVDTGIDILQYREKPGTKDRKTMLEECEKIRKITADAHVPFIINDFLDIAMIIGADGVHMGQTDLPVRAVKQLAPRLLVGCSTHSPAQAAQAMADGADYIGVGPLFATQTKEDVCEAV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-met... |
A0A357B6B6 | MLIKRYQMKCTLVSQYRPLFTGEVELVAARSVEGEFEVMAGHAPLIAVLAAAPLRIQTATEEHIYAVRHGLLRVASDQVSILTEEALLPTEIDRDQVTQQHAKITTLLQCAVKENKEQLTSELAWLEAQIKVNNRAYE | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 138
Sequence Mass (Da): 15514
Location Topology: Peripheral membrane protein
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D7CX81 | MNATLKLPRGFRTAALAAGIKASGRPDCALIAADAPLRWALAATTNTLQAACVVRNRALFTGERAVRAVAINSGNANCATGEAGARANGAFAAAAAAALGVAPDEVLTASTGVIGEPLPVDKLTAALPRLAAALTDDAAGLAQAILTTDLVPKVAEARLEGGARIVGVAKGSGMIHPNMATMFAFVMTDADLPQGALRALWPEVVAQSFNQISVDGDTSPNDMAFLLANPRVAVREAAFAEALRRVARELAKRIARDGEGATKLLCVRVTGASSDAEARRAARAVVVSPLVKAAAHGCDPNWGRVLSAVGASGVPLALPR... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
A0A0D3G088 | MTPPRPRGSLQVKGDFTRVPFLGFGSSILLGRTRPIQLHVFGPWPITRPIAHRCRVVFFLFPSSSALLYSRSQASAAIPSAAPTSFAARFRRASAIRALPDSSAFVFFDLLLRRPRRSIPGEVMSGVLAKFAIASAVMWTAPVAIVYGFYYQMIPGVSQLSSSTQTLASGFLAVISINLVIGFYICMAMKETPHQEPQPDPTFLANAKASIDQPTPSQVNDDSHGKGKVE | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 230
Sequence Mass (Da): 25029
Location Topology: Multi-pass membrane protein
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A0A1F3J5J6 | MNNTQIPKRYARALFELADEMNILPAVEQNIRLLKSTCEQVPEFRQLLRSPIVKPLLKKKVVSALFEKDFHDLSIRFLKLVIQQGRENYLLETANEFIALCREKDGIIEVELTSAVNLNEEIIKQIEDRISELTGLKPDTTRKVNPNLLGGFKVRFGDNMYDASLRNKILKIKRDFQTNIYEKGF | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A1F6QFJ7 | MNVLVIGSGGREHAICWKLHQSSHVKQIFCSPGNAGIAEIATCVPVSPTDIERLAEFAIVQKIDLTIASMDEPLARGIVDYFRKKGLRIFGPTKEAAKLEWSKYFAKEFMLRHNIPTAPYACFEQKEFALAYAKSQKHPIVVKADGLALGKGVTVAQSFEEAKIAIHDCFDGKFGQAGEKVVIEEFMRGHEVSVFAISDGKDAVTLVPAQDYKRLYDGDSGPNTGGMGAYAPVPFMTGELIGQVKEEIIMPTIKGMEKEGNPYHGILYCGLMVTDESKIKVVEFNSRLGDPEAQVVLPLLDEDLFEICWAVTEGELGKYK... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A3M0GM00 | MTSPVYEEGDCRHARYSGSVDQTEERVHRDVVSFVRRSKRMNDSQKGAWARHASTFVLPLPVGDVPTSVADGAHVDWDTTFGRQAPRIVEIGSGVGDSLVPMAAARPDVDFVAFEVFKPAVASTLGRIGRAGITNVRIAMVDGSRGLDRLFDDATLAEVWTFFADPWHKTRHHKRRLVTPAFGDVVASKLVPGGLWRLATDWEDYALWQRDALDSHGHLVNVHDGWAPRWEGRPITKYEQRGLTAGRATHDLTYERVR | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 258
S... |
A0A9E3K387 | TEGVVGQVAGTVAVALAAVNVFGGFLVTQRMLEMFKKKEPKAKAGDKA | Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
EC: 7.1.1.1
Catalytic Activity: H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)
Sequence Length: 48
Sequence Mass (Da): 4964
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A0A2P4W703 | MYFSKRIGDVALKTVRERRANPFVDYIRDLSKRKPLQHSYPADLLNKYEAELKQLPPYVYAGFDPTAESLHVGNLLILVNLIRCQQFGLRPIALIGEFTASIGDPSGKKSERDLLGEDVVIHNSKKVSEQIRNVFANTCRSSEPPIVVNNNDWLGKFFAQLHDDKAEELLLLFSLRGVEDLEELLQNHRNNLGKWIAQKELAMEVTKMVHGEDGLDSALRCTKAMFGSKKADLTGLSRSEILKLFRTTIDLKKEDISSMGDLANVTRQGNGKGYLLMQKGAFSVNGTKKVNPAESIEGVSSSLPALTDLTLVCWGKRDYR... | Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and i... |
A0A0P6XHN2 | MPIHCEIISQDRIVFQDDVDIVVLPGEEGVMGILPNHAPLLTTLKYGIITVRKKGEEQYFTVAGGVAEVLPEEVVILADAAENVMEINLARAEEARRRAEELLSKIGDVDTDEYLAAQAALRRSTLRISAAQRYRSGQPRIGGG | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 144
Sequence Mass (Da): 15769
Location Topology: Peripheral membrane protein
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A0A3D3WZ68 | MRCVMKVPCRWLAEYVDIEVSKEAVERLAERLTLAGLEVEGITPTGRVHGAVVGRVLSHRPHPNSDRLSLCLVDIGTDEVEVVCGAANVVAGETVPVVTVGGELPGGLKVKARKIRGIASHGMICSRAELGLEESSSGIWNIETDLKLVPGIELNDLLEFDDYVLDVKVTSNRPDCMGIYGIAREVAAIINQPLRPLAIDLCESEPPTEELFSIEVENATDTPRYGVRLMSDLITGPSPLRMQHRLLKAGMRPLLNVVDVTNYVMLELGQPLHPFDADLVAKRILVRRARAGERFRTLDGVERSLSEEVLMITDSDGGLA... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 794
Sequence Mass (Da): 87607
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A0A6A3A4R8 | MANNLAMISISSVFLVTMVVVVVVRMDHDTNKSDGDDDGGGVTSSKKELHALCQPVNYKETCEQSLSQTNSTDTKELIRVSFQAAVTEIKAVLSKSATIHELQTDEGTKDAFKVCQEVMGYAIDDLENSFKALGEYDVTKIDDYLMNLKVWLSGAVTSQQTCIDSYEEKNGTAADKMRSLMKKSQELTSNSLHIVSGISSILKDLNIPGIDNLDTTGLERKLLSSGGGDDFSQWGRMEYHGRKLSWLEGLFKTPDHDGAITGWMIKSPQRKLLSRSDDDDFSQWGGMEYHGRKLSWLEGIFKTPDHDGAITGWMIKSPQR... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) ... |
A0A3G3A4K7 | MPVLMGGFGNWLMPMMINPDMAFPRMNNMSFWLLPPSLFLLILSMMMGSGSGTGWTVYPPLSNNXFHSNMSVDFTIFSLHIAGISSIMASINMITSIINIRSKLMKMNKISLFSWSILLTSFLL | 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-cytoc... |
A0A8B7NWR4 | MLCGLSAPLSALTRSYQSQWVTFTPLTQFMAHHTCSHIATCNAQSFMHNVATNPSHCHAVCMVQQHSNCTGPKLKTPHSLYMRGYTINHLNNNTTTSRIVDQIIRQGFNERYLSTTAGAVHNDSHSNHNISNGANSDSSSSSDTDDMSGQESYGSVSDVRAAVLDAALQHVPLLGWTEAAIAKGAEELGYSCAAHSLVEGGGAELFLWLQRRLNQQVEEHLEEFTLQGGEKRDVMLEALKQRLLLLMPYRAVYAQGLGTLATSPSLLGESISITASLADIVCHYSGSNQPDTSWYVDRASVAAVYKLTELCYLQDQSADC... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Location: Mitochondrion
Sequence Length: 373
Sequence Mass (Da): 40550... |
A0A498JGF8 | MERAKLHSNMVWQFQFIKQNAIHLEEKEKREKELLVQIIEEADEFKKRKITTENNKVANREREKLIKRSFIAEVDKNHWKAIADLIPNEVPAMEKKRGKKDTEKKPSILVVQGPKPGKPTELSRMRQMLRRT | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 132
Sequence Mass (Da): 15699
Location Topology: Peripheral membrane protein
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A7SUG5 | MDTVKELQEISEELQDIEVQIESLLERQQFLLSRKQELEVIALSNSNDSVLLSFSSNVACAQGSDWSSTAFSWSQEVEAALKNVFKIDTFRHLQLECINATMSGVDCILIMPTGGGKSLCFQLPAVVSKGLTLVVSPLVSLMEDQLWALKRLGIKAALLNASSTREEVNSVHASIVDKKSDLKMLYVTPEKIAKSKRFMAKLEKSYESGLLSRIVIDEVHCTSQWGHDFRPDYKILGILKRQYPGVPILGLTATATTKVIEDVKKILGLHANCLLLKASFNRPNLFYEVQSKPTTNSAFMSTIHQLITKRFSGDSGIIYC... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 582
Sequence Mass (Da): 65083
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A0A2N6TY50 | MPTSPEAASPDACPPAAPAPPAPERPQRPEPPERPQHPVPPLLAVVGATATGKSELGISLAQALDGEIINADALQLYRGMDIGTAKVTPAERADIPHHLLDVLDVTDEASVSAYQQQARAAIAAIRSRGRTPILVGGSGLYLRAVLDDIAFPPTDPAVRERYEQRIATEGTAALHAELAVRDPEAARTIGPGDARRIVRALEVGELTGQPFAAFLPRPRYLDPTTIQIGVHRPRPILHERISRRVHRMVEQGLLEEIRSLRAAGLDQGLTARRAIGYEQGLAVLDGTLGCAEAIEATIVGTRRLVRKQDTWFRRDERVRW... | 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... |
A0A662EWL5 | MILRLAWRLGYKPGRVMSEVLEWIEVLAVAGALAAIIMSFVTVRMHVPTGSMIPTIDPHDSFFVDRITYYFRDPKPGDIIVFRHTEQVL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 89
Sequence Mass (Da): 10203
Location Topology: Single-pass type II membrane protein
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A0A378RNC7 | MMSLFFESEWIIYWEVAYFIIAILVSIRIIYDTDSISKTLAYLLLVFFVPIFGIIFYFSFGINYRRRKMYSKKLIANDNYAERFNKRISEIHLDLTQQGHPIVDQHRSFVQLLSNAIVGEGPLLVDNDVELLQNGEAFFPRLLQDIKEAKHHIHIEYYIYENNEIGKEIADLLKIKAQEGVEVRFIYDDFGSRSIRKNIVKELRANGVQAFAFNKIILLALANRLNYRNHRKIVVIDGQIAYTGGINISDRYDNSRKGENDFFWRDTHIRIEGSGAYGLQHVFLTDWNFCSKENINFSADYFPKIHMGKQKILPLQVIAS... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membra... |
A0A6A2ZD88 | MDPTLTFRRSCREGICGSCAMNINGCNGLACLTKIESGASETTVTPLPHITSCPSYWWNPESYLGPAALLQANRWISDSRDEYTKERLDAINDEFKLYRCHTILNCARACPKGLNPGKQIQHIKQLQLTGGA | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succ... |
A0A0G1E2G9 | MIAMANNLMDLQTISNAARRAGSFFLEKAKTEKFKIAAIGAVFLLVLLGAAGMIWAWWQIYAPLNGEDGQYRDFLVEKGQGVNEIAKKLEDEKIIKSSFWFEVDIWRKKQGSRLQAGKYSLSASLNIAQIGEVITGGKIIPDEINITLPEGFTLRQMRQRIFESGITESMYLGDEQVGRYQLQYKFLADIPAQNDLEGFLFPDTYRFKPDIELGEISKRFLENFDRKVTPVMREEISRQGKTLYQILTMASIIQKEALNESEMGTISGIFWNRLDAKMKLQSDATVNYATGKNIRQVTYSDLEDPSPYNTYKYEGLSPGP... | 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: 369
Sequence Mass (Da): 41714
Location Topology: Single-pass membrane protein
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B9XDM4 | MESPDLSPSSSSAAPNPGMSANGHLPTADSRIRVLVVDDSYFMQRRLAEILHGAPDLRVVGYADNGAEAIRLAEKLSPDVITMDINMSQMDGLQAIDYIMRSNPRPIVIISAYTQKGSRAAFYGLDIGVIDIIEKPSSCGSTSDLLHCTSEIINKVRMAAGVRLASRLHRLSEEGTVPPLDACASERQNQMECALLQNLPDGFPQVIAMGASTGGPTVLQKLLGAVPQEAFPPVVIVQHLPEKFNRELAEHLNAVSSLEVVEAREGQHLTNGTVYIAPGSSYLQINAHGCLTMNEGPRVNYRKPSIDVLFNSLARHHGSQ... | 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... |
A7S8N3 | MAAVTRAFPRLPVVVILGCTGTGKSKLAIEIGKRIGGEIISADSMQVYKGLDIITNKVTTEEMRECKHHMIDFVSPLNEFSVVDFRNMALPLIEEIKGRGKIPIVVGGTNYYIESLLWEILIDNDNKPPENSDVDDDGELQIVDPVMARRIHPNDTRKIARSLQVFEQHGRPHSELLAEQQSKDGGSAYGGPLRFDLTCVFWLHCEKEILNKRLDSRVDAMLDKGLVQELLEFHGSYNKLRQDDNSRYSEGIFQSIGFKEFHNFLVQQQKGDTVNSLIKEEDKKVFDECVEAMKAVTRRYAKKQTMWVKNRFLSRPIGSS... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37.
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 420
Sequence Mass (Da): 47957
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A0A6I1JB19 | KTSAALGMVFRHIGHGIPVAVVQFTKSPDYVTGEAILLRRFPELCTLEIMGDGFTWDTQDRAADIASARAAWDRSKDLIRDDRHGLALLDELNIVLRYDYLPMEEIVDFLRAEKPPGKHVVITGRNAKPELIAIADLVTEMTLVKHPFRAGVKAQTGIEF | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
Function: Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids... |
A0A494WYI1 | MTGEHCARDCAFCAQARSSRGRAHRLSRVIWPPFPAGEVLPRLGDACRAGRIRRACFQVVHSEDYFHRVRQAIAEVRREVDIPLCVSIGLRTVEQVRELLEAGVDVVGLPLDAVTPQLYRDVKGGNWERHLRLLQEAAARFPGRVGTHLIIGLGESEEEAIRLIGELAACGIGVALFAFTPLPGTRLEHHRPPDLRTYRRVQAAHYLLKRGLVRPGGMKFKDGRLVDWGISREELVLYLADGEAFRTTGCPDCNRPYYNERPGKTPYNYPRPLKPREAAEAVGLVVED | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe... |
D7CT15 | MKLFSAHEMRAADQAAADAGIPLLLLMEAAGRAVADAVTRHFAHPEVLVLCGGGNNGGDGYVAARHLLASRRVSVLELSSAPRSDDARTMRRALLAHGLTPRPLEEAALTRALEGRPLVVDALFGSGLTRPLEGEVAAAVARVNASGCEVLSVDVPSGVASDTGELLGPHVRATRTVQLAGAKVASLFHPARAAFGAAEVADIGIPKAILEAHASVTVLSPDGVRAHLPTRAPDTHKYEVGTLLVIAGSATYLGAAEMACRAALRAGAGLVTLASEGSFPGTWPEIIHERLAWDHDPLGTLAELGENRAQVRLIGPGLDR... | 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... |
A0A3S4D7J5 | MMPKNNENDIEQLRATLRHHEYCYHVLDNPEVPDAEYDRLMQRLKALEAEHPELITPDSPTQRVGASPLSAFEQVRHEIPMLSLDNVFDEESYLAFDKRVRDRLKDTQDLTFCCELKLDGLAVSLLYENGSLVQAATRGDGTTGENITANVRTIRAIPLKLRGENIPQRIEIRGEVFMPQKGFEAMNEEARRTGGKVFANPRNAAAGSLRQLDPAVTAKRPLTFFCYGVGVLEGGTLPGSHYDRLQQFKAWGLPVSDRVMRCTGSQAVLDFYHKVEESRPVLGFDIDGVVIKVDSIALQEALGFVSRAPRWATAFKFPAQ... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
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