ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8R3I9 | MRCRKCQLCLSALLTLLGLKVYIEWTSESWLKKAEPRGALPSPTPPNAEPTLPTNLSARLGQTGPLSSAYWNQQQRQLGVLPSTDCQTWGTVAASEILDFILYPQELRRFLLSAACRSFPLWLPAGEGSPVASCSDKDVPYLLLAVKSEPGHFAARQAVRETWGSPVAGTRLLFLLGSPLGMGGPDLRSLVTWESRRYGDLLLWDFLDVPYNRTLKDLLLLTWLSHHCPDVNFVLQVQDDAFVHIPALLEHLQTLPPTWARSLYLGEIFTQAKPLRKPGGPFYVPKTFFEGDYPAYASGGGYVISGRLAPWLLQAAARVA... | Function: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N-glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da):... |
Q17QZ8 | MRRRLRLRREALLTLLLGATLGLLLYAQQEGAAPTTSAPRAQGRAAPGPTPGLRVFQAPDTGAAPPAYEGDTPEPPTPTGPFDFGRYLRAKDQRRFPLLINQPHKCQGNGAFPRGPDLLIAVKSVAADFERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGTGTVAGEAEAGTQTHWSALLRAESRAYADILLWAFDDTFFNLTLKEIHFLAWASDYCPDVRFVFKGDADVFVHVGNLLEFLAPRDPAQDLLAGDVIVQARPIRVRASKYYIPEAVYGLPAYPAYAGGGGFVLSGATLRRLAGACAQVELFPIDDVFLGM... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43876
Sequence Length: 401
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q6UX72 | MRRRLRLRRDALLTLLLGASLGLLLYAQRDGAAPTASAPRGRGRAAPRPTPGPRAFQLPDAGAAPPAYEGDTPAPPTPTGPFDFARYLRAKDQRRFPLLINQPHKCRGDGAPGGRPDLLIAVKSVAEDFERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGAGSGGADEVGEGARTHWRALLRAESLAYADILLWAFDDTFFNLTLKEIHFLAWASAFCPDVRFVFKGDADVFVNVGNLLEFLAPRDPAQDLLAGDVIVHARPIRTRASKYYIPEAVYGLPAYPAYAGGGGFVLSGATLHRLAGACAQVELFPIDDVFLG... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43751
Sequence Length: 402
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q8VI16 | MRRRRRPRLCPDAWLTLLLSAALGLLLYAQRDVASPTTRPPARGPQLPRPTPSLRARELPNTARAAPLAYEGDTPVPPTPTDPFDFGGYLRAKDQRRFPLLINQRRKCRSDGASGGSPDLLIAVKSVAADFERREAVRQTWGAEGRVQGALVRRVFLLGVPKGAGSGGAGTRSHWRTLLEAESRAYADILLWAFEDTFFNLTLKEIHFLSWASAFCPDVHFVFKGDADVFVHVRNLLQFLELRDPAQDLLAGDVIVQARPIRARASKYFIPRAVYGLPVYPAYAGGGGFVLSGATLRRLADACSQVELFPIDDVFLGMCL... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44231
Sequence Length: 399
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q9SAA4 | MSFKNRGDYNFTPRNVVSRNSVFFMCLASFCLGMFFTNRMWNIVPEARGISRLSKLSLSSSDCDKKNVLDYGNNTIGILDKSISNLEMKLVAARAERESLSGKFNISNEAKKRKYFMVIGINTAFSSRKRRDSVRSTWMPQGENLKKLEEEKGIIVRFVIGHSVLSHGILDKAIEAEEKTHGDFLRLEHTEGYMKLSAKTKTFFATAVSLWDAEFYIKVDDDVHVNLASLKKALSAHQNKPRVYVGCMKSGPVLARKSVKYHEPEYWKFGEVGNKYFRHATGQFYAISKDLATYILINQDLLHKYANEDVSLGSWFIGLN... | Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43622
Sequence Length: 384
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi ap... |
Q9Y5Z6 | MASKVSCLYVLTVVCWASALWYLSITRPTSSYTGSKPFSHLTVARKNFTFGNIRTRPINPHSFEFLINEPNKCEKNIPFLVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSKAKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGGPIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVAELIYKTSLHTRLLHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQISPEEMHRIWNDMSS... | Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-alpha-D-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylg... |
P39641 | MERKTVLVIADLGGCPPHMFYKSAAEKYNLVSFIPRPFAITASHAALIEKYSVAVIKDKDYFKSLADFEHPDSIYWAHEDHNKPEEEVVEQIVKVAEMFGADAITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAEDEFNRVNDYLKSINVPKAVTFEAPFIAEEFLQGEYGDWYQTEGYSDYISIEGIMADGEYFPIAIHDKTPQIGFTETSHITPSILDEEAKKKIVEAAKKANEGLGLQNCATHTEIKLMKNREP... | Cofactor: Binds 2 Mg(2+) ions per monomer.
Function: Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the formation of alpha-dipeptides from various L-amino acids in the presence of ATP. In vivo cataly... |
P56817 | MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPD... | Function: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragme... |
Q9Y5Z0 | MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGLALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVV... | Function: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. It ... |
P39642 | MKQLKPNSKYLLYGQALSFMGDYCVLPALLILSTYYHDYWVTSGVIVVRSIPMVFQPFLGVLVDRLDRIKIMLWTDIIRGIIFLGLTFLPKGEYPLIFLALLFITYGSGVFFNPARLAVMSSLESDIKSINTLFAKATTISIIVGAAAGGLFLLGGSVELAVAFNGVTYLVSAFFISRIKLQFVPIQSENIKEAFQSFKEGLKEIKTNSFVLNAMFTMITMALLWGVVYSYFPIVSRFLGDGEIGNFILTFCIGFGGFIGAALVSKWGFNNNRGLTYFTVLSIVSLALFLFTPIFAVSVIAAILFFIAMEYGEVLAKVKV... | Function: Part of the bacilysin biosynthesis operon. May be involved in self-resistance to bacilysin by permitting efflux of this antibiotic.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43417
Sequence Length: 394
Subcellular Location: Cell membrane
|
W8W138 | MHFSLPTSRIVVVVPAAAICIVCVLIETCTAARSHVYTIPLRKGKETSFAETVGEPVRTNQVNVSVEEQKNNIRGRPGLGYYIEVDIGTPPQKLNVLIDTGSSNFAVAASSHNAISTYYRRNESSTYEDQGTYVKVPYTQGEWSGDLGQDLVQIASLGNQSFQANIAAITESKMFFLNDSRWQGILGLGYAEIARPDSSVEPFFDSLTSQTSIQDIFALQMCGALASTNDTNLGSSADGPVEEVIGSMNIGGLDASLYHGTMQYAPLRDEWFYEVIMTDIRVGNDSLGLDCKEYNFDKTIVDSGTTNLRLPVRVFEAITN... | Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 59336
Sequence Length: 540
Subcellular Location: Membrane
EC: 3.4.23.-
|
P39643 | MEITPSDVIKTLPRQEFSLVFQKVKEMEKTGAHIINLGQGNPDLPTPPHIVEALREASLNPSFHGYGPFRGYPFLKEAIAAFYKREYGVTINPETEVALFGGGKAGLYVLTQCLLNPGDIALVPNPGYPEYLSGITMARAELYEMPLYEENGYLPDFEKIDPAVLEKAKLMFLNYPNNPTGAVADAAFYAKAAAFAKEHNIHLIHDFAYGAFEFDQKPASFLEAEDAKTVGAELYSFSKTFNMAGWRMAFAVGNEKIIQAVNEFQDHVFVGMFGGLQQAASAALSGDPEHTESLKRIYKERIDFFTALCEKELGWKMEKP... | Function: Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase . Catalyzes the reductive amination of the C2 ket... |
P39644 | MSKRTAFVMGASQGIGKAIALKLADQHFSLVINSRNLDNIESVKEDILAKHPEASVIVLAGDMSDQHTRAGIFQKIESQCGRLDVLINNIPGGAPDTFDNCNIEDMTATFTQKTVAYIDAIKRASSLMKQNEFGRIINIVGNLWKEPGANMFTNSMMNAALINASKNISIQLAPHNITVNCLNPGFIATDRYHQFVENVMKKNSISKQKAEEQIASGIPMKRVGSAEETAALAAFLASEEASYITGQQISADGGSMKSI | Function: Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase . BacG catalyzes the stereoselective redu... |
O14867 | MSLSENSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKFKFLDSTADQQECPRKKCFSSHCQKTDLKLSLLDQRDLETDEVEEFLENKNVQTPQCKLRRYQGNAKASPPLQDSASQTYESMCLEKDAALALPSLCPKYRKFQKAFGTDRVRTGESSVKDIHASVQPNERSENECLGGVPECRDLQVMLKCDESKLAMEPEETKKDPASQCPTEKSEVTPFPHNSSIDPHGL... | Function: Transcriptional regulator that acts as repressor or activator, depending on the context. Binds to NF-E2 DNA binding sites. Plays important roles in coordinating transcription activation and repression by MAFK (By similarity). Together with MAF, represses the transcription of genes under the control of the NFE... |
Q9BYV9 | MSVDEKPDSPMYVYESTVHCTNILLGLNDQRKKDILCDVTLIVERKEFRAHRAVLAACSEYFWQALVGQTKNDLVVSLPEEVTARGFGPLLQFAYTAKLLLSRENIREVIRCAEFLRMHNLEDSCFSFLQTQLLNSEDGLFVCRKDAACQRPHEDCENSAGEEEDEEEETMDSETAKMACPRDQMLPEPISFEAAAIPVAEKEEALLPEPDVPTDTKESSEKDALTQYPRYKKYQLACTKNVYNASSHSTSGFASTFREDNSSNSLKPGLARGQIKSEPPSEENEEESITLCLSGDEPDAKDRAGDVEMDRKQPSPAPTP... | Function: Transcriptional regulator that acts as repressor or activator (By similarity). Binds to Maf recognition elements (MARE) (By similarity). Plays an important role in coordinating transcription activation and repression by MAFK (By similarity). Induces apoptosis in response to oxidative stress through repression... |
Q6ZUV0 | MIKEAGAIISTRHCNPQNGDRCVAALARVECTHFLWPMCIGEVAHVSAEITYTSKHSVEVQVNMMSENILTGAKKLTNKATLWYAPLSLTNVDKVLEEPPVVYFRQEQEEEGQKRYKTQKLERMETNWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHSFVHEGVTMKVMDEVAGILAARHCKTNLVTASMEAINFDNKIRKGCIKTISGRMTFTSNKSVEIEVLVDADCVVDSSQKRYRAASVFT | Function: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH.
Catalytic Activity: H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate
Sequ... |
Q941L2 | MIYFGRSIDNHYTTMMTKTLEIDLRSAEGLKLNRRPIKKKTFAVVKIDEKCRKSNLDESRRSNPTWNYKSEMPINGNEQFIFIEVFYRTGSGHDKKIGEAKIPTNDFMGRYSPEGHLNFLSYRLRDEFGDKCGIVNLSILVKSDPTRDYGACSSQAAVTGLWRPRLETASIDGYGGRTVTGVPVWGLYQRQF | Function: Negative regulator of cell death and defense responses. Exhibits calcium-dependent phospholipid binding properties.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21992
Sequence Length: 192
Subcellular Location: Membrane
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A2VDM8 | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGIKYEARLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPLALETSRAPVASESTHTDGVEEVAGSCPQAPTHSPPSKPKLVVKP... | Function: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitina... |
Q92560 | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSSVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYEARLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKSASNKSPLVLEANRAPAASEGNHTDGAEEAAGSC... | Function: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1 . Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) . Does not deubiquitinate monoubiquiti... |
Q99PU7 | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYETRLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPLGLEAGRTPVASECTQTDGAEEVAGSC... | Function: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitina... |
D3ZHS6 | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNSMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRVKYEARLHVLKGNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPFGLEAGRTPAASECTHTDGAEEVAGSC... | Function: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitina... |
Q32KL9 | MTLQWTAVATFLYAEIGLILIFCLPFIPPQRWQKIFSFSVWGKIASFWNKAFLTIIILLIVLFLDAVREVRKYSSTHTIEKSSASRPAAYEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAKELSHKGVLKHQAENINQAAKKFMEENERLKRLLKNYGKEEEHILEAENKKLEEDKEKLKTELKKASDALSKAQNDVMIMKMQSERLSKEYDRLLREHSELQDRAGKDKKCL | Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28212
Sequence Length: 240
Subcellular Location: Endoplasmic reticulum memb... |
Q9UHQ4 | MTLQWAAVATFLYAEIGLILIFCLPFIPPQRWQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIEKSSTSRPDAYEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQDRLERGNKKRL | Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28320
Sequence Length: 241
Subcellular Location: Endoplasmic reticulum memb... |
Q61334 | MTIQWAAVASFLYAEIGLILLFCLPFIPPQRWQKIFSFSVWGKIASFWNKAFLTIIILLIILFLDAVREVRKYSSTNVVEKNSAIRPSAFEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAKEIANKGVLKIQAENTNKAAKKFMEENEKLKLGLRNDNAEEHLLEAENKKLIESKENLKTELKKASDALLKAQNDVMTMKIQSERLSKEYDRLLKEHSELQNRLEKEKKKGL | Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27964
Sequence Length: 240
Subcellular Location: Endoplasmic reticulum memb... |
Q9R9H8 | MEYAAIHHQPFSTDAYSYDGRTVHIKIRTKKGDADHIRFIWGDPYEYNDGKWSANEQPMRKIAATEMHDYWFAEVVPPFRRLQYAFVVTDDHEDIFFGSSGVCPYNEKTLETIHYYFKFPFVHEADTFQAPEWVKSTVWYQIFPERFANGREDLSPKNALPWGSKDPGVNDFFGGDLQGIVDKLDYLEDLGVNGIYLTPIFSAPSNHKYDTLDYFSIDPHFGDPEIFRTLVSQLHQRGMRIMLDAVFNHIGSASPQWQDVVKNGDQSRYKDWFHIHSFPVTDDNYDRFAFTADMPKLNTANPEVQKYLLDIALYWIREFD... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Hydrolyzes beta-cyclodextrin to maltose and glucose, soluble starch to maltose and glucose, and pullulan to panose with trace amounts of maltose and glucose. It is also able to hydrolyze acarbose. Can also exhibit a transglycosylation activity transferring glucose or ... |
P54690 | MAYLSRATATLARQDCSNGCSASYAEEEELEASTESYDEEGGSEASTQTFRAKDLIITKADVLKKKPDPSSLVFGASFTDHMLMVEWTSKYGWDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQLDREWVPYSTSASLYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNGTFSPVSLWANPKFVRSWKGGTGDFKMGCNYGSSLLAQCEAAENGCHQVLWLYGKENRITEVGTMNLFLYWINKDGEEELATPPLDGVILPGVTRQSIL... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
PTM: The N-terminus is blocked.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 46046
Sequence Length: 411
Subcellular Locatio... |
Q9GKM4 | MDCNNGCSAEGTGEGGSKEPVETFKAEDLIITRATILKEKPDPSTLVFGTVFTDHMLTVEWSLELGWEKPRIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFRPNLNMDRMYRSAMRATLPAFDKKELLECIQQLVKLDEEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVILSPVGPYFSSGSFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVENACQQVLWLYGEENQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVMRQSILDLAHKWGEFKVSERYLTMDDLTTAVE... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 43073
Sequence Length: 385
Subcellular Location: Cytoplasm
EC: 2.6.1.42
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Q9M439 | MIKTITSLRKTLVLPLHLHIRTLQTFAKYNAQAASALREERKKPLYQNGDDVYADLDWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEGMAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVH... | Function: Converts 2-oxo acids to branched-chain amino acids. Shows activity with L-Leu, L-Ile and L-Val as amino donors and 2-oxoglutarate as an amino acceptor, but no activity for D-isomers of Leu, Ile, Val, Asp, Glu or Ala.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Seque... |
O15382 | MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITM... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine . May also function as a transporter of branched chain alpha-keto acids (By similarity).
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence M... |
K7QHS5 | MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRK... | Function: Converts 2-oxo acids to branched-chain amino acids. Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA biosynthesis.
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 44520
Sequence Length:... |
O35854 | MSAAILGQVWTRKLLPIPWRLCVPGRCVSSNFKAADLQVQVTREPQKKPAPSQPLLFGKTFTDHMLMVEWNSKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQKKGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGELELATPPLDGIILPGVVRQSLLDLARTWGEFRVAERKVT... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine . May also function as a transporter of branched chain alpha-keto acids .
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 44276... |
Q9M401 | MERAAILPSVNQNYLLCPSRAFSTRLHSSTRNLSPPSFASIKLQHSSSSVSSNGGISLTRCNAVSSNSSSTLVTELADIDWDTVGFGLKPADYMYVMKCNIDGEFSKGELQRFGNIEISPSAGVLNYGQGLFEGLKAYRKKDGNNILLFRPEENAKRMRNGAERMCMPAPTVEQFVEAVTETVLANKRWVPPPGKGSLYVRPLLMGTGAVLGLAPAPEYTFIIYVSPVGNYFKEGVAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCIYKRYLEEVSSCNIFIVKDNVISTPEIKGTILP... | Function: Converts 2-oxo acids to branched-chain amino acids. Acts on leucine, isoleucine and valine. Also involved in methionine chain elongation cycle of aliphatic glucosinolate formation. Catalyzes the conversion of 5-methylthiopentyl-2-oxo and 6-methylthiohexyl-2-oxo acids to their respective Met derivatives, homom... |
Q9LE06 | MAPSAQPLPVSVSDEKYANVKWEELAFKFVRTDYMYVAKCNHGESFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGTLYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHKDNSGLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVTFKDKKTGFKTG... | Function: Converts 2-oxo acids to branched-chain amino acids. Shows activity with L-Leu, L-Ile and L-Val as amino donors and alpha-keto-glutarate as an amino acceptor, but no activity for D-isomers of Leu, Ile, Val, Asp, Glu or Ala. Acts on methionine and its derivatives and the corresponding 2-oxo acids. Catalyzes the... |
Q9LPM9 | MAPSSSPLRTTSETDEKYANVKWEELGFALTPIDYMYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRT... | Function: Converts 2-oxo acids to branched-chain amino acids. Acts on leucine, isoleucine and valine (By similarity).
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 38861
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isol... |
P54688 | MPAILSRVAPRTFNLVGSRLMASAARLETVPREEIHKEYDRKKTFYHRDLEIQLAGPTQLKTKPLDPTKLKFGHTYADYMMTCDWDAERGWHHPKIEPIGELKIHPGAKVLHYASELFEGMKAYRGIDNKIRMFRPEMNMARMKRTALRAALPDFDSEEMINVLTELLRLDQEWVPNSDVCSLYLRPTLIGTDPTLGVGCATEAKMFVITGPVGAYYSTGFQPVSLLADSRFIRAFPGGVGAYKMGCNYAPTIWVGKEAASKNCQQVLWLYGENEDLTEVGTMNIFLFWKNEEGDMELITPPLHRGLILPGVTRDSLLEL... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 47342
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 2.6.1.42
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Q54N47 | MFGRFIRQYSTSKNIINVNELIVEKTKTPFQKYTDKTKLVFGKQFSDHMIEVQWTKEEGWGVPKISGYHNLSIPPSASVLHYALECFEGMKAYKDSNGKIRLFRPDQNMNRFLNSAKRICLPEFNKEAVIELIKKLCVLDKDWIPEGKGYSLYLRPTLIATQNSLGVGASNSALMFVIASPVGPYYPEGFKPVKLIADDQYVRAWAGGSGAFKLGSNYAPTIFPQLEAAKKGFSQVLWLLNDYVTEVGTMNMFVFWNNAQGEKELITPPLGDGTILPGVTRDSILKLTQQWGEFKITEKNFTMTELAKAIKEGRVFEAFG... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 42244
Sequence Length: 378
EC: 2.6.1.42
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A9UZ24 | MAAALRLTPHMRQAYPVVAAPSVARLSTLDASKLTIETTTQPRERVEKTKLVFGHTFSDHMLKCKWDVNEGWAAPTISPYANLSLAPSSIVLHYAIECFEGMKAFRGDDDRIRLFRPNLNMDRLHRSSVRLALPDFDQDELLKCITELVIKDKDWIPAGRGYSLYLRPTHIGTAEYLGVGKSSSSLLFCINSPSGAYYSTGFKPVSLLADPAYVRAWPGGVGNTKGGCNYAPSIYPQSQAQAQGCQQVLWLFGEDHEVTEVGTMNLFMYWKNEQGEDELITPPLDGTILPGVTRQSIVDMARGWNEFKVSERKFNMGQVS... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 43290
Sequence Length: 390
EC: 2.6.1.42
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A7SLW1 | MAARVGLLQTIGKLQSSFLYRAWPKHSINAKQLARQLSSYHDIKSSNLLIEKTNKPKPKPDPNTLVFGKEFTDHALILKWSDEDGWDNPQIIPYGNLSLPPAASALHYGLECFEGMKAYRGDDGKIRMFRPLMNMKRMNNSAARACLPTFNSGEMVECIRKLIHLEREWVPHSNTCSLYIRPTMIGTQASLGVNKANSAMLFVILSPVGPYFRTGTFNPVALLADPQYVRAWPGGVGDCKMGGNYAPTILAQQNAERQGLQQVLWLFGEDHQITEVGTMNMFMFWINENGEKELVTPPLNGLILPGVTRDSLLALAKRWG... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 45659
Sequence Length: 405
EC: 2.6.1.42
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Q9F716 | MPVSSDCQILKEDNVTHSFCGLACVGWLYQKIKDSFFLILGTHTCAHFLQNALGMMIFAKPRFGVALIEEADLSRAEPQLEAVIEEIKRDHNPSVIFLLSSCTPEVMKVDFKGLAHHLSTDKTPVLFVPASGLVFNFTQAEDSVLQALVPFCPEAPAGEKKVVFVGSVNDITADDLRTEAEQLGIPVGGFLPESRFDKLPAIGPDTVLAPIQPYLSRVCSRLNRERGSQVLTSLFPFGPDGTKTFWEDLAAMFGIKVDLSDRAEAAWEKIKPQTDLLKGKKIFLTADTMMELPLARFLKNAGAEVVECSSAYINKKFHAR... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophy... |
B0TBM7 | MEGIERENGCFHTFCPIASVAWLHRKIKDSFFLIVGTHTCAHFIQTALDVMVYAHSRFGFAVLEESDLVAASPTAELAKVVEDIKAEWQPKVIFLLSTCSCDILKLDLENSSKDLTIRFGFPVVPVQTSGLDRTFTQGEDAVLHALLPFVPKEDPKVAVVEEKKRSWFSFGKDEGNKASVPAAPTRNLVLVGAVTDSTTQQLQWELKQLGLERVDVFPSGDITNMPVINEHTVIVPLQPYLSDTLATLRRERGAKVLTTLLPIGPDGTARFLEAICAEFGLDASPVAEREAQTWRSLESQRALLRGKRIMFLGDNLLEIP... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophy... |
P26164 | MSLDSPTFGCTDSPVRRERGQKAVFCGLTSIVWLHRKMQDAFFLVVGSRTCAHLLQAAAGVMIFAEPRFGTAVLEEQDLAGLADAHKELDREVAKLLERRPDIRQLFLVGSCPSEVLKLDLDRAAERLSGLHAPHVRVYSYTGSGLDTTFTQGEDTCLAAMVPTLDTTEAAELIVVGALPDVVEDQCLSLLTQLGVGPVRMLPARRSDIEPAVGPNTRFILAQPFLGETTGALERRGAKRIAAPFPFGEEGTTLWLKAVADAYGVSAEKFEAVTAAPRARAKKAIAAHLETLTGKSLFMFPDSQLEIPLARFLARECGMK... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer . The cluster is bound at the heterodimer interface by residues from both subunits .
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorop... |
P37652 | MKRKLFWICAVAMGMSAFPSFMTQATPATQPLINAEPAVAAQTEQNPQVGQVMPGVQGADAPVVAQNGPSRDVKLTFAQIAPPPGSMVLRGINPNGSIEFGMRSDEVVTKAMLNLEYTPSPSLLPVQSQLKVYLNDELMGVLPVTKEQLGKKTLAQMPINPLFISDFNRVRLEFVGHYQDVCEKPASTTLWLDVGRSSGLDLTYQTLNVKNDLSHFPVPFFDPSDNRTNTLPMVFAGAPDVGLQQASAIVASWFGSRSGWRGQNFPVLYNQLPDRNAIVFATNDKRPDFLRDHPAVKAPVIEMINHPQNPYVKLLVVFGR... | Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86024
Sequence Length: 779
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
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P58934 | MTSNIFARPHPRRALALMIASLMGFNTLAQAAEQAVATVPVQSTDTGYSLTLKQLGRRDTMNLQGVESSDSVNFDIRADEVVKGAQLLLKYSYSPALLADLSQINVLVNGEVAASLPLPKEGAGTPQEQLVQIPAHLITEFNRLSLQFIGHYTMSCEDPLHSSLWAKISNSSELKVQVEPIVLKDDLAVLPLPFFDKRDARQVSLPFVFATAPDSAALEAAGALSSWIGGLASYRGATFPTTLGELPAKGNAIVLVQTADAMDIHGVAVAKPAGPTLTLIANPNDANGKLLIVTGRDGAELKRAANAVVLGNPVLAGNSV... | Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 81763
Sequence Length: 755
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
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P58933 | MRGVSVCFTRTQLMRMFPAVLSCALTLLAGLAQAQQPMPATPSAQAGSQMQAATPSQVPVAFAAAPLPGGSTRAATLRELGIDYEITLRGVQGSAGVPFSVRSDEIVTAATLNLKYSYSPSLLPDLSHLKVTINGVTVATLPTDKANAGKLLSADLPIDPRLVTDYNQLNLQLIGHYTRDCEDPDHSSLWANVDAATSLSLTTTPLALANNLALLPVPFFDMRDTRRLELPFYFPQRPDTATLQAAGTVASWFGSLAGYRGAVFPASTEALPASGNAVVFATPGTLPAQFATADSGVADIRGPTVAVLANPNDRNGKLLL... | Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85170
Sequence Length: 788
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
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Q5ZJZ5 | MLATKLSRPLLNLPVKTLTVKNPGNSFRPVQRFCFPLLSSCGSRSYASEVDQIGSRAVLTLGLDLPWPKHLHTKGFIIYAGCLQKNKGEGGSKDLDNMNSDRMRTVQLNVCDSKEVDRAVEHVNSSLEDPEKGLWGLVNNAGISTFGEVEFTSMDTYMEVAEVNLWGTVRTTKAFLPLIRRSKGRVVNISSMMGRMGSPARSPYCITKFGVEAFSDCLRYEMQPQGVMVSIVEPGNFIAVTNLYSPERIKAIADKMWDELPEIVRKDYGRKYFDEQVSKMETYCNSGSTDTSPVIESVAHALTSTAPYTRYHPMDYYWWL... | Catalytic Activity: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH
Sequence Mass (Da): 38237
Sequence Length: 339
Subcellular Location: Mitochondrion inner membrane
EC: 1.1.1.30
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Q02338 | MLATRLSRPLSRLPGKTLSACDRENGARRPLLLGSTSFIPIGRRTYASAAEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTDTSPVIDAVTHALTATTPYTRYHPMDY... | Catalytic Activity: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH
Sequence Mass (Da): 38157
Sequence Length: 343
Subcellular Location: Mitochondrion inner membrane
EC: 1.1.1.30
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K4N0V2 | MASTVLRRLEGKVALITGAASGIGESAARLFSRHGAKVVIADIQDELALNICKDLGSTFVHCDVTKEFDVETAVNTAVSTYGKLDIMLNNAGISGAPKYKISNTQLSDFKRVVDVNLVGVFLGTKHAARVMIPNRSGSIISTASAATAAAAGTPYPYICSKHGVVGLTRNAAVEMGGHGIRVNCVSPYYVATPMTRDDDWIQGCFSNLKGAVLTAEDVAEAALYLASDESKYVSGHNLLVDGGVSIMNQGCNMFDLMDS | Function: Involved in the biosynthesis of monoterpenes natural products related to camphor . Catalyzes the conversion of borneol into camphor .
Catalytic Activity: borneol + NAD(+) = camphor + H(+) + NADH
Sequence Mass (Da): 27270
Sequence Length: 259
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
... |
P86198 | AVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLLKEVAEVNLWGTVRSFLPLLRRVVNISSMLGRSPYCITKFGVEAFSDCLRYEMHPLGVKVSVVEPGNFIAATSLYSPERMWDELPEVVRKYHPMDYYWWLR | Catalytic Activity: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH
Sequence Mass (Da): 15007
Sequence Length: 132
Subcellular Location: Mitochondrion inner membrane
EC: 1.1.1.30
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Q5FA46 | MKAARFYNKGDIRIEDIPEPTVAPGTVGINVAWCGICGTDLHEFMEGPIFIPPCGHPHPISGESAPVTMGHEFSGVVYAVGEGVDDIKVGQHVVVEPYIIRDDVPTGEGSNYHLSKDMNFIGLGGCGGGLSEKIAVKRRWVHPISDKIPLDQAALIEPLSVGHHAYVRSGAKAGDVALVGGAGPIGLLLAAVLKAKGIKVIITELSKARKDKARESGVADYILDPSEVDVVEEVKKLTNGEGVDVAFECTSVNKVLDTLVEACKPAANLVIVSIWSHPATVNVHSVVMKELDVRGTIAYCNDHAETIKLVEEGKINLEPF... | Cofactor: Binds 1 Zn(2+) per subunit.
Function: NAD-dependent butanediol dehydrogenase which catalyzes the oxidation of (R,R)-butane-2,3-diol to (3R)-acetoin and of meso-butane-2,3-diol to (3S)-acetoin . Preferentially oxidizes (R,R)-butane-2,3-diol, with a catalytic efficiency approximately fourfold higher than with m... |
P29147 | MLAARLSRPLSQLPGKALSVCDRENGTRHTLLFYPASFSPDTRRTYTSQADAASGKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLLKDKGDAGVRELDSLKSDRLRTIQLNVCNSEEVEKAVETVRSGLKDPEKGMWGLVNNAGISTFGEVEFTSMETYKEVAEVNLWGTVRTTKSFLPLLRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMHPLGVKVSVVEPGNFIAATSLYSPERIQAIAKKMWDELPEVVRKDYGKKYFDEKIAKMETYCNSGSTDTSSVINAVTHALTAATPYTRYHPMDY... | Catalytic Activity: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH
Sequence Mass (Da): 38202
Sequence Length: 343
Subcellular Location: Mitochondrion inner membrane
EC: 1.1.1.30
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P0C742 | MVDEQVAVEHGTVSHTISREEDGVVHERRVLASGERVEVFYKAPAPRPREGRASTFHDFTVPAAAAVPGPEPEPEPHPPMPIHANGGGETKTNTQDQNQNQTTRTRTNAKAEERTAEMDDTMASSGGQRGAPISADLLSLSSLTGRMAAMAPSWMKSEVCGERMRFKEDVYDGEAETLAEPPRCFMLSFVFIYYCCYLAFLALLAFGFNPLFLPSFMPVGAKVLRGKGRDFGVPLSYGCPTNPFCKVYTLIPAVVINNVTYYPNNTDSHGGHGGFEAAALHVAALFESGCPNLQAVTNRNRTFNVTRASGRVERRLVQDM... | Function: Rearranges cellular actin to increase intercellular contacts and thereby promote virus cell-to-cell spreading. Induce the outgrowth of long, branched plasma membrane fronds to create intercellular network for virion traffic. The fronds are actin based and RhoA-dependent (By similarity).
Location Topology: Sin... |
B2IZD3 | MVNQVATDRFIQDLERVAQVRSEMSVCLNKLAETINKAELAGDSSSGKLSLERDIEDITIASKNLQQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFPKFMDSLN... | Function: Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangement, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bi... |
Q9U4G1 | MPAKRSRTFRQSGSALLALLAIILLMNISCTSAARDHRRQTNLEAKVGSHVVFNCYIDFPFDAPIPYLVHWTKDNKKIFTWYEQETSTSELFNGRLHLVENHPEFGRASVNLTAIRESDQGWYHCQVSFPNRSPSVRNNGTAYHLAVQGGSLIRIPPVNQTIREGQTAFFHCVMKHPENSQASWYKDGVLLQEVQDLVRRFYMGPDGSLSIDPTMMSDLGEYECKVRNSDGELQTAKAFLNIQYKAKVIYAPPEVFLPYGQPAVLDCHFRANPPLKNLRWEKDGLLFDSYNVPGVFYKMNGSLFFAKVDENHAGSYTCTP... | Function: In the developing eye, has a role in axonal targeting of the R7 photoreceptor where it functions together with tutl. Probably mediates homotypic cell adhesion; the effect is inhibited by Lar.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 81213
Sequence Length: 719
Subcellular Location: C... |
P07772 | MNSTQRFEHKVVIVTGAAQGIGRGVALRIAQEGGCLILADRSDLIQAVLAEIKALGALAIAVETDLETYAGAELVVSHAIAEYGRIDVLINNVGGAIWMKPFQEFSEEEIIQEVHRSLFPALWCCRAVLPEMLKHQQGTIVNVSSIATRGIHRIPYSASKGGVNALTASLAFEHAQHGIRVNAVATGGTKAPPRKIPRNAQPLSKSEQVWMQQVVDQTIDRSFLGRYGSIDEQVNAITFLASDESSYITGSVLPVGGGDQG | Function: Degradation of 2-hydro-1,2-dihydroxy benzoate (DHB) to catechol.
Catalytic Activity: (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD(+) = catechol + CO2 + NADH
Sequence Mass (Da): 27982
Sequence Length: 261
Pathway: Aromatic compound metabolism; benzoate degradation via hydroxylation; catechol fr... |
P07775 | MTTLLKTLKQDWSLSATIAGFLAVLISYSGPLIIFFQAAQKAHVSTEMMISWIWAISIGAAVTGIFLSIRFKTPVVTAWSAPGTALLVTLFPNISLNEAVAAYITAAIVIFLVGITGYFDKLLKWIPQGIAAGMMAGILFQFGLGLFLATDTLPLIVFSMLLCYLISRRFSPRYCMLWVLICGVAFSFFLGKMNPVPLDFQIARPQFIAPEWSWFSTLNLALPLILVSLTGQFLPGMAILKLSGYNTPAKPIIAAASLASLFAAFAGGITIVLASITATLCMGKDAHELKDKRYIAGIANGLFYVLGGVFAGSIVALFSL... | Function: Probably involved in the transport of benzoate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42289
Sequence Length: 394
Subcellular Location: Cell membrane
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O30513 | MSREINVNQMIDDSKLTPFHWRVIILSTLIIIFDGYDLVIYGVALPLLMKEWAIDPVTAGFIGSIALFGMMFGALIFGTIADKLEHLGVSRKKVIAVCIILFSLCTVLCGFSETTTQFSIFRFLAGVGIGGVMPNVIALVSEYAPKKFKSFFVTLMFSGYAIGGMTAAFLGSILVPLYGWKIMFMIAGIPLVLLLPLMKVLPESIDYLVRKKKDETVRFIMTKMVPSYQYQPDHVFVLNSSNQNQAQAPVKMIFQEQRAFSTMMFWCSIFMTLIMVYALGNWLPKLMIEAGYNLSKSLIFLFSLNVGGMIGSILGGYLAD... | Function: Probable uptake of benzoate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51403
Sequence Length: 466
Subcellular Location: Cell inner membrane
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P9WEU7 | MSAVEIPHPSGCRVYDIRQQAQGSMNLQTAITDGLLSTPKTLPSLLLWDAEGLRLFDEFAHSASYYLRDKELTILRDRSHEIVTVVPAQSILVELGSLQKTGRLIRALEKQQKPVRYYAVDVSLSGLTNSLTELRKELGDLHFVDITGLLGTYDDCVNWISNPSGQDPMSSPTVTFLWMGNSISNLNHYIDSSSLLSQFRLACDASRLRCQFLIAADACQDAQVVRTAYDAQNPTLRAFLLNGLSHANSVLGRAAFSPQDWSCESGFYPEQGQLEVYYVPLRDVELDVGGDRVYRVQRGERVRAISSGKWGKKLMGRVAC... | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of benzomalvin A and D . The pathway begins with the loading of amino acid precursors onto the A domains of the non ribosomal peptide synthetases benY and benZ . BenY and the A1 domain of benZ are loaded with anthranilate (Anth), whi... |
Q6G2A9 | MPKAKAKTKNTEIISPHHYVYPNTTTLKNKYGIKNLNAFLEKCSHDTAKAMINLREESLPEYFDTAYLCHIHQQLFKNTFEWAGYLRHIPFTFADGTTAAMPEMKRTGWKNAFAIGDEIQEGLQRLDQTLAEKNNLQGLTREEFNSEAIELFNSLNQLHPFREGNGRTQRLFFENLAKAAGHQLNFSLITKERMMVASVAVAENGDLEPMQHLFEDISNPEKIRLLKEFMHTMKNTGRNVNDRPVMVAKEGETYTGTYRGAGLEGFALNVKGAYIIGNIDHLPPEQLKILKPGDKITFTAPKAEELKKTLIPKETLVPLT... | Function: Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host target proteins.
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 61341
Sequence Length: 544
Domain: The fido... |
P66948 | MFRQLKKNLVATLIAAMTIGQVAPAFADSADTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRSAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARNRANQMRPMVVQSSEDFYLAKARTLGMYNSGRNQLTSDLLDEWAKGNVRQQRAAQYGRALQAM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its bioge... |
Q9KQ40 | MKFFPTRTLLCLCIAAPCLPAIAQNDPIELPDIGTVAGSTLTIDQELIYGDAYMRMLRNNQPVINDPVLNEYIDNLGHRLVASANDVKTPFTFFMIRDRNINAFAFFGGYVALHSGLFLHAQSESELASVMAHEIAHVTQRHLARSMEEQARRSPATIAALAGSLLLAIAAPEAGIAAINATMAGSIQGQINYTRSNEKEADRFGIATLAKAGFDANAMPQFFTRLADEYRYASKPPPMLLTHPLPEDRITDSRERARQYPPLKLAPHLDYHLARARIIARYAGIDADAALDWFARSEKKIDATLQPSIQYGKALVYLDL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
Sequence Mass (Da): 54104
Sequence Length: 484
Subcellula... |
Q3J4E9 | MRAQPAASHFVDGRPLEDETGAPIPVIYPATGEEIARLHEATPAVIEAALASGARAQAAWAAMRPVERARILRRASDLIRAHNEELSLLETLDTGKPLQETLVADWASGADALEFFAGLAPVVTGETVPLGQDFVYTIREPLGLCVGIGAWNYPSQIACWKAAPALALGNAMVFKPSEVTPLGALKLAEILIEAGLPPGLFNVVQGRGAVGASLVTDSRVAKVSLTGSVPTGRRVYAAAAEGVRHVTMELGGKSPLIVFDDADLESAIGAAMLGNFYSAGQICSNGTRVFVQKGIKEAFLARLAERADAIRMGDPLDPEV... | Cofactor: Binds 2 potassium ions per subunit.
Function: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.
Catalytic Activity: betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH
Sequence Mass (Da): 50804
... |
P56998 | MQGNQAVVDYMNELLSGELAARDQYFIHSRLYSEWGYTKLFERLNHEMEEETTHAEDFIRRILMLGGTPKMARAELNIGTDVVSCLKADLQTEYEVRDALKKGIKLCEEAQDYVSRDLMVAQLKDTEEDHAHWLEQQLRLIELIGEGNYYQSQL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
O33833 | MFKPNYHFFPITGWMNDPNGLIFWKGKYHMFYQYNPRKPEWGNICWGHAVSDDLVHWRHLPVALYPDDETHGVFSGSAVEKDGKMFLVYTYYRDPTHNKGEKETQCVAMSENGLDFVKYDGNPVISKPPEEGTHAFRDPKVNRSNGEWRMVLGSGKDEKIGRVLLYTSDDLFHWKYEGVIFEDETTKEIECPDLVRIGEKDILIYSITSTNSVLFSMGELKEGKLNVEKRGLLDHGTDFYAAQTFFGTDRVVVIGWLQSWLRTGLYPTKREGWNGVMSLPRELYVENNELKVKPVDELLALRKRKVFETAKSGTFLLDVK... | Function: Hydrolysis of sucrose, raffinose, inulin and levan. Specific for the fructose moiety and the beta-anomeric configuration of the glycosidic linkages of its substrates. The enzyme released fructose from sucrose and raffinose, and the fructose polymer inulin is hydrolyzed quantitatively in an exo-type fashion.
C... |
A0R647 | MTNSGALDTKFHALIQDQIRSEFTASQQYIAIAVFFDGADLPQLAKHFYAQALEERNHAMMLVQYLLDRDVEVEIPGIDPVCNNFTTPRDALALALDQERTVTEQISRLASVARDEGDHLGEQFMQWFLKEQVEEVAAMTTLVRIADRAGSNLFHIEDFVAREMSAAGADPTAPRAAGGAL | Function: Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 20040... |
H8F1Z2 | MTEYEGPKTKFHALMQEQIHNEFTAAQQYVAIAVYFDSEDLPQLAKHFYSQAVEERNHAMMLVQHLLDRDLRVEIPGVDTVRNQFDRPREALALALDQERTVTDQVGRLTAVARDEGDFLGEQFMQWFLQEQIEEVALMATLVRVADRAGANLFELENFVAREVDVAPAASGAPHAAGGRL | Function: Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 20442... |
P81549 | MKFYSSHPMPESLAAAIAVPLLGLLPAAQAASTAVQLPSVTVEGEYSSYQPESAQSPKFTAPLADTPRTVQVIPERLIQDQGASDLEAVLRNAPGISMTAGEGGRPASDLPFIRGQNSASSLFVDGLRDPSTQSRDTFNLEQVDVVKGPDSVFSGRGGAGGSINLVTKTPRNQDFTEVQAGIGTAETYRGTIDGNWVLGENTALRLNLLGTRDTVPGRDKAVEFSRVGIAPSLRLGLSGPTRVTLGLYHYRHRRVPDYSIPYDPRTGTPITETIGVSRRNFYGLVRRDSGDTEDYAATVKWEHDLANGFKVENLARYSRA... | Function: Probably involved in iron transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81581
Sequence Length: 743
Subcellular Location: Cell outer membrane
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P49944 | MKGEPKVIERLNDALFLELGAVNQYWLHYRLLNDWGYTRLAKKEREESIEEMHHADKLINRIIFFEGFPNLQTVSPLRIGQNVKEVLEADLKGEYDARASYKESREICDKLGDYVSKQLFDELLADEEGHIDFLETQLDLLAKIGEERYGQLNAAPADEAE | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
Q93PP9 | MAGNREDRKAKVIEVLNKARAMELHAIHQYMNQHYSLDDMDYGELAANMKLIAIDEMRHAENFAERIKELGGEPTTQKEGKVVTGQAVPVIYESDADQEDATIEAYSQFLKVCKEQGDIVTARLFERIIEEEQAHLTYYENIGSHIKNLGDTYLAKIAGTPSSTGTASKGFVTATPAAE | Cofactor: Binds 1 Fe-coproporphyrin III group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) ... |
P94804 | MTVGVCYFPEHWSRERWETDISQMAEAGIEYVRMGEFAWRRIEPERGTFDFAWLDEAVELIGKFGMKAVLCTPTATPPKWLVDEHPDVRQREQDGTPREWGSRRFTCFNSPTYRSETERIVSVLTDRYADNPHVAGWQTDNEFGCHETVTCYCEDCGEAFSEWLADRYESVADLNDAWGTTFWSQQYDDFESIDPPKPTPAANHPSRVLAYERFSNDSVAEYNRLHAALIREANDEWFVTHNFMGGFSLDAFRLAADLDFLSWDSYPTGFVQDRQPDTPTVDELRAGNPDQVSMNHDLQRGAKGKPFWVMEQQPGDINWP... | Function: When overexpressed, cleaves several different substrates including o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) and lactulose, but not lactose. Has also beta-D-fucosidase activity. No beta-L-fucosidase, beta-glucosidase, beta-arabinosidas... |
P83252 | TGVTYDHRALVIDGXXXVLVSGSIHYPRAASSWYAVET | Function: Involved in cell wall degradation. Degrades polysaccharides containing beta-(1-->4)-linked galactans, acting as an exo-(1-->4)-beta-D-galactanase (By similarity).
PTM: The small subunit is N-glycosylated.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.... |
P16278 | MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGA... | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 76075
Sequence Length: 677
Subcellular Location: Lysosome
EC: 3.2.1.23
|
Q02603 | MQANLQWLDDPEVFRVNQLPAHSDHHYYHDTAEFKTGSRFIKSLNGAWRFNFAKTPAERPVDFYQPDFDATDFDTIQVPGHIELAGYGQIQYINTLYPWEGKIYRRPPYTLNQDQLTPGLFSDAADNTVGSYLKTFDLDDVFKGQRIIIQFQGVEEALYVWLNGHFIGYSEDSFTPSEFDLTPYIQDQGNVLAVRVYKHSTAAFIEDQDMFRFSGIFRDVNILAEPASHITDLDIRPVPNANLKSGELNITTKVTGEPATLALTVKDHDGRVLTSQTQTGSGSVTFDTMLFDQLHLWSPQTPYLYQLTIEVYDADHQLLE... | Function: Component of a beta-galactosidase that displays activity with the artificial chromogenic substrate o-nitrophenyl-beta-D-galactopyranoside (ONPG).
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 72113
Sequence Length: 626
EC: 3.2.1.2... |
Q60HF6 | MPGFLVRILPLLLPLLLLGPTRGLRNATRRVFEIAYSQDRFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNTIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKEAILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPIITVQVENEYGSYFACDFDYLRFLQKRFHHHLGDDVVLFTTDGAHETFLQCGALQGLYTTVDFGPGSNITDAFQIQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEVVASSLYDILARGASVNLYMFIGGTNFAYWNGA... | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 76826
Sequence Length: 682
Subcellular Location: Lysosome
EC: 3.2.1.23
|
P23780 | MLRVPLCTPLPLLALLQLLGAAHGIYNVTQRTFKLDYSRDRFLKDGQPFRYISGSIHYFRIPRFYWEDRLLKMKMAGLNAIQMYVPWNFHEPQPGQYEFSGDRDVEHFIQLAHELGLLVILRPGPYICAEWDMGGLPAWLLEKQSIVLRSSDPDYLVAVDKWLAVLLPKMKPLLYQNGGPIITVQVENEYGSYFACDYDYLRFLVHRFRYHLGNDVILFTTDGASEKMLKCGTLQDLYATVDFGTGNNITQAFLVQRKFEPKGPLINSEFYTGWLDHWGKPHSTVKTKTLATSLYNLLARGANVNLYMFIGGTNFAYWNG... | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 73121
Sequence Length: 647
Subcellular Location: Lysosome
EC: 3.2.1.23
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P26218 | MFRRNLITSAILLMAPLAFSAQSLAESLTVEQRLELLEKALRETQSELKKYKDEEKKKYTPATVNRSVSTNDQGYAANPFPTSSAAKPDAVLVKNEEKNASETGSIYSSMTLKDFSKFVKDEIGFSYNGYYRSGWGTASHGSPKSWAIGSLGRFGNEYSGWFDLQLKQRVYNENGKRVDAVVMMDGNVGQQYSTGWFGDNAGGENYMQFSDMYVTTKGFLPFAPEADFWVGKHGAPKIEIQMLDWKTQRTDAAAGVGLENWKVGPGKIDIALVREDVDDYDRSLQNKQQINTNTIDLRYKDIPLWDKATLMVSGRYVTAN... | Function: Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.
Location Topology: Multi-... |
Q4WU49 | MVQLDVEKTIEELTLGEKVALTAGIDFWHTAAVPRLNIPSLRMSDGPNGVRGTRFFNGVPAACFPCATALGATWDTKLLYEVGRLMGEESIAKGAHVVLGPTINTQRSPLGGRGFESFAEDGVLSGILAGHYCKGLQETGVAATLKHFVCNDQEHERLAVDSIVTMRAMREIYLLPFQLAMRICKTACVMTAYNKVNGTHVSENKQIITDILRKEWGWDGLVMSDWFGTYSTCDAINAGLDLEMPGPTRWRGTALAHAVSSNKAFEFVMDERVRNILNLHNFVEPLGIPENAPEKALNRPEDQALLRRAAAESVVLIKNQ... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
A2R989 | MARVDFWHTASIPRLNIPALRMSDGPNGVRGTRFFNGIPAACFPCATALGATWDAHLLHEVGQLMGDESIAKGSHIVLGPTINIQRSPLGGRGFESFAEDGVLSGILAGNYCKGLQEKGVAATLKHFVCNDQEHERLAVSSIVTMRALREIYLLPFQLAMRICPTACVMTAYNKVNGTHVSENKELITDILRKEWNWDGLVMSDWFGTYTTSDAINAGLDLEMPGKTRWRGSALAHAVSSNKVAEFVLDDRVRNILNLVNWVEPLGIPEHAPEKALNRPQDRDLLRRAAAESVVLMKNEDNILPLRKDKPILVIGPNAQI... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
Q0CAF5 | MTRLDVEKTIEELTLGEKVALTAGIDFWHTASVPRLNIPTLRMSDGPNGVRGTRFFNGVPAACFPCATALGATWDTELLHECGRLMGEESIAKGSHIILGPTINTQRSPLGGRGFESFAEDGVLSGNLAGYMSKGIQEKGVAATLKHFVCNDQEHERLAVDSIVTMRAMREIYLMPFQLAMRICPTACVMTAYNKVNGTHVSENKQIITDILRKEWGWDGLVMSDWFGTYSTSEAINAGLDLEMPGKTRWRSTPLAHAVSSNKVAEFVMDERVRNVLNLVNFVEPLGIPENCPEKALNRPQDQALLRRAAAESIVLMKND... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
Q5BB53 | MPQLDVDKTIEELRLGEKIDLVSGIDFWHTASVPRLNIPSLRMSDGPNGVRGTRFFNGVPAACFPCATALGATWDTELLHKVGHLMGEEAIAKGAHVILGPTINTQRSPLGGRGFESFAEDGVLAGHLAGYCSKGIQEKGVAACLKHFVCNDQEHERLAVDSIVTDRATREIYLLPFQIAMRICKTATVMTAYNKINGTHVSENKKYITDILRKEWGWDGLVMSDWFGTYSCTSESIIAGLDIEMPGKTRWRGDALAHAVSSNKVHEFVLDERVRNVLNLVNYVEPLGIPENAEEKVLNRPEDQALLRRAAAESIVLLKN... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes, and catalyze the last step releasing glucose from the inhibitory cellobiose.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 92621
Sequence Length: 839
Pathway: ... |
A1DFA8 | MVQLDVEKTIEELTLGEKVALTAGIDFWHTAAVPRLNIPSLRLSDGPNGVRGTRFFNGVPAACFPCATALGATWDTKLLHEVGRLMGEESIAKGTHVVLGPTINIQRSPLGGRGFESFAEDGVLSGILAGHYCKGLQETGVAATLKHFVCNDQEHERLAVDSIVTMRAMREIYLLPFQLAMRICKTACVMTAYNKINGTHVSENKQIITDILRKEWGWDGLVMSDWFGTYSTSDAINAGLDLEMPGPTRWRGTALAHAVSSNKAFEFVVDERVRNILNLHNFVEPLGIPENAPEKALNRPEDQALLRRAAAESVVLMKNQ... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
Q4WLY1 | MGSIDTVGMGQRAIDQIISELSLNEKVALLSGVDAWHTFAIPRLGIPSIRTTDGPNGARGTRYFNGVPSACLPCGTALGATFDRDLIFSLGQLLAAECRAKGAHVLLGPTINIQRGPLGGRGFESFSEDPVLSGLAAASYCSGVQDGGVVPTLKHLVCNDQEHERVAVSALVTPRALREIYLLPFQLAIQGARPGAVMTSYNKVNGLHASENPGLIRDILRGEWGYEGAVISDWFGTYSVADAVNAGLDLEMPGPTRFRGPALMHALTSNKVSEKTLNERVRKVLELVQLASRAGVPEYAPERKLNRPEDRALLRRAAGE... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
O14503 | MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTDTDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGHFTSSDLISSPFLGPHPHQPP... | Function: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes . Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional r... |
O35185 | MERIPSAQPPPTCLPKAPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGDLSGRNLEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGASRKPLDSAPKAVDLKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFAVGERVSTIKQESEEPPTKKSRMQLSEEEGHFAGSDLMGSPFLGPHPHQPP... | Function: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes . Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional r... |
P53744 | MNRVGAVFLFVYERNFFLSIVPDRHRTEIRMSSSERSEVKFDKHFNWWSLLGIAFSLSCSWVGISASMAVGIASGGPLLIIYGLIIAAFFSLMCGISLGDFAAILPNSSGGSFWVLKMLEQESVTLKTPEYEDPSDDDEEVFLENYCQTFNVEVSSKFQKVSSMVVGLLNYFGAIFTTASICSSLSMSCIGIHKLLHPDYELKHWHVFVGYECINAVLTLFNIYSTPLPYISQFGLYTSLLSFAMTFIICIVSRSDNTVDPWPKASNIFGSFDNQTGWNSSGMAFVVGLVNPIWAFVGIDSATHMIDEVGYSKSRFLVPK... | Function: Transport into the cell of 7-keto 8-aminopelargonic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62428
Sequence Length: 561
Subcellular Location: Membrane
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Q8A7T2 | MTLQEIKDQVLAGFDISSAQATWLANMADSEALYAAAHEITITCASHEFDMCSIINAKSGRCPENCKWCAQSSHYKTQAEIYDLLPAEECLRQAKYNESQDVNRFSLVTSGRKPSPKQISQLCDAARLMRKHSSIQLCASLGLLNEEELRALHTAGITRYHCNLETAPSYFPTLCSTHTQEQKLATLDAARRVGMDICCGGIIGMGETMEQRIEFAFTLAELNVQSIPINLLSPIPGTPLENEKALSEEEILRTIALFRFINPTAFLRFAGGRSQLTPEAMRKALFVGINSAIVGDLLTTLGSKVSDDKKMILEEGYHFA... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes two activities which are involved in the biotine biosynthesis: the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical... |
O66557 | MWELDPKTLEKWDKEYFWHPFTQMKVYREEENLIFERGEGVYLWDIYGRKYIDAISSLWCNVHGHNHPKLNNAVMKQLCKVAHTTTLGSSNVPAILLAKKLVEISPEGLNKVFYSEDGAEAVEIAIKMAYHYWKNKGVKGKNVFITLSEAYHGDTVGAVSVGGIELFHGTYKDLLFKTIKLPSPYLYCKEKYGELCPECTADLLKQLEDILKSREDIVAVIMEAGIQAAAGMLPFPPGFLKGVRELTKKYDTLMIVDEVATGFGRTGTMFYCEQEGVSPDFMCLGKGITGGYLPLAATLTTDEVFNAFLGEFGEAKHFYH... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
P57379 | MSQSDTIFDYKHIWHPYSSMNNPHPCYTVISAKGVYLKLKNRKYMIDGMSSWWAAIHGYNHPVLNKALKKQIRKMSHVMFGGITHPPAISLCRKLISLTPEKLDCVFLSDSGSVAIEVAIKMLIQYWQALGQKRKLFLTIRNGYHGDTFSAMSVSDPKNSFHQIYHNLLPKHLFADAPVSSFYKNWDNEDILSFKKIIEKNSFKIAGVILEPIVQGVGGMNFYHPMYLKQIKILCNHYSIPVIFDEIATGFGRTGKMFAFEHANVVPDILCLGKSITGGTITLAATLTSRHIADTISKGKVGCFMHGPTYMGNPLACAVA... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
Q89AK4 | MQKNNLNFDKQHIWHPYASMIQPTPCILVKSAKGIILKLHNGKKLIDGMSSWWSTIHGYNHPRLNNALKNQINKMSHVMFGGITHYPAISLCKKLIEITPNSLTRIFLSDSGSVSIEIAIKMILQYWQSLGKNKVIFLTIKKSYHGDTFAAMSVCDPKNSFHQFYHNFLPINIFADNPKCSFDGLWNKKDIISFKKLIQKHKDVVAAVILEPIVQSVGGMKFYHPNYLKQVRFLCDLYKIPLILDEIATGFGRTGKFFAFEHSNIVPDVLCIGKAITGGTITLSATLTTDKIANVISNSASGCLMHGPTFMGNPLACAAA... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
P46395 | MENPSLRELDHRNIWHPYAAPGVRNRLVTKTDGVFLTLEDGSTVIDAMSSWWSAIHGHGHPRLKAAAQKQIDTMSHVMFGGLTHEPAIKLTHKLLNLTGNSFDHVFYSDSGSVSVEVAIKMALQASKGQGHPERTKLLTWRSGYHGDTFTAMSVCDPENGMHSLWKGTLPEQIFAPAPPVRGSSPQAISEYLRSMELLIDETVSAIIIEPIVQGAGGMRFHDVALIEGVATLCKKHDRFLIVDEIATGFGRTGELFATLSNGLQPDIMCVGKALTGGFMSFAATLCTDKVAQLISTPNGGGALMHGPTFMANPLACAVSH... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
Q728P4 | MSTSPFNSRVAPMPHDDATAPVLHYAHDAAGAHDAADAAGAHDAADAAGTPPCAASRTARLRSLDAAHVWHPFTQMRDWMGSEPCIIDAADGNHLIDTDGNRYLDGVSSLWTNVHGHRHPHIDEAIRRQLDRVAHSTLLGLGGTPSIELAARLTAIAPAGLTRVFYSDSGSTAVEAALKIAFQYHRQAPEGDARRTRVMAFSNAYHGDTIGSVSLGGMSLFHGIYGPLLFDPVRAPAPHCYRCPADLRPETCGMACLGEVERLMRHHGHELCAVVVEPLVQGAAGMLVQPRGWLRGLRDLCDRHGVFMVADEVAVGFGKT... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
P12995 | MTTDDLAFDQRHIWHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAAHRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAA... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA) . It is the only animotransferase known to utilize SAM as an amino donor . Complements a bioU deletion in Synechocystis PCC 6803 .
Catalytic Acti... |
P44426 | MVDEQSLLAFDTQHIWHPYSSVSSDMPLYAVERADGVMITLKDGRRLIDGMSSWWAALHGYNHPRLNAAAQNQLAKMSHIMFGGFTHDPAVELAQLLVQILPNGLDKIFFADSGSVAVEVAMKMAIQYQHAKGEVQRQKFATIRSGYHGDTWNAMSVCDPTTGMHHLFHHSLPVQYFLPQPNIPFNESWNDCAIEPLADLLKKKGNEIAALILEPVVQGAGGMYFYSPTYLVKAQALCKQYGILLIFDEIATGFGRTGKLFAAEHAGISPDIMCIGKALTGGYLTLSASITTTEIAQTICSGEAKCFMHGPTFMANPLAC... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
O25627 | MNFQENLAALDLEYLWHPCSQMQEHQNFPIIPIKKAQGIYLYDFNDNAYMDLISSWWVNLFGHNNAYISQQLKNQIDDLEHVLLASFSHKPIITLSQRLCQLTHMDKCFYADNGSSCVEIALKMSYHAHFLKNQTRRKKLFLSLSNSYHGETLGALSVGDVKLYKDTYTPLLLKNLTTPVPKNDHEIENSLNALKRLLDKHSEEICAFIAEPLLQCAGNMHIYSARYLKQAVLLCKQKNIHIIFDEIATGFGRTGSMFAYEQCEIKPDFLCLSKGISGGYLPLSALLTHNEIYNQFYAPYEENKAFLHSHSYTGNALACA... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
P22805 | MKQVLTELQEKDLQHVWHPCSQMKDYEAFPPIVIKKGEGVWLYDEQNQRYLDAVSSWWVNLFGHANPRISQALSEQAFTLEHTIFANFSHEPAIKLAQKLVALTPQSLQKVFFADNGSSAIEVALKMSFQYHMQTGKTQKKRFLALTDAYHGETLGALSVGGVDLYNEVYQPLLLDTVRAQGPDCFRCPFKHHPDSCHAQCISFVEDQLRMHHKEITAVIIEPLIQAAAGMKMYPAIYLRRLRELCTQYDVHLIADEIAVGFGRTGTLFACEQANISPDFMCLSKGLTGGYLPLSVVMTTNDVYQAFYDDYATMKAFLHS... | Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionin... |
B0TE53 | MQSIIRQTEAALFAGAVLDRETAGKLARIEGSDIYTLMDVARRVRDHFGAGKVDLCSIVNAKSGACSEDCRFCAQSAHHQACVKTYDLLDPDAIVGRARVMEAEGAHRFSLVTSGRGMSDAELEPVLAIYERLRRETKLSLCASLGILNEAQLRRLAEAGVTMYHHNLEASRRFFPQICTTHSYDERIATIRAAQAAGMVVCSGGIFSMGETIDDRIDMAFELRELGIRSVPINILNPIAGTPLEGQPLIPPLEILKSIALYRLILPSARIRMAGGREGALRDLQSLPFIAGADAALVGSYLTTSGRTVAEDIQMLRDLG... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
O25956 | MQEIFLCSISNVRSGDCKEDCAYCTQSSHHQGAIKRYKFKDEKVVLQEARALRQLGALGFCLVTSGRELDDEKCEYIAKLAKAINQEELGLHLIACCGRADLEQLEFLRDAGIHSYNHNLETSQNFFPKICSTHTWEERFITCENALRAGLGLCSGGIFGLNESWEDRIEMLRALASLSPHTTPINFFIKNPVLPIDAETLSADEALECVLLAKEFLPNARLMVAGGREVVFKDNDKKEAKLFEYGINAVVLGDYLTTKGKAPKKDIEKLLSYGLTMATSCH | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
B4U973 | MEQVFFDIYQKAKNDEISKEEALFILKAEDKYIPLIVYLTSKLKDEFFDSQKFEFCSIINAKSGACSEDCKFCAQSKFYKTPINIYKLVDKEELVEGAIRGVEFGANRYCMVLSSRAASDEEVEKLCEAVQEIKAQNIPINVCVSAGTIGLESLLKLKEAGVTRINHNLETSENYFPNIVSTHTWKERLETIKNVQKAGLSTCSGVIFGLGETDEDRVDLAFVYKELGVDSIPLNFLMPIPNTPLENNKPLRALDALKIIAMFRFINKSAELRLCGGREQTLGDFHGMAAFMTNALMAGGYLTRAGRDIKKDYKMLEDMN... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
A9EXH2 | MLEGIEREAAEHSNGCSGPAGHAPPAGAPRHDWTVQQAVALHDLPLFELIDRARAVHRAFHGEHEVQLCTLLSVKTGGCPEDCAYCPQSSHYETEVGPERMLDVGAVLAAAERAREGGSTRFCMGAAWREVKDGPAFERVLDMVRGVKALGLEACCTLGMLTDDQARRLKEAGLDAYNHNLDTSRKAYKSIISTRTYDERLVTLRNVRRAGITVCSGGIIGMGESIADRCEMLVELARLDPHPESVPINALVRSPGTPLESLPPVDPIEFVRMIAVARVMMPRAMVRLSAGRTELSRETQLLCMYAGANSIFYGDRLLTT... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
C1FR34 | MARGIFITATGTDIGKTYVTALIIKRLRETNINCGYYKAALSEAERRDGKLIAGDANYVYNIANIKGDPNDAVSYIFQQAVSPHLAAKLNNVEISMERIKKDFYSIKNKYDYITVEGSGGIVCPISTGKEKIMLDNIIKIFKLPAIVVADAGLGTINSTILTLQYMKEKNISVKMILLNNYNHEDIIHIENKGYLSDNLLIPVYTCNKNANNLEIPVEKLIEIYEEI | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
Q0TQ60 | MEKGVYIIGTSTDIGKTFISGLILKKLREEGRNAGYYKAVLSGAIKDKKGLIPLDCEEVMEISGLKESYENMVSYILENPYSPHLASEVEEVSISMEKIKKDYKSVRDKYDFILCEGSGGIVCPISFSEKKLMLEDIIKEFNLPIILVSNSGLGAINHTVLTVSYLRNLGLKVKGIILNKFNKSDIIHRDNKKIIKELTGVNNISTVPKIEDIEKYDLNELNEVLYGI | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
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