ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B2FQN4 | MKALVKREAAKGIWLEEVPVPTPGPNEVLIKLEKTAICGTDLHIYLWDEWSQRTIKPGLTIGHEFVGRVAALGSAVTGYEIGQRVSAEGHIVCGHCRNCRGGRPHLCPNTVGIGVNVNGAFAEYMVMPASNLWPIPDQIPSELAAFFDPYGNAAHCALEFNVIGEDVLITGAGPIGIIAAGICKHIGARNVVVTDVNDFRLKLAADMGATRVVNVANQSLKDVMKELHMEGFDVGLEMSGNPRAFNDMLDCMYHGGKIAMLGIMPKGAGCDWDKIIFKGLTVQGIYGRKMYETWYKMTQLVLSGFPLGKVMTHQLPIDDF... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Catalytic Activity: L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH
Sequence Mass (Da): 37013
Sequence Length: 340
Pathway: Amino-acid degradation; L-threonine degrada... |
Q5SKS4 | MRALAKLAPEEGLTLVDRPVPEPGPGEILVRVEAASICGTDLHIWKWDAWARGRIRPPLVTGHEFSGVVEAVGPGVRRPQVGDHVSLESHIVCHACPACRTGNYHVCLNTQILGVDRDGGFAEYVVVPAENAWVNPKDLPFEVAAILEPFGNAVHTVYAGSGVSGKSVLITGAGPIGLMAAMVVRASGAGPILVSDPNPYRLAFARPYADRLVNPLEEDLLEVVRRVTGSGVEVLLEFSGNEAAIHQGLMALIPGGEARILGIPSDPIRFDLAGELVMRGITAFGIAGRRLWQTWMQGTALVYSGRVDLSPLLTHRLPLS... | Cofactor: Binds 2 Zn(2+) ions per subunit. Contains one structural ion and one catalytic ion that may be less tightly bound at the site.
Function: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Catalytic Activity: L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH
Seque... |
A5F0N6 | MKIKALSKLKPEQGIWMNEVDMPELGHNDLLIKIKKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVRGFQIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRTGCFSEYLVIPAFNAFKIPDGISDDLASIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLDLARKMGVTRAVNVAEQNLEDVMKELGMTEGFDVGLEMSGVPSAFSAMLKTMNHGGRIALLGIPPSSMAIDWNQVIFKGLVIKGIYGREMFETWYKMASLIQSGLDISPIITHHFKV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Catalytic Activity: L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH
Sequence Mass (Da): 37541
Sequence Length: 343
Pathway: Amino-acid degradation; L-threonine degrada... |
Q8R844 | METEAIENIPRVCLPQIGAPAPDFKANSTFGPIKLSDYRGKWVVLFSHPGDFTPVCTTEFIAFTQVYTSFVERNVQLIGLSVDSNPSHLAWVENIYKTTGVEIPFPIIEDKDMRIAKLYGMISPAETSTSAVRAVFIIDDKQILRLILYYPLEIGRNIQEIIRIIDALQTVDKYKVLAPANWYPGMPVIVPPPKTYPELKQRLKNVEGYTCTDWYLCYKKV | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
Q6L140 | MPVYLGKRAPDFTANTTRGVISLSDYKNKWVLLFSHPADFTPICTTEFIEFSRRYNDFKELNVELIGLSVDSLQSHIEWLKDIYEKFGIEIQFPVIADINKEIAREYNLIDENAGNTVRGVFIIDPNQTVRWMIYYPAETGRNIDEILRSVKALQANWSRKIATPVNWRPGDKGILPPPSTLEDALQRIREGNKTWYIKTE | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
Q9Y9L0 | MPGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFSHPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYEEARTHLH | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
O67024 | MEVVSLPRLGEPAPAFEAQTTFGPVKFPDDFKGQWVVLFSHPADFTPVCTTEFVAFAKNYEEFKKRNVQLIGLSVDSNFSHIAWVMNIKEKFGIEIPFPIIADHNMEVAKKYGMIHPAQSTTFTVRALFVIDDKGILRAMIYYPLTTGRNIREVIRLVDALQTADREGVATPADWVPEPQTWEFTEENTKVIVPPPTTYEDAVKRLQEGYECADWYICKKKV | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
O29969 | MAPLLGDNFPEIEVVTTHGRMKLPEAFKGKWFVLFSHPADFTPVCTTEFVAFQNRYDEFRKLNCELIGLSIDQVFSHIKWIEWIKEKLDIEIEFPVIADDTGRVAEMLGLIHPAKGTNTVRAVFIVDPEAVIRAVIYYPQELGRNMDEILRAVKALQVSDQNGVAMPANWPNNELVGDAVIIPPPISEAEAKERLEKAKAGDISCYDWWFCYKKI | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
Q8PYP6 | MPLIGDDAPSFTAVTTQGIIKFPDDYKGKWVILFSHPADFTPVCTTEFMTFASMQEEFRSMNTELIGLSIDSVFSHIAWLKRIEEKIEYKGMKNLEIKFPVIEDLKMDVAKKYGMVQPKASTTQAVRAVFIIDPEAKIRTILYYPQSTGRNMQEIKRIVVALQKNAAEKVATPANWQPGEDVIIPPPSSMEAVKERMGKEEEGKRCLDWFMCLKKDTQK | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
Q6LY19 | MVVIGEKFPEVEVTTTHGKLKLPEHYIESGKWFVLFSHPGDFTPVCTTEFVAFQKRYDQFRELNTELIGLSIDQVFSHIKWVEWIKEKLDVDIEFPIIADDRGELAVKLGMISPYKGNNTVRAVFVVDATGTIRAIIYYPQEVGRNMDEIVRLVKALQTADKGYATPANWPNNDFLNEKVIVPPANNMDARKKRLEACKSGELEGYDWWFCYTDLKE | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
O26262 | MPLIGDKFPEMEVQTTHGPMELPDEFEGKWFILFSHPADFTPVCTTEFVAFQEVYPELRELDCELVGLSVDQVFSHIKWIEWIAENLDTEIEFPVIADTGRVADTLGLIHPARPTNTVRAVFVVDPEGIIRAILYYPQELGRNIPEIVRMIRAFRVIDAEGVAAPANWPDNQLIGDHVIVPPASDIETARKRKDEYECYDWWLCTQSRG | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
Q90955 | VFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFNNIDPNESKHKRTDRSILCCLRKGESGQAWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDDDVDLPEVDGADDDSPDSDDEKMPDLE | Function: Molecular chaperone.
Catalytic Activity: prostaglandin H2 = prostaglandin E2
Sequence Mass (Da): 16869
Sequence Length: 146
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subcellular Location: Cytoplasm
EC: 5.3.99.3
|
Q15185 | MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE | Function: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) . Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassem... |
Q9R0Q7 | MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMDHMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE | Function: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassemb... |
B6TPF2 | MDGGGVDTATTAAWMEKHRHMYERATRHPFTVSIRDGTVDMSAFKRWLSQDYLFVREFVAFIASVLLKCCKQEDSSDMEIILGGVASISDEISWFKNEATVWGVDLASVSPLKANLEYHRFLRSFTEPEISYAVAVTTFWTIETVYQDSFGFCIQDGNKTPPELLGTCQRWGSAGFRQYCQSLQSIVDRCLANAPADAVQSAEEAFVRVLELEIGFWDMSSSRS | Function: Involved in thiamine salvage by hydrolyzing the thiamine breakdown product 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) . Has a high formylamino-HMP amidohydrolase activity . No activity with other thiamine degradation products such as thiamine mono-... |
F4KFT7 | MRFLFPTRLINNSSLGLLRSPHTTAPIRSLWFRTKSPVFRSATTPIMTAVAFSSSLSIPPTSEEALPGKLWIKFNRECLFSIYSPFAVCLAAGNLKIDTFRQYIAQDVHFLKAFAHAYELAADCADDDDDKLAISDLRKSVMEELKMHDSFVQDWDLDINKEVSVNSATLRYTEFLLATASGKVEGCKAPGMLDTPFEKTKVAAYTLGAVTPCMRLYAFLGKEFGSLLDLSDVNHPYKKWIDNYSSDAFQASAKQTEDLLEKLSVSMTGEELDIIEKLYQQAMKLEVEFFHAQPLAQPTIVPLLKNHSKDDLVIFSDFDL... | Function: May be involved in the salvage of thiamine breakdown products . This protein has a haloacid dehalogenase family domain fused to its TenA domain . Phosphatase with the highest activity against thiamine monophosphate (ThMP) and, with a lower activity, against thiamine diphosphate (ThDP), flavin mononucleotide, ... |
Q9ASY9 | MEKRGVIDTWIDKHRSIYTAATRHAFVVSIRDGSVDLSSFRTWLGQDYLFVRRFVPFVASVLIRACKDSGESSDMEVVLGGIASLNDEIEWFKREGSKWDVDFSTVVPQRANQEYGRFLEDLMSSEVKYPVIMTAFWAIEAVYQESFAHCLEDGNKTPVELTGACHRWGNDGFKQYCSSVKNIAERCLENASGEVLGEAEDVLVRVLELEVAFWEMSRGGQ | Function: Involved in thiamine salvage by hydrolyzing the thiamine breakdown product 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) . Has a high formylamino-HMP amidohydrolase activity . No activity with other thiamine degradation products such as thiamine mono-... |
Q9SWB6 | MEEKAKAEQKKIGMTETWLKKHRLLYNGATRHPLIISIRDGTINTASFKTWLAQDYLFVRAFVPFVASVLIKAWKESDCSGDMEVILGGMASLEDEISWFKTEANKWGISLSDVVPQQANKNYCGLLESLMSPDAEYTVAITAFWAIETVYQESFAHCIEEGSKTPPELKETCVRWGNEAFGKYCQSLQNIANRCLQKASDEELKKAEVMLLSVLEHEVEFWNMSRGNV | Function: May be involved in thiamine salvage.
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Mass (Da): 25988
Sequence Length: 229
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.1.-
|
P25052 | MKFSEECRSAAAEWWEGSFVHPFVQGIGDGTLPIDRFKYYVLQDSYYLTHFAKVQSFGAAYAKDLYTTGRMASHAQGTYEAEMALHREFAELLEISEEERKAFKPSPTAYSYTSHMYRSVLSGNFAEILAALLPCYWLYYEVGEKLLHCDPGHPIYQKWIGTYGGDWFRQQVEEQINRFDELAENSTEEVRAKMKENFVISSYYEYQFWGMAYRKEGWSDSAIKEVEECGASRHNG | Function: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP). To a lesser extent... |
Q9K9G8 | MSFAASLYEKAQPIWEAGYNHPFVQGIGDGSLEKSKFQFFMKQDYLYLIDYARLFALGTLKGNDLQTMSTFSKLLHATLNVEMDLHRAYAKRLGISAEELEAIEPAATTLAYTSYMLNVAQRGSLLDLIAAVLPCTWSYYEIGVKLKGIPGASDHPFYGEWIKLYASDEFKELADWLIQMLDEEAKGLSSKEKAKLETIFLTTSRLENEFWDMAYNERMWNYNG | Function: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP). To a lesser extent... |
A8KRL3 | MQVSQYLYQNAQSIWGDCISHPFVQGIGRGTLERDKFRFYIIQDYLFLLEYAKVFALGVVKACDEAVMREFSNAIQDILNNEMSIHNHYIRELQITQKELQNACPTLANKSYTSYMLAEGFKGSIKEVAAAVLSCGWSYLVIAQNLSQIPNALEHAFYGHWIKGYSSKEFQACVNWNINLLDSLTLASSKQEIEKLKEIFITTSEYEYLFWDMAYQS | Function: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds to give a hydroxymethylpyrimidine (HMP). Displays low activity on 4-amino-5-aminomethyl-2-methylpyrimidine as substrate, indicating that the enzyme may act on a different HMP precursor that may derive f... |
Q9UGI8 | MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVKEMEQFVKKYKSEALGVGDVKLPCEMDAQGPKQMNIPGGDRSTPAAVGAMEDKSAEHKRTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSTCHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQN... | Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth.
Sequence Mass (Da): 47996
Sequence Length: 421
Domain: The N-terminal and... |
P47226 | MSATHPTRLGTRTKESNACASQGLVRKPPWANEGEGFELHFWRKICRNCNVVKKSMTVLLSNEEDRKVGRLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPKEVKEMEQFVKKYKSEALGVGDVKFPSEMNAQGDKVHNCGNRHAPAAVASKDKSAESKKTQYSCYCCKHTTNEGEPAIYAERAGYDKLWHPACFICSTCGELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAEN... | Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity).
Sequence Mass (Da): 47983
Sequence Length: 423
Domain: The N-terminal and the C-termi... |
Q2LAP6 | MDLETKMKKMGLGHEQGFGAPCLKCKENCEGFELHFWRKICRNCKCGQEEHDVLLSTEEDRKVGRLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPKEVKEMEQFVKKYKSEALGVGDVKLPSEMNAQGDKVHNPAGDRNTPAAVGSKDKSAEAKKTQYSCYCCKNTMREGDPAIYAERAGYDKLWHPACFICSTCGELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWH... | Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity).
Sequence Mass (Da): 47632
Sequence Length: 419
Domain: The N-terminal and the C-termi... |
P52655 | MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLIQHMNASNMSAAATAATLALPAGVTPVQQILTNSGQLLQVVRAANGAQYIFQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPTPAQAQITATGQQQPQAQPAQTQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDV... | Function: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
PTM: The alpha and beta subunits are postranslationally produced from the precursor form by TASP1. The cleavage pro... |
Q99PM3 | MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHQHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLLQHMNASSITSAAATAATLALPAGVTPVQQLLTNSGQLLQVVRAANGAQYILQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPAPAQAPMPAAGQQQPQAQPAQQQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSED... | Function: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity).
PTM: The alpha and beta subunits are postranslationally produced from the precursor form by TASP1. ... |
P03001 | MAAKVASTSSEEAEGSLVTEGEMGEKALPVVYKRYICSFADCGAAYNKNWKLQAHLCKHTGEKPFPCKEEGCEKGFTSLHHLTRHSLTHTGEKNFTCDSDGCDLRFTTKANMKKHFNRFHNIKICVYVCHFENCGKAFKKHNQLKVHQFSHTQQLPYECPHEGCDKRFSLPSRLKRHEKVHAGYPCKKDDSCSFVGKTWTLYLKHVAECHQDLAVCDVCNRKFRHKDYLRDHQKTHEKERTVYLCPRDGCDRSYTTAFNLRSHIQSFHEEQRPFVCEHAGCGKCFAMKKSLERHSVVHDPEKRKLKEKCPRPKRSLASRL... | Function: Involved in ribosomal large subunit biogenesis (By similarity). Acts as both a positive transcription factor for 5S RNA genes and a specific RNA binding protein that complexes with 5S RNA in oocytes to form the 7S ribonucleoprotein storage particle. May play an essential role in the developmental change in 5S... |
P81453 | MRIRRRALVFATMSAVLCTAGFMPSAGEAAADNGAGEETKSYAETYRLTADDVANINALNESAPAASSAGPSFRAPDSDDRVTPPAEPLDRMPDPYRPSYGRAETVVNNYIRKWQQVYSHRDGRKQQMTEEQREWLSYGCVGVTWVNSGQYPTNRLAFASFDEDRFKNELKNGRPRSGETRAEFEGRVAKESFDEEKGFQRAREVASVMNRALENAHDESAYLDNLKKELANGNDALRNEDARSPFYSALRNTPSFKERNGGNHDPSRMKAVIYSKHFWSGQDRSSSADKRKYGDPDAFRPAPGTGLVDMSRDRNIPRSP... | Function: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
Catalytic Activity: L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 45684
Sequence Length: 407
EC: 2.3.2.13
|
P04867 | MDMTKTVEEKKTNGTDSVKGVFENSTIPKVPTGQEMGGDGSSTSKLKETLKVADQTPLSVDNGAKSKLDSSDRQVPGVADQTPLSVDNGAKSKLDSSDRQVPGPELKPNVKKSKKKRIQKPAQPSGPNDLKGGTKGSSQVGENVSENYTGISKEAAKQKQKTPKSVKMQSNLADKFKANDTRRSELINKFQQFVHETCLKSDFEYTGRQYFRARSNFFEMIKLASLYDKHLKECMARACTLERERLKRKLLLVRALKPAVDFLTGIISGVPGSGKSTIVRTLLKGEFPAVCALANPALMNDYSGIEGVYGLDDLLLSAVP... | Function: Participates in the transport of viral genome to neighboring plant cells directly through plasmodesmata, without any budding . Multifunctional movement protein with RNA-binding, ATPase and helicase activities . Engages in homologous interactions leading to the formation of a ribonucleoprotein complex containi... |
P10600 | MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPL... | Function: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively.
PTM: Transforming growth factor beta-3 proprotein: The precursor proprotein... |
O43294 | MEDLDALLSDLETTTSHMPRSGAPKERPAEPLTPPPSYGHQPQTGSGESSGASGDKDHLYSTVCKPRSPKPAAPAAPPFSSSSGVLGTGLCELDRLLQELNATQFNITDEIMSQFPSSKVASGEQKEDQSEDKKRPSLPSSPSPGLPKASATSATLELDRLMASLSDFRVQNHLPASGPTQPPVVSSTNEGSPSPPEPTGKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFVCGGCSTALGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPF... | Function: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to t... |
Q62219 | MEDLDALLSDLETTTSHMSRLGAPKERPPETLTPPPPYGHQPQTGSGESSGTTGDKDHLYSTVCKPRSPKPVAPVAPPFSSSSGVLGNGLCELDRLLQELNATQFNITDEIMSQFPSSKMAEGEEKEDQSEDKSSPTVPPSPFPAPSKPSATSATQELDRLMASLSDFRVQNHLPASGPPQPPAASPTREGCPSPPGQTSKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFLCSGCSTTLGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPF... | Function: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to t... |
Q2TCH4 | MEDLDALLADLQITTPPRCPVLLTDSPEKPQPTETRPPPPPYDPKTAMSNKTSDHETFPVDKDHLYSTVQKYPLPSVSPALGGGLCELDRLLNELNATQFNITDEIMSQFPTRDPSEQKAEAQKEAEKRALSASSATLELDRLMASLSDFHKQNTVSQEVEAPGAYKGSEEVSRPGDTEDLSSPRSTACVPKDLEDAPTPKSFKVVSAPGHLEVKTNQVNSDEVTASRVPDSVSGSKVPEATSVPRSDLDSMLVKLQSGLKQQGIETYSKGLCESCQRPIAGQVVTALGHTWHPEHFVCAHCHTLIGTSNFFEKDGRPYC... | Function: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. May regulate both Wnt and steroid signaling pathways and play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-... |
P36897 | MEAAVAAPRPRLLLLVLAAAAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEI... | Function: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethor... |
Q90999 | MPPRLRPLLLRVSLWVLVGSSSPALLHDRSKENGLQLPRLCKFCDVKATTCSNQDQCKSNCNITSICEKNNEVCAAVWRRNDENVTLETICHDPQKRLYGHMLDDSSSEQCVMKEKKDDGGLMFMCSCTGEECNDVLIFSAIDPHKPEEKDEISKVTIISLVPLLVISVAVIVIFYAYRTHKKRKLNKAWEKNVKPKKHKDCSDVCAIMLDDDHSDISSTCANNINHNTELLPIELDIVVGKGRFAEVYKAKLKQNTSEQYETVAVKIFPYEEYASWKTEKDIFSDVNLKHENILQFLTAEERKTDLGKQYWLITAFHAR... | Function: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora... |
P37173 | MGRGLLRGLWPLHIVLWTRIASTIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQVTGISLLPPLGVAISVIIIFYCYRVNRQQKLSSTWETGKTRKLMEFSEHCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQ... | Function: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and thus regulates a plethora of ... |
Q62312 | MGRGLLRGLWPLHIVLWTRIASTIPPHVPKSVNSDVMASDNGGAVKLPQLCKFCDVRLSTCDNQKSCMSNCSITAICEKPHEVCVAVWRKNDKNITLETVCHDPKLTYHGFTLEDAASPKCVMKEKKRAGETFFMCACNMEECNDYIIFSEEYTTSSPDLLLVIIQVTGVSLLPPLGIAIAVIIIFYCYRVHRQQKLSPSWESSKPRKLMDFSDNCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYSSWKTEKDIFSDINLKHENILQFLTAEERKTELGKQ... | Function: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora... |
P38551 | MGRGLLGGLWPLHVVLWTRIASTIPPHVPKSVNSDMMVTDSNGAVKLPQLCKFCDVRSSTCDNQKSCLSNCSITAICEKPQEVCVAVWRKNDENITIETVCDDPKIAYHGFVLDDAASSKCIMKERKGSGETFFMCSCSSDECNDHIIFSEEYATNNPDLLLVIFQVTGVSLLPPLGIAIAVIITFYCYRVHRQQKLSPSWDSGKPRKLMEFSEHLAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLRQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDL | Function: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora... |
B8E2N5 | MIFEIIVRDKKTRARLGKLKTFHGEINTPVFMPVGTQGAVKTLSPEEVEKVGAEIILSNTYHLFLRPGHEIVRKGGGLHKFMGWEKPILTDSGGYQVFSLARLRRIDEDGIYFNSHIDGTRYFYTPELVMEIQKSLGSDIIMPLDICLGYGASYWETKEALEITLRWLKRSIDYKNNSNMDHQLLFGIVQGGFYKELRKEAVERMLNIDLPGLALGGISVGEPKDKMYEIIDYTVSLLPEEKPRYLMGVGAPEDLVVGVSMGIDMFDCVLPTRLARHGVFYTSKGRKNIKNAQYKEDFSPLEEDCDCYTCRKFTKAYIRH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement... |
Q6P3Z3 | MVICCAAVNCSNRQGKGEKRAVSFHRFPLKDSKRLIQWLKAVQRDNWTPTKYSFLCSEHFTKDSFSKRLEDQHRLLKPTAVPSIFHLSEKKRGAGGHGHARRKTTAAMRGHTSAETGKGTIGSSLSSSDNLMAKPESRKLKRASPQDDAAPKVTPGAVSQEQGQSLEKTPGDDPAAPLARGQEEAQASATEADHQKASSSTDAEGADKSGISMDDFTPPGSGACKFIGSLHSYSFSSKHTRERPSVPREPMDRKRLKREMEPRCSGNSVAQSPPSSSLTATPQKASQSPSAPPTDVTPKPAAEAVQSEHSDASPMSINEV... | Cofactor: Binds 1 heme b group per subunit, that coordinates a highly solvent-exposed Fe(III) atom.
Function: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Theref... |
Q7Z6K1 | MPRYCAAICCKNRRGRNNKDRKLSFYPFPLHDKERLEKWLKNMKRDSWVPSKYQFLCSDHFTPDSLDIRWGIRYLKQTAVPTIFSLPEDNQGKDPSKKKSQKKNLEDEKEVCPKAKSEESFVLNETKKNIVNTDVPHQHPELLHSSSLVKPPAPKTGSIQNNMLTLNLVKQHTGKPESTLETSVNQDTGRGGFHTCFENLNSTTITLTTSNSESIHQSLETQEVLEVTTSHLANPNFTSNSMEIKSAQENPFLFSTINQTVEELNTNKESVIAIFVPAENSKPSVNSFISAQKETTEMEDTDIEDSLYKDVDYGTEVLQI... | Function: Has sequence-specific DNA-binding activity and can function as transcriptional repressor (in vitro) . May be a regulator of cell cycle: THAP5 overexpression in human cell lines causes cell cycle arrest at G2/M phase .
PTM: Cleaved by HTRA2 during apoptosis.
Sequence Mass (Da): 45416
Sequence Length: 395
Subce... |
P24557 | MEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTGCKPNPSRQHQPS... | Function: Catalyzes the conversion of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2), a potent inducer of blood vessel constriction and platelet aggregation . Cleaves also PGH2 to 12-hydroxy-heptadecatrienoicacid (12-HHT) and malondialdehyde, which is known to act as a mediator of DNA damage. 12-HHT and malondialdehy... |
P36423 | MEVLGLLKFEVSGTIVTVTLLVALLALLKWYSMSAFSRLEKLGIRHPKPSPFVGNLMFFRQGFWESQLELRERYGPLCGYYLGRRMHVVISEPDMIKQVLVENFSNFSNRMASGLEPKMVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPFVQHCRRASTFCIPRPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFLQMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPT... | Function: Catalyzes the conversion of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2), a potent inducer of blood vessel constriction and platelet aggregation. Cleaves also PGH2 to 12-hydroxy-heptadecatrienoicacid (12-HHT) and malondialdehyde, which is known to act as a mediator of DNA damage. 12-HHT and malondialdehyd... |
Q7VFU4 | MRTQWVQQRADDKIRTQLHYAKKGIITKEMEYVANIENISAELIRQEIERGRLIIPANINHTNLKPMGIGIATRTKINSNIGSSSLASSIDEEVEKVKVSIKYGADTIMDLSTGGDLDEIRTAVIQASSVPIGTVPIYQILYDVKNDILQLDIDTMLSVLKKQAKQGVSYFTIHCGFLLSHMPFVAKRKMGIVSRGGSLMASWMMHYHKENPFYEYFDEILKICQEYDVSLSLGDSLRPGCLADASDEAQFAELKVLGELAKRAWKADVQVMIEGPGHVPLNQIERNVELQKQYCNHAPFYVLGPLVTDIAAGYDHIASA... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dep... |
Q9BWD1 | MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEI... | Function: Involved in the biosynthetic pathway of cholesterol.
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 41351
Sequence Length: 397
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
|
Q72NZ8 | MEPVQKLQIPYKSIRLSDGTEYQSYHTEGALSGKQPADYKNGIPAFRKEWIQKRFNHSNHSQMYFAKKGIITEEMRYAAFRENMEPEFVRSEIACGRAILPSNRNHPELEPMVIGKNFLVKINANIGNSTFSSSIEEEVEKLHWAIKWGADTVMDLSTGKNIHETREWILRNSPVPIGTVPIYQALEKVKGKTENLNIQIFLETLEEQAEQGVDYFTIHAGVLLRYIPLTTNRITGIVSRGGSILAKWCQAHHKENFLYTHFDEILKVMKKYGVSISLGDGLRPGSIADANDKAQFSELETLGELTQLAWKEDIQVMIEG... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dep... |
Q57688 | MVILAIGGYDPTSGAGISADIKTAHTLGVYCPTITTSVIPQNNKMVYEKFDLPEENIKNQFKAVFEEFDIEYVKTGVLTKPAIDTLLKYIDKYDLKVICDPVLASTTKFSFVDEKLMEKYIELFNKSFLITPNKEEYKKIMEFIKNNNLMIRNDLYILATGIDDILMKNFKPIKTFKGFRVDKEVHGTGCVYSTAITAFLSKGYDLEEAIKEAKRFVLSSVIYAKKSKFGYNSNPTYINKEKVIKNLSYAIYLLKKMNFTLIPEVGSNIAESLPFPKDFKDVAALTGRIIKNKLGGFYIVGDIEFGASEHIAKIILSASK... | Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+)
Sequence Mass (Da): 47056
Sequence Length: 417
Pathway: Cofactor biosyn... |
Q9WZP7 | MVLVVAGFDPSGGAGIIQDVKVLSALGVKTHAVISALTVQNENRVFSVNFRDWEEMRKEIEVLTPPRVIKVGLSAPETVKRLREMFPDSAIVWNVVLESSSGFGFQDPEEVKKFVEYADYVILNSEEAKKLGEYNNFIVTGGHEKGNTVKVKYRDFVFEIPRVPGEFHGTGCAFSSAVSGFLAMSYPVEEAIRSAMELLKKILERSSGVVETEKLLRDWYRYDTLNTLDEILPEFLEIGHLTVPEVGQNVSYALPWAKNEFEVGKFPGRIRLKEGKAVAVSCASFKDRSHTARMAVTMMRYHPHMRCVVNVRYEREYVER... | Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+)
Sequence Mass (Da): 45392
Sequence Length: 398
Pathway: Cofactor biosyn... |
O67772 | MIALSIAGFDNSGGAGTLADIRTFKHFGIYGVAVITALAVQNTQKVYEVFPIPPDVVKEELKAIFEDFPIKGVKIGMLANKEIAEVVYETLKSKKTNFIVLDPVFRSKSGRELLSEEGVEFLKSEFIKIVDLITPNVPEAEILCGEEIKSLEDVKNCAQKIYSLGAKSVLIKGGHLKGNYAIDILYDGKSFYEFKAPKIAGKTPRGTGCVYSSAILANYLRHKDLIKAIKTAKDFITEAIKNSKKLGKGYEIMDF | Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+)
Sequence Mass (Da): 28066
Sequence Length: 255
Pathway: Cofactor biosyn... |
O31620 | MSIYKALTIAGSDSGGGAGIQADIKTFQELDVFGMSAITAVTAQNTLGVHGVHPLTVETLRQQIDAVAEDLRPDAVKTGMLWNADMIEEVARKIDEYGFNRVIVDPVMIAKGGASLLRDESVATLKELLIPRSYAITPNVPEAETLTGMTISSLDDRKKAAEQLVKMGAQHVIIKGGHQPEDNHITDLLFDGSMFMQITHPYINTKHTHGTGCTFAAALTAQTAKGDSIHQAFEVAANFVREAVENTLGIGSGHGPTNHFAFKRNSLNTSR | Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine.
Catalytic Activity: 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+)
Sequence ... |
P76422 | MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDIVEAVAERLQRYQIQNVVLDTVMLAKSGDPLLSPSAVATLRSRLLPQVSLITPNLPEAAALLDAPHARTEQEMLEQGRSLLAMGCGAVLMKGGHLDDEQSPDWLFTREGEQRFTAPRIMTKNTHGTGCTLSAALAALRPRHTNWADTVQEAKSWLSSALAQADTLEVGHGIGPVHHFHAWW | Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine.
Catalytic Activity: 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+)
Sequence ... |
P44697 | MSNVKQVLTIAGSDSGGGAGIQADLKTFQMRGVFGTSAITAVTAQNTLGVFDIHPIPLKTIQAQLEAVKNDFQIASCKIGMLGNAEIIECVADFLADKPFGTLVLDPVMIAKGGAPLLQRQAVSALSQKLLPLADVITPNIPEAEALTGIAIVDDISIQQAAKALQKQGAKNVIIKGGHSLNSQSELCQDWVLLADGRHFTLQSPRFNTPHTHGTGCTFSACLTAELAKGEPLQSAVKTAKDFITAAISHPLNIGQGHGPTNHWAYSRL | Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+)
Sequence Mass (Da): 28295
Sequence Length: 269
Pathway: Cofactor biosyn... |
O25515 | MVKIYPQVLSIAGSDSGGGSGIQADLKAFQTLGVFGTSVITCITAQNTQGVHGVYPLSVESVKAQILAIRDDFSIKAFKMGALCNAQIIECVADTLETCDFGLCVLDPVMVAKNGALLLEEEAILSLKKRLLPTTHLLTPNLPEVYALTGVQVRDDKSASKAMGVLRDLGVKNAVIKGGHTEHFQGEYSNDWVFLEDAEFILNAKRFNTKNTHGTGCTLSSLIVGLLAQGLDLKNAISKAKELLTIIIQNPLNIGHGHGPLNLWSIKELV | Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+)
Sequence Mass (Da): 28925
Sequence Length: 270
Pathway: Cofactor biosyn... |
A1TYG6 | MGTVRSQIRPGLYAITDNRLTPADTLIVSVEAALAGGARLVQYRDKGSTASERLVQARNLNSLCQGFDVPLLINDDPELAARVGAAGVHLGQDDCSLVDARRLLGEHAIIGITCHHSLNLAQTAVDGGADYLAFGRFYDSATKPGAPPASPDVLTEAKALGLPITAIGGITGNNAEPLIRAGADLVAVVGGLFGGQPSDIEARAKAFNRQFARHHPLFSLSE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
Q8TMD6 | MNQKNSNPKNPPRKISLLKQIDFYLVTDSGLSKKGTLSDVREAVDAGCKIVQYREKNKSTKEMIDEASEIKRICGDRAIFLVNDRIDVALAVDADGVHIGQDDMPIEIAKKLLGPEKIIGLTVHNVEEALEAERNGADYVGLGSIFDTSTKKDAGKGIGPASIKEVKNAIKIPVVAIGGINRENCIPVVENGADSFVAISAVVCSDDVKRETRKFIEIIREIKNSGRQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
A7IA09 | MRLDLYVITDGAIGGGRSHAEIARFACAGGADAIQLRDKACGPDALCRIGREIRAITRDTGTLFIVNDRLDVALACGADGVHLGQGDLRVDTARRLAPRPFMIGVSVGNAEEAISAVVAGADYVAASPIFATSSKDDAGPGCGISGLREIRAAVAVPVVAIGGITRDNVAEVIAGGADSIAVISAVVGQPDIVAAARDLRERITTAKEQYREKRDA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
Q602R3 | MKNSMYLPFPSKGLYAITPDRLQGDALLAAAESAILGGAAVVQYRPKSGPASDRLSDGIRLQELCRTAGIPLIVNDSPRLAAEIGADGVHLGKNDGSVAAARHVLGDRAIVGISCYDSLERALRAEAEGANYVAFGALFPSATKPCASRARLETLREAGTRLQIPIAAIGGIDTTNAGQVIGAGADLVAAVEAVFGAADVARAARELCSLFHAPRKRRPRCDDA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
Q2FM63 | MDCGLYIITDEILAPGCSHIQIAKESLSGGAKIIQLRDKRRNAAELYAIAQEIRSLCTQHHARFIVNDRLDIALAVQADGVHLGQDDLPLSAARLLAPRPFIIGVSVGTVEEAVLAEKGGADYLGVGPVYPTGTKADAGPAVGPGLIRSIRERVAIPIIAIGGINLTNAGDVLAAGADGIAVISAVICSPDIAAASRKFADLMIHS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
Q2RGI8 | MPQWDLYVVITTKLGGGRPTLELVRGALAGGATAIQLREKELPARELVELGRAIRELTRDAGATFIVNDRLDIALAVEADGLHIGQEDLPAPVARKLLGPEKILGVSAGTTDEARQAEVDGADYLGVGSIFATGSKGDAGSPIGLEGLRAIRAAVKIPIVGIGGINPDNAAGVIAAGADGVSVISAVIGAADVAAAARRLREVVTRARGK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
Q2S2A8 | MENTSTNGEPARAEKSIGRLHVLTDFHLQQDRSHAELARLAIRGGADTIQFRQKHGGIQNKLLEARKVATVCADASTPLLIDDHLDIAQATDADGVHLGQDDFPIDAARSVLGPSPIIGGTASKPHEAAEAYEQGADYIGFGPVFPTTSKRNPKSVKGPDGLADACEAVPIPVIAIGGITHDRVRSVLEAGAHGVAVLSAVDTARNPEQATARFRAAIDGVLREADS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
A4XBL2 | MSSLGRLHLITDARAGRNPLTVVQAALSVARTELVVQVRVADDATDRQAYDLARRVIALCARYDATCLVNDRLHVALAVGAAGGHVGADDLPVGAARAVLGSAAVLGVTARDADTAVEAVAAGASYLGVGPVHPTTSKEGLPPAIGVAGVGVVAAAVSVPVIAIGAVTAADVPVLRAAGAYGVAVIGALSHAADPAGATAALLEALTW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
A8G8F3 | MTDITTPFPATPHKLGLYPVVDSVEWIARLLDAGVTTLQLRIKDLPDEQVEDDIAAAIALGKRYDARLFINDYWQLAIKHGAYGVHLGQEDLDTTDLAAIHRAGLRLGVSTHDDSELARAIAVKPSYIALGHIFPTQTKDMPSAPQGLVELKRHIAGLSDYPTVAIGGISIDRVAAVLDCGVGSVAVVSAITQAPDWRAATAQLLQLIEGKE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
C4XIJ2 | MKPNFDPTLYLVTDRGCLAGRDLLDVVGRAVAGGAKLVQLREKNACTREFVELARALVGLVRPLGARLVINDRVDVALACDADGVHVGQDDMRPADVRALIGPDRLLGLSVTGEDEARAARGEPVDYLGAGPVFATATKKDAGAPQGIEGLIRMIALAEVPVVAIGAVTAANAAAVMAAGAAGLAMVSAICAAPDPEAAARELRVIAEQGR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate +... |
Q3SPS2 | MVSFYDREFSSRLLIGTALYPSPKIMQDAIRAAGSQIVTVSLRRETAGGKTGDAFWSLIRELDVTVLPNTAGCKTVREAVTTAKLARELFGTSWIKLEVIADNDTLQPDVVGLVEAAAILIRDGFDVFPYCTEDLGVAMRLVEAGCKVVMPWAAPIGSAKGITNRDALKLLRERLPDVTLVVDAGLGAPSHAAQACELGYDAVLLNTAVAKAADPVVMAGAFRLAVEAGRNAYEAGLMEARDFASPSTPVVGTPFWHAVS | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate... |
Q4FMP0 | MVNDKLIIDKKKFNSRLIVGTGKYKSMAECAKAIKLSGAEIVTVAVRRVNISDKKKPLLMDYIDPKKITYLPNTAGCFNSEEALRTLRLAREIGGWKLVKLEVLGDKKNLFPDMIETLKSTEVLTREGFRVMVYCNDDPLMAKRLENVGACAIMPLAAPIGSGLGIQNTTNIKIIRSQTKLPLIIDAGLGQASDAAIAMELGCDGVLANTAIAKAKKPFQMALAFKNGVIAGRQSYLAGRIEKSIYGSASSPKTGII | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate... |
Q8ZAP9 | MLKIADTTFTSRLFTGTGKFSSPELMLEALRASGSQLITMAMKRVDLQSGNDAILAPLRQLGVRLLPNTSGAKTAEEAIFAARLAREALNTHWVKLEVHPDVRYLLPDPIETLKAAEVLVKEGFVVLPYCGADPVLCKRLEEVGCAAVMPLGSPIGSNLGLRTRDFLQIIIEQSKVPVVVDAGIGAPSHALEALELGADAVLVNTAIAVAHSPVQMAHAFRLAVESGERARLAGLGASPFNPSQPDTLQLRATATSPLTGFLSQLEEQDHV | Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate... |
P30140 | MKTFSDRWRQLDWDDIRLRINGKTAADVERALNASQLTRDDMMALLSPAASGYLEQLAQRAQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNRIKRKTLDEADIARESAAIREMGFEHLLLVTGEHQAKVGMDYFRRHLPALREQFSSLQMEVQPLAETEYAELKQLGLDGVMVYQETYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDNWRVDSYMVAEHLLWLQQHYWQSRYSVSFPRLRPCTGGIEPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDRVIPLAINNVSA... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated cleavage of tyrosine to 2-iminoacetate and 4-cresol.
Catalytic Activity: L-tyrosine + NADPH + S-adenosyl-L-methionine = 2-iminoacetate + 4-met... |
Q9S498 | MKTFTDRWRQLEWDDIRLRINGKTAADVERALNAAHLSRDDLMALLSPAAADYLEPIAQRAQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNRIKRKTLDEVDIQRECDAIRKLGFEHLLLVTGEHQAKVGMDYFRRHLPTIRRQFSSLQMEVQPLSQENYAELKTLGIDGVMVYQETYHEAIYAQHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDNWRVDCYMVAEHLLWMQKHYWQSRYSVSFPRLRPCTGGVEPASVMDEKQLVQTICAFRLLAPEIELSLSTRESPWFRDHVIPLAINNVSA... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated cleavage of tyrosine to 2-iminoacetate and 4-cresol.
Catalytic Activity: L-tyrosine + NADPH + S-adenosyl-L-methionine = 2-iminoacetate + 4-met... |
A3DEB6 | MKKVILVRYGEILLKGLNRPIFEDKLMSNIKRAIHKLGKVRITKSQARIYIEPLEENYDFDEALKLLSKVFGIVSVSPVWKIDSDFECIKENSVKMVKDLINREGYKTFKVETKRGNKRFPMDSPEISRQLGGYILRNVPELSVDVKNPDFILYVEVREFTYIYSEIIQAVCGMPLGSNGKAVLLLSGGIDSPVAGWMIAKRGVEIEAVHFYSYPYTSERAKEKVIELTKILATYCQKINLHIVPFTEIQLEINEKCPHEELTIIMRRAMMRIAEIIANKTGALALVTGESVGQVASQTIQSLVVTNAVVSLPVFRPLIG... | Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiami... |
A9NHG7 | MEKAILIRFGDLVLKGKNKPKFIGQIKKNIRSKLKNVNVEYTFQHDRIYVHFNEVDSDEVIKQLGYVSGIHSFSYIYKTTKDIESIAQLAKEVIQKEVKLPTTFKIETKRTDKNYPLKSLEISQKVASLVLPSFDGLKVEVRNPETVLDIELRSEGTYIYVGKIPALGGFPIGLGGKGLVMLSGGIDSPVAAHLMMKQGIDVELFHFESTPLTPLESVQKVIEIAKKLAYYTPYNKIKLHLVPFTKIHEAILSYVADPYIITIMRRMFYRLGEIYANQHGLDTLINGESVGQVASQTLSSIKVIENVTSIPILRPVITYD... | Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiami... |
Q9YEW8 | MEYNVVLVRYSEIAVKGGYTRSRMERLLLRALEESLAAAGVEAEVERLQGRVLVRLRSPGDAAAAARASARVFGVKSVSPAVEVEYSGIEDLAEKAAEFFGERVRGRVFRVRARRSGVEGFTSKDVERLLGKLLLERGAGGVDLEKPEYTAYVEVRGRRAYFFDTINPGPGGLPVGSEEPSLALYSGGFDSGVAAWMIMRRGSPVHLAFYDFGVPEALEVAVEGAKTLAGEWAWGYRPRLYVVNFRGAALIVNGLVKPSYRTLVLRRLMLLHAQDLAAREGFEALVTGESVGQVASQTVRNLRLISSGLELPVLRPLAGM... | Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiami... |
P14611 | MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVPAMTINKVCGSGLKAVMLAANAIMAGDAEIVVAGGQENMSAAPHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGITAENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIVPVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAGTVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF... | Function: Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA . Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation . Also catalyzes the reverse reaction, i.e. the cl... |
Q6AZA0 | MTSRALYSTRSQLCRHLAHKYLSRSYSTRPSLNEVVIVSAVRTPIGSFKGSLSTLPATKLGSIAIKGAIDKAGIPVEEVKEVYMGNVLQAGEGQAPTRQALLGAGLPLSTPATTINKVCASGMKSIMLASQSLMCGHQDVMVAGGMESMSQVPYIMAREAPPYGGVKMEDLIVKDGLTDVYNKFHMGNCAENTAKNSSISREEQDAFAIKSYTLSKAAWESGILAKEVVPVSIPQRGKPDVVVKEDEEYRKVDFSKVPKLKAVFLKENGTVTAANASTLNDGAAALVLMTADAAQRLNVTPLAKIVAFADAAVAPIDFPI... | Function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened ... |
Q57190 | MAMGEFDLIKRYFQQQILVDDSVQLSIGDDCALVSVPENYQLAITTDTMVENTHFLPTISPEDLAYKAVATNLSDLAAMGAQPKWVSLALTLPNVDENWISTFSQSLLHTLKQYNVTLIGGDTTKGNLSITITAQGFVEKNKGICRHKAQIGDLIYVSSTLGDSAAGLTQILLGKSAVDSDDVFLQQRHLRPTPRIELGQALIGIAHVAIDLSDGLISDLGHILERSQCSAEVELTALPLSSSILNKYDRTQAEQFALSGGEDYELCFTIPPEYKDELELRLKKLNVPCTCIGKINEKCGDFSPRFLRDGKPVNITFSSG... | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 36016
Sequence Length: 328
Pathway: Cofactor biosynthesis; thiamine dip... |
Q9HNP1 | MDERAALELVGGLVSRAGDDAAVVGDTALTIDMLHDATDFPSGTTRYTAGWRSVGASLSDVAATGATATAAVAAYGAPGFDDDELAAFVTGARDVCTAVGAEYVGGDLDGHSEFTVATAAIGDADHRVTRSGARPGDSVVVTGSLGRSAAAMALFDAGDTERANDLFQFMPRVAAGRVLGAHATAMMDASDGLARSLHQLAAASDCGMAVDSGRLPVADALAEVTADPVERAVSFGGDFELVAAVPPERVEAARAAVPGSLSVVGRVTAAADGVRLDGDALADDGWTH | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 28864
Sequence Length: 288
Pathway: Cofactor biosynthesis; thiamine dip... |
P24752 | MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAV... | Function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened... |
Q8F0S9 | MKENLILKESEVIRILYPPGIVQTDDCYLDEEGRIYTTDTICEGTHFRIEWSGPKEIAQKLVEVNVSDIAAGGGIPTKAFLNLGLSTQCSKEEWILPFSISLQESLSSYNIELCGGDTYRSSSLNLTLTLIGVTTKPWKRSGGKDGDFLYLTGSVGLSLLGYKILKEGLDIPEPLRSLALERHLTPKARLKVSKELSKNSPVSCCMDLTDGLLLDLPKLASSSNLGLKIDLEKIPILSNILTYLSLGEVLSSGEELELIFLSPVELPKTLCETSLTKIGNTTSDWKGVKFFQGNSEKTFEHLGFEHF | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 33838
Sequence Length: 307
Pathway: Cofactor biosynthesis; thiamine dip... |
Q2FSV9 | MDDRDLLEIIRPVCGSDTCSDDCAILTLPCGALVTSTDMLHERSDFPAGMTGWQIGWMSVAVTISDIAAMGAEPLQIVLAIGLDTEERLAEIVLGAQACCDTYGAVYAGGDLDAHSELTIVSTGVGIIRDGEPVRRGGAKPGDIICVTGTLGRAILGLTGDSRFWKDLCEPQPRVREGTVARLAGAHAMMDISDGLAISLYDIAAESHVGMEISSGRIPLPPEADVQVALEAALYGGGDFELLFFISEEKMKNLTIPVTQIGRVSEGLKITMDGMELPKKGYLHHW | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 30431
Sequence Length: 286
Pathway: Cofactor biosynthesis; thiamine dip... |
Q60337 | MDEMKVIEIIKKTLKFSNENIVKGIDDDCAIIKIDENFYLVATTDMMVKKAHIPSILSPYEIGGRILTANVSDIASMGAKPLAFLVSISLSKEEANEKFIKELYSGLDDFSKLYDCPVVGGDTNRGDELILSGTAFGITDNPIYRRGKVGDDICVTNDLGRVYCALTLYYMLKENKISYKEFERLCQKYPKIIEKLRKPIARIKEGLLMNKLINGCCDISDGLGKEITYFKNFEIYSDRIFKLIPEDVIEFCDAFNLNPIKVALNSGEEFELLFTTSKFNKVKDSLKGYSKIYKIGKIIEDGQFIDGEEFYGGGYIHKW | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 36160
Sequence Length: 319
Pathway: Cofactor biosynthesis; thiamine dip... |
Q8TXQ3 | MSSGFKRPSPRTWRPKEEEELIELIVEACPTEGPRVKAGDDDAAVLPDGTVVNFDAMTRSRHVPKELRDRDLGWKFVASVVSDVGAMGGEPSFFGFSVCLDDEVDVEQLVLGISEGLREFGVSLIGGDVVEGEELVLSGTCLGKLKGEPLLMSNARPGDVVAVTGPLGGPNAFVRAILNGMEPEETLYERFARPRPPVEVGVELARGGYRAAVTDISDGLLAEAEAIARRSGVAIEIHTWKVPVDEGVEEVAQEFDVDPVDLALEGGEDYEFLICGPEDVVKEFGLTTIGRVTEGEGVRIVRNPRARSE | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 33289
Sequence Length: 309
Pathway: Cofactor biosynthesis; thiamine dip... |
O27447 | MHDRISSLGEKKLISRIISRARSVFGSSEVMGLGDDAALIDAGEEFLVLTSDLLLETRHFPDPERPRDMGWKTVTVNMSDLAAMGSRPEGFILSVALPDLELEFFDSLMDGVIEACCHYQAPLIGGDTNEADEIILSGTAIGRAEKDMVLMKSGARPGDLVAVTGPLGVGAAGTELILSGRDTGGFENAVERSLRPVARIEEGLILAESGLVSSATDITDGLVSELGELMDASGTGMRIYEDRLPLGREVPEIASILGRDPLELALYYGEDFELVFTAPPTGMEELSDMMELHVIGEVTVGGGIEMVDKDGVTYKLHVRG... | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 35012
Sequence Length: 327
Pathway: Cofactor biosynthesis; thiamine dip... |
P9WG70 | MTTKDHSLATESPTLQQLGEFAVIDRLVRGRRQPATVLLGPGDDAALVSAGDGRTVVSTDMLVQDSHFRLDWSTPQDVGRKAIAQNAADIEAMGARATAFVVGFGAPAETPAAQASALVDGMWEEAGRIGAGIVGGDLVSCRQWVVSVTAIGDLDGRAPVLRSGAKAGSVLAVVGELGRSAAGYALWCNGIEDFAELRRRHLVPQPPYGHGAAAAAVGAQAMIDVSDGLLADLRHIAEASGVRIDLSAAALAADRDALTAAATALGTDPWPWVLSGGEDHALVACFVGPVPAGWRTIGRVLDGPARVLVDGEEWTGYAGW... | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 34331
Sequence Length: 333
Pathway: Cofactor biosynthesis; thiamine dip... |
A9A3T2 | MSKLDESEIIKIFQRKLGNKNSEDVEIFKLKQNIIAKTDTLVQSTDIPPKMKLGEAARKSVVACVSDFAAKGVKPQYGIISINFPSNISRSKVEEAATGFRKACSEFGISILGGDTNAGKEIVFNVCLFGSAEKIVPRNGSESKDLIFATGPFGYTGAGLSILLYKKKGKREFVAKAIKAVTHPKPRVDFGVKNKRYFTSSMDSSDGLSTTLNEMAKQSKKKFVINNSPHKKDLGEFAKSNQDNLVFHGGEEYEFVFTINPKHKKTILKNAKSLRTPIIEIGYVTTGKGVILQRDNKDIPLKDKGWKHFR | Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Mass (Da): 34329
Sequence Length: 310
Pathway: Cofactor biosynthesis; thiamine dip... |
P14610 | QAVLGAGLPCNTTTSPIIKVCASGMK | PTM: Succinylation, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 2561
Sequence Length: 26
Subcellular Location: Mitochondrion
EC: 2.3.1.9
|
C4XIJ3 | MPFAAAVFADLARIRQNAPLVVNITNNVVTNATANALLALGASPAMTHHPADAAELAALAGALVCNMGTPGGENIEAMLAAGGAANAGGVPVVFDPVAAGVTSRRREVAGRMLETVRLAAVRGNASEILALAGEAALSKGADSQHASREAAPAAVALARSLGCTVCVSGEVDVVTDGERVVELAGGHAMMTRVTGLGCTATAFVGAFLAVNPDYFAATCHAMAVMAAAGRLAAAGVAGPGSLAVRFLDVVYSLTEAEIAAGARVSA | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 26257
Sequence Length: 266
Pathway: Cofactor biosynthesis; thiamine diphos... |
Q6GEY3 | MNYLNNIRIENPLTICYTNDVVKNFTANGLLSIGASPAMSEAPEEAEEFYKVAQALLINIGTLTAQNEQDIIAIAQTANEAGLPIVFDPVAVGASTYRKQFCKLLLKSAKVSVIKGNASEILALIDDTATMKGTDSDANLDAVTIAKKAYAIYKTAIVITGKEDVIVQGDKAIVLANGSPLLARVTGAGCLLGGIIAGFLFRETEPDIEALIEAVSVFNIAAEVAAENENCGGPGTFSPLLLDTLYHLNETTYQQRIRIQEVE | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28040
Sequence Length: 263
Pathway: Cofactor biosynthesis; thiamine diphos... |
Q4QLQ1 | MIYLNNVILNDKTLPMCFNLNVKAGERVAIIGESGAGKSTLLNLIAGFEFPAQGEIWLNDKNHTRSAPYERPVSMLFQENNLFPHLTVQQNLALGIKPSLKLTALEQEKIEQAACSVGLGDYLERLPNSLSGGQKQRVALARCLLRDKPILLLDEPFSALDQKLRVEMLALIAKLCDEKDLTLLLVTHQPSELIGSIDQVLVVENGQISQLQKGV | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23740
Sequence Length: 215
S... |
Q0I354 | MIKLNTIFDYPNISLHFDLHISLGEKIAIIGESGAGKSTLLNLIAGFEPVKQGEIRLNGENHTYTAPHQRPVSILFQEHNLFTHLTVWQNIAIGLRADLKLSKEEIKQLEKVASAVGLTDFLSRLPKELSGGQRQRVALARCLLRDKPILLLDEPFSALDPHLRQEMLTLIDKFCREKQLTLLLVTHQLSEVIDKIDRIVEIKNGQATEREIPR | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24251
Sequence Length: 214
S... |
Q28VL7 | MLHLENIRVRQGSFTLSAHLTIAKGARVALMGASGSGKSTLLSTLSGFLWPDAGRITMAGADVAKTPVADRPISILFQDGNLFPHLSVFDNVALGIRPNLKLGSEDERRVTRALTQVGLEGMEQRKPSALSGGQQSRVALARMLLRDKPVALLDEPFSALDPGLRREMLSLVRKLCDETGQTLIMATHDLRDAERLCDRVLLLDDGKVVLDAPLAEAVANNAEPLRPWM | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24853
Sequence Length: 229
S... |
Q6D0F3 | MIALEKLTYFYQHLPMRFDFHVKPGERIAILGPSGAGKSTLLNLVAGFLMADSGELRLNGESHRETSPAKRPVSILFQENNLFPHLTIGQNIALGLHPGLRLNAAQRATLQQIADRVGLTDLLDRLPSQVSGGQRQRAALARCLVRHQPILLLDEPFSALDPALRQEMLDLVESVCEERKFTLLMVSHNLDDAMRIAKRTVLIVDGQIYYDGPTQALQDGSADAAAILGISRSSSD | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25943
Sequence Length: 236
S... |
Q1GCR8 | MLRLEDLDIRKGSFCLSGTASIGAADSVAVIGPSGAGKSTLLEAIAGFQPLHAGQVLWRGEDLTAHRPGQRPVAMLFQDGNLFPHLTVRQNAGLGIDPNRKLRPKERQTVEEAIARVGLGGLEERKPAELSGGQQSRAALARVLVQRRDILLLDEPFAALGPALKAEMLDLVKEITSENGVTLLMVSHDPDDARRIADQVILIAEGQLYPPAPTHALLDNPPPALRGYLGA | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24701
Sequence Length: 231
S... |
Q8ZRV2 | MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGDDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIAHQMGIESLMTRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKSHIL | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import . Responsible for energy coupling to the transport system (Probable). Is also involved in thiamine pyrophosphate (TPP) transport .
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Per... |
Q1JPJ8 | MKPPAACTGDALDVVAPCSAVNHLRWDLSAQQIAELTTELIEQTKRVYDCVGAQEPQDVSYENTLKALADVEVSYTVQRNILDFPQHVSPSKDIRTASTEADKKLSEFDVEMSMRQDVYQRIVWLQEKVQKDSLRPEASRYLERLIKLGRRNGLHLPEETQEKIKSIKKKLSLLCIDFNKNLNEDTTFLPFTREELGGLPEDFLNSLEKTEDEKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEENCAILRELVRLRAQKSRLLGFSTHADYVLEMNMAKTSQVVATFLDELAQKLKPLGEQERAVILELKRAE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the metabolism of neuropeptides under 20 amino acid residues long (By similarity). Involved in cytoplasmic peptide degradation. Able to degrade the amyloid-beta precursor protein and generate amyloidogenic fragments (By similarity). Also acts as a regulator ... |
P52888 | MKPPAACAGDMADAASPCSVVNDLRWDLSAQQIEERTRELIEQTKRVYDQVGTQEFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPSKDIRTASTEADKKLSEFDVEMSMREDVYQRIVWLQEKVQKDSLRPEAARYLERLIKLGRRNGLHLPRETQENIKRIKKKLSLLCIDFNKNLNEDTTFLPFTLQELGGLPEDFLNSLEKMEDGKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEENCAILKELVTLRAQKSRLLGFHTHADYVLEMNMAKTSQTVATFLDELAQKLKPLGEQERAVILELKRAE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation . Able to degrade the amyloid-beta precursor protein and generate amyloidogenic fragments . Also acts as a regulator of cannabinoid signaling pathw... |
A0QYB5 | MRLGTTAFAIASATALGLGLTACGAGDPAANSDTTRIGVTVYDMSSFITAGKEGMDAYAKDNNIELIWNSANLDVSTQASQVDSMINQGVDAIIVVPVQADSLAPQVASAKAKGIPLVPVNAALDSKDIAGNVQPDDVAAGAQEMQMMADRLGGKGNIVILQGPLGQSGELDRSKGIEQVLAKYPDIKVLAKDTANWKRDEAVNKMKNWISGFGPQIDGVVAQNDDMGLGALQALKESGRTGVPIVGIDGIEDGLNAVKSGDFIGTSLQNGTVELAAGLAVANRLAKGEPVNKEPVYIMPAITKDNVDVAIEHVVTERQQ... | Function: Part of an ABC transporter complex involved in D-threitol import. Binds D-threitol. Functions in the transport for the degradation pathway of D-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36350
Sequence Length: 349
S... |
Q9YB03 | MVGRLARLRDSIAHTGVPMKTVEDENFHITLRFIGEVSEPVAAEIGERLASIRFERFRIELRGLGAFPRPDRPRVVWVGVGGGAGELRRIRDEVERILTSMGFSPEKQEFHPHVTLARIKGARNLPALVKLLREMGDVEVGSVEVSSIRLKQSILTRQGPIYKTLYEVKAASSGRV | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Mass (Da): 19666
Sequence Length: 176
EC: 3.1.4.58
|
O66967 | MKVVRAFVGFFTSKSINEVAERIKKEVDLKIMGKWVEPQNVHMTLQFLGDITEAQAIEVIKNLQEISKKNIPFRIKYKGLGVFPDVKRPRVLWIGVSEGANKLTNLAKEVARLNAKKGIIPKNSKNFVPHVTICRIKSYDRKTLNELLRKYRTVEFGEDEVNKIALISSTLTSVGPIYTVVEEFYLGG | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Mass (Da): 21366
Sequence Length: 188
EC: 3.1.4.58
|
O28125 | MRLFVAVDVDDSIREKVKPILKELSGVSGVKAVEPENLHITLLFLGEVGEEKLARIEERLSEVTFQPFKISFEGVGAFPNPGSPRVVWIGVKEEGELTRLANSVYEKLKKLGFRRDKDFKAHLTVGRVKRKNPEVADIVRKYSSESFGEMEVRDFRLKQSILTPKGPIYKDLRVFE | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Mass (Da): 20060
Sequence Length: 176
EC: 3.1.4.58
|
O34570 | MPDIRPHYFIGVPIPEGIANPIYQAAKNEPILTFQKWVHPLDYHITLIFLGAADETQIKKLEGSLAEIASEIDPFSIKFGKIDVFGDRRKPRVLHLEPKKNKTLDRLREHTKQAVLQAGFQVEKRPYHPHMTLARKWTGEDGFPAHVPFESGEVSMMAERFSLFQIHLNQSPKYEEIFKFQLS | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Mass (Da): 21146
Sequence Length: 183
EC: 3.1.4.58
|
Q9SMB8 | MATTNNKNLTITEKVYVRVRLANEADISHIYKLFYQIHEYHNYTHLYKATESSLCDLLFKANPNPLFYGPSVLLLEVSPTPFENTKKDEKFKPVLKTFDLRATVEDKEAEEFKSKSCGDEKEDVFIAGYAFFYANYSCFYDKAGIYFESLYFRESYRKLGMGSLLFGTVASIAANNGFASVEGIVAVWNKKSYDFYVNMGVEIFDEFRYGKLVGDALQKYADKEKA | Function: Synthesizes amides which are involved in stress response in the cell wall. Catalyzes the synthesis of hydroxycinnamic acid amides from hydroxycinnamoyl-CoA thioesters and various hydroxyphenylethylamines such as 4-coumaroyl-CoA and sinapoyl-CoA.
Catalytic Activity: (E)-feruloyl-CoA + tyramine = CoA + H(+) + N... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.