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stringlengths 6
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B2FQN4 | MKALVKREAAKGIWLEEVPVPTPGPNEVLIKLEKTAICGTDLHIYLWDEWSQRTIKPGLTIGHEFVGRVAALGSAVTGYEIGQRVSAEGHIVCGHCRNCRGGRPHLCPNTVGIGVNVNGAFAEYMVMPASNLWPIPDQIPSELAAFFDPYGNAAHCALEFNVIGEDVLITGAGPIGIIAAGICKHIGARNVVVTDVNDFRLKLAADMGATRVVNVANQSLKDVMKELHMEGFDVGLEMSGNPRAFNDMLDCMYHGGKIAMLGIMPKGAGCDWDKIIFKGLTVQGIYGRKMYETWYKMTQLVLSGFPLGKVMTHQLPIDDFQKGFDLMEEGKAGKVVLSWN | 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 degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.103
|
Q5SKS4 | MRALAKLAPEEGLTLVDRPVPEPGPGEILVRVEAASICGTDLHIWKWDAWARGRIRPPLVTGHEFSGVVEAVGPGVRRPQVGDHVSLESHIVCHACPACRTGNYHVCLNTQILGVDRDGGFAEYVVVPAENAWVNPKDLPFEVAAILEPFGNAVHTVYAGSGVSGKSVLITGAGPIGLMAAMVVRASGAGPILVSDPNPYRLAFARPYADRLVNPLEEDLLEVVRRVTGSGVEVLLEFSGNEAAIHQGLMALIPGGEARILGIPSDPIRFDLAGELVMRGITAFGIAGRRLWQTWMQGTALVYSGRVDLSPLLTHRLPLSRYREAFGLLASGQAVKVILDPKA | 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
Sequence Mass (Da): 36638
Sequence Length: 343
Pathway: Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.103
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A5F0N6 | MKIKALSKLKPEQGIWMNEVDMPELGHNDLLIKIKKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVRGFQIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRTGCFSEYLVIPAFNAFKIPDGISDDLASIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLDLARKMGVTRAVNVAEQNLEDVMKELGMTEGFDVGLEMSGVPSAFSAMLKTMNHGGRIALLGIPPSSMAIDWNQVIFKGLVIKGIYGREMFETWYKMASLIQSGLDISPIITHHFKVDDFQKGFDIMRSGASGKVILDWQ | 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 degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.103
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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 + an alcohol + H2O
Sequence Mass (Da): 25136
Sequence Length: 221
Subcellular Location: Cytoplasm
EC: 1.11.1.24
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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 + an alcohol + H2O
Sequence Mass (Da): 23283
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
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 + an alcohol + H2O
Sequence Mass (Da): 28703
Sequence Length: 250
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
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 + an alcohol + H2O
Sequence Mass (Da): 25308
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
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 + an alcohol + H2O
Sequence Mass (Da): 24452
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
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 + an alcohol + H2O
Sequence Mass (Da): 24946
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
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 + an alcohol + H2O
Sequence Mass (Da): 24969
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
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 + an alcohol + H2O
Sequence Mass (Da): 23884
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
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 disassembly of transcriptional regulatory complexes . Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway .
PTM: Proteolytically cleaved by caspase-7 (CASP7) in response to apoptosis, leading to its inactivation.
Catalytic Activity: prostaglandin H2 = prostaglandin E2
Sequence Mass (Da): 18697
Sequence Length: 160
Domain: The PXLE motif mediates interaction with EGLN1/PHD2.
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subcellular Location: Cytoplasm
EC: 5.3.99.3
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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 disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway.
PTM: Proteolytically cleaved by caspase-7 (CASP7) in response to apoptosis, leading to its inactivation.
Catalytic Activity: prostaglandin H2 = prostaglandin E2
Sequence Mass (Da): 18721
Sequence Length: 160
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subcellular Location: Cytoplasm
EC: 5.3.99.3
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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- or diphosphate, oxothiamine, oxythiamine, thiamine disulfide, desthiothiamine or thiochrome as substrates . Does not display thiaminase II activity, as it is unable to hydrolyze thiamine . Is able to carry out two successive steps in the salvage of thiamine breakdown product, whereas two separate enzymes are required in Bacillus species (Probable). May also serve a damage pre-emption function by hydrolyzing products that would otherwise do harm (Probable).
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Mass (Da): 25234
Sequence Length: 224
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.1.-
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F4KFT7 | MRFLFPTRLINNSSLGLLRSPHTTAPIRSLWFRTKSPVFRSATTPIMTAVAFSSSLSIPPTSEEALPGKLWIKFNRECLFSIYSPFAVCLAAGNLKIDTFRQYIAQDVHFLKAFAHAYELAADCADDDDDKLAISDLRKSVMEELKMHDSFVQDWDLDINKEVSVNSATLRYTEFLLATASGKVEGCKAPGMLDTPFEKTKVAAYTLGAVTPCMRLYAFLGKEFGSLLDLSDVNHPYKKWIDNYSSDAFQASAKQTEDLLEKLSVSMTGEELDIIEKLYQQAMKLEVEFFHAQPLAQPTIVPLLKNHSKDDLVIFSDFDLTCTVVDSSAILAEIAIVTAPKDEQSRSGQQIHRMLSSDLKNTWNLLSKQYTEHYEECIESILNKKKADKFDYEGLCKALEQLSDFEKEANNRVIESGVLKGLNLEDIKRAGERLILQDGCINVFQKILKTENLNAELHVLSYCWCGDLIRAAFSAGGVDAVEVHANEFTFEESISTGEIERKVESPINKAQQFKSILQNRKNENNKKSFLSVYIGDSVGDLLCLLEADIGIVVSSSSSLRRVGSHFGVSFVPLFSGIVQKQKQHTEESSSSAWKGLSGTLYTVSSWAEIHSFALGWE | 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, inorganic pyrophosphate, CTP and dATP . Has a thiamine salvage hydrolase activity, but only against 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP) and not against N-formylamino-HMP, desthiothiamine, thiamine, ThMP, and ThDP .
Catalytic Activity: H2O + thiamine phosphate = phosphate + thiamine
Sequence Mass (Da): 68964
Sequence Length: 617
Domain: The thiamine monophosphate phosphatase activity resides in the HAD domain (297-571), while the TenA domain (85-292) has thiamine salvage hydrolase activity .
Subcellular Location: Mitochondrion
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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- or diphosphate, oxothiamine, oxythiamine, thiamine disulfide, desthiothiamine or thiochrome as substrates . Does not display thiaminase II activity, as it is unable to hydrolyze thiamine . Is able to carry out two successive steps in the salvage of thiamine breakdown product, whereas two separate enzymes are required in Bacillus species (Probable). May also serve a damage pre-emption function by hydrolyzing products that would otherwise do harm (Probable).
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Mass (Da): 25070
Sequence Length: 221
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.1.-
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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.-
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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, is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity is unlikely to be physiologically relevant. Therefore, is involved in the regeneration of the thiamine pyrimidine from thiamine degraded products present in the environment, rather than in thiamine degradation.
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Mass (Da): 27417
Sequence Length: 236
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.99.2
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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, is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity is unlikely to be physiologically relevant. Therefore, is involved in the regeneration of the thiamine pyrimidine from thiamine degraded products present in the environment, rather than in thiamine degradation.
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Mass (Da): 25585
Sequence Length: 224
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.99.2
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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 from the human stomach food assumption or processing. Is probably involved in thiamine biosynthesis. Does not display thiaminase II activity, as it is unable to hydrolyze thiamine.
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Mass (Da): 25013
Sequence Length: 217
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.99.2
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Q9UGI8 | MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVKEMEQFVKKYKSEALGVGDVKLPCEMDAQGPKQMNIPGGDRSTPAAVGAMEDKSAEHKRTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSTCHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDSILAGEIYVMVNDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKRMS | 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 the C-terminal halves of the protein can associate with each other, thereby hindering interactions with ZYX.
Subcellular Location: Cytoplasm
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P47226 | MSATHPTRLGTRTKESNACASQGLVRKPPWANEGEGFELHFWRKICRNCNVVKKSMTVLLSNEEDRKVGRLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPKEVKEMEQFVKKYKSEALGVGDVKFPSEMNAQGDKVHNCGNRHAPAAVASKDKSAESKKTQYSCYCCKHTTNEGEPAIYAERAGYDKLWHPACFICSTCGELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDHILAGKIYVMVTDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKRMMS | 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-terminal halves of the protein can associate with each other, thereby hindering interactions with ZYX.
Subcellular Location: Cytoplasm
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Q2LAP6 | MDLETKMKKMGLGHEQGFGAPCLKCKENCEGFELHFWRKICRNCKCGQEEHDVLLSTEEDRKVGRLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPKEVKEMEQFVKKYKSEALGVGDVKLPSEMNAQGDKVHNPAGDRNTPAAVGSKDKSAEAKKTQYSCYCCKNTMREGDPAIYAERAGYDKLWHPACFICSTCGELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDNILAGKIYVMVRDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKMMS | 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-terminal halves of the protein can associate with each other, thereby hindering interactions with ZYX.
Subcellular Location: Cytoplasm
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P52655 | MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLIQHMNASNMSAAATAATLALPAGVTPVQQILTNSGQLLQVVRAANGAQYIFQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPTPAQAQITATGQQQPQAQPAQTQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDVSDEEGQELFDTENVVVCQYDKIHRSKNKWKFHLKDGIMNLNGRDYIFSKAIGDAEW | 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 promotes proteasomal degradation.
Sequence Mass (Da): 41514
Sequence Length: 376
Subcellular Location: Nucleus
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Q99PM3 | MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHQHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLLQHMNASSITSAAATAATLALPAGVTPVQQLLTNSGQLLQVVRAANGAQYILQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPAPAQAPMPAAGQQQPQAQPAQQQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDVSDEEGQELFDTENVVVCQYDKIHRSKNKWKFHLKDGIMNLNGRDYIFSKAIGDAEW | 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. The cleavage promotes proteasomal degradation (By similarity).
Sequence Mass (Da): 41614
Sequence Length: 378
Subcellular Location: Nucleus
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P03001 | MAAKVASTSSEEAEGSLVTEGEMGEKALPVVYKRYICSFADCGAAYNKNWKLQAHLCKHTGEKPFPCKEEGCEKGFTSLHHLTRHSLTHTGEKNFTCDSDGCDLRFTTKANMKKHFNRFHNIKICVYVCHFENCGKAFKKHNQLKVHQFSHTQQLPYECPHEGCDKRFSLPSRLKRHEKVHAGYPCKKDDSCSFVGKTWTLYLKHVAECHQDLAVCDVCNRKFRHKDYLRDHQKTHEKERTVYLCPRDGCDRSYTTAFNLRSHIQSFHEEQRPFVCEHAGCGKCFAMKKSLERHSVVHDPEKRKLKEKCPRPKRSLASRLTGYIPPKSKEKNASVSGTEKTDSLVKNKPSGTETNGSLVLDKLTIQ | 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 RNA gene expression. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III . Also binds the transcribed 5S RNA's (By similarity).
PTM: The N-terminus is blocked.
Sequence Mass (Da): 41911
Sequence Length: 366
Subcellular Location: Nucleus
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P81453 | MRIRRRALVFATMSAVLCTAGFMPSAGEAAADNGAGEETKSYAETYRLTADDVANINALNESAPAASSAGPSFRAPDSDDRVTPPAEPLDRMPDPYRPSYGRAETVVNNYIRKWQQVYSHRDGRKQQMTEEQREWLSYGCVGVTWVNSGQYPTNRLAFASFDEDRFKNELKNGRPRSGETRAEFEGRVAKESFDEEKGFQRAREVASVMNRALENAHDESAYLDNLKKELANGNDALRNEDARSPFYSALRNTPSFKERNGGNHDPSRMKAVIYSKHFWSGQDRSSSADKRKYGDPDAFRPAPGTGLVDMSRDRNIPRSPTSPGEGFVNFDYGWFGAQTEADADKTVWTHGNHYHAPNGSLGAMHVYESKFRNWSEGYSDFDRGAYVITFIPKSWNTAPDKVKQGWP | 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
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P04867 | MDMTKTVEEKKTNGTDSVKGVFENSTIPKVPTGQEMGGDGSSTSKLKETLKVADQTPLSVDNGAKSKLDSSDRQVPGVADQTPLSVDNGAKSKLDSSDRQVPGPELKPNVKKSKKKRIQKPAQPSGPNDLKGGTKGSSQVGENVSENYTGISKEAAKQKQKTPKSVKMQSNLADKFKANDTRRSELINKFQQFVHETCLKSDFEYTGRQYFRARSNFFEMIKLASLYDKHLKECMARACTLERERLKRKLLLVRALKPAVDFLTGIISGVPGSGKSTIVRTLLKGEFPAVCALANPALMNDYSGIEGVYGLDDLLLSAVPITSDLLIIDEYTLAESAEILLLQRRLRASMVLLVGDVAQGKATTASSIEYLTLPVIYRSETTYRLGQETASLCSKQGNRMVSKGGRDTVIITDYDGETDETEKNIAFTVDTVRDVKDCGYDCALAIDVQGKEFDSVTLFLRNEDRKALADKHLRLVALSRHKSKLIIRADAEIRQAFLTGDIDLSSKASNSHRYSAKPDEDHSWFKAK | 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 containing plus-sense viral RNAs (vRNPs) . ATPase activity is probably required for vRNPs movement complex assembly . Intracellular delivery of TGBp1-containing vRNPs to plasmodesmata is facilitated by TGBp2 and TGBp3 (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 58095
Sequence Length: 528
Subcellular Location: Host cell junction
EC: 3.6.4.-
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P10600 | MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS | 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 is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive.
Sequence Mass (Da): 47328
Sequence Length: 412
Subcellular Location: Secreted
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O43294 | MEDLDALLSDLETTTSHMPRSGAPKERPAEPLTPPPSYGHQPQTGSGESSGASGDKDHLYSTVCKPRSPKPAAPAAPPFSSSSGVLGTGLCELDRLLQELNATQFNITDEIMSQFPSSKVASGEQKEDQSEDKKRPSLPSSPSPGLPKASATSATLELDRLMASLSDFRVQNHLPASGPTQPPVVSSTNEGSPSPPEPTGKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFVCGGCSTALGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGDEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECFAPFSGGSFFEHEGRPLCENHFHARRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERAGKPYCQPCFLKLFG | 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 the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity.
PTM: Phosphorylated by gonadotropin-releasing hormone-activated SRC.
Sequence Mass (Da): 49814
Sequence Length: 461
Domain: The LIM zinc-binding domains mediate glucocorticoid receptor coactivation and interaction with AR, CRIP2, ILK, LIMS1, NR3C1, PPARG, TCF3, TCF7L2, SLC6A3 and SMAD3. The LIM zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to focal adhesions and actin stress fibers. The LIM zinc-binding 3 and LIM zinc-binding 4 domains mediate interaction with TRAF4 and MAPK15. The LIM zinc-binding 4 domain mediates interaction with HSPB1, homooligomerization and targeting to the nuclear matrix. The LIM zinc-binding 3 domain mediates interaction with PTPN12.
Subcellular Location: Cell junction
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Q62219 | MEDLDALLSDLETTTSHMSRLGAPKERPPETLTPPPPYGHQPQTGSGESSGTTGDKDHLYSTVCKPRSPKPVAPVAPPFSSSSGVLGNGLCELDRLLQELNATQFNITDEIMSQFPSSKMAEGEEKEDQSEDKSSPTVPPSPFPAPSKPSATSATQELDRLMASLSDFRVQNHLPASGPPQPPAASPTREGCPSPPGQTSKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFLCSGCSTTLGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGEEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECLAPFSGGSFFEHEGRPLCENHFHAQRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERASKPYCQPCFLKLFG | 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 the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity.
PTM: Phosphorylated by gonadotropin-releasing hormone-activated SRC.
Sequence Mass (Da): 50101
Sequence Length: 461
Domain: The LIM zinc-binding domains mediate glucocorticoid receptor coactivation and interaction with AR, CRIP2, ILK, LIMS1, NR3C1, PPARG, TCF3, TCF7L2, SLC6A3 and SMAD3. The LIM zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to focal adhesions and actin stress fibers. The LIM zinc-binding 3 and LIM zinc-binding 4 domains mediate interaction with TRAF4 and MAPK15. The LIM zinc-binding 4 domain mediates interaction with HSPB1, homooligomerization and targeting to the nuclear matrix. The LIM zinc-binding 3 domain mediates interaction with PTPN12.
Subcellular Location: Cell junction
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Q2TCH4 | MEDLDALLADLQITTPPRCPVLLTDSPEKPQPTETRPPPPPYDPKTAMSNKTSDHETFPVDKDHLYSTVQKYPLPSVSPALGGGLCELDRLLNELNATQFNITDEIMSQFPTRDPSEQKAEAQKEAEKRALSASSATLELDRLMASLSDFHKQNTVSQEVEAPGAYKGSEEVSRPGDTEDLSSPRSTACVPKDLEDAPTPKSFKVVSAPGHLEVKTNQVNSDEVTASRVPDSVSGSKVPEATSVPRSDLDSMLVKLQSGLKQQGIETYSKGLCESCQRPIAGQVVTALGHTWHPEHFVCAHCHTLIGTSNFFEKDGRPYCEKDYFMLYAPRCALCELPIVQNMVTALGCTWHPEHFCCKVCKKPIGEEGFHEKDGEQYCSDDYFRLFGAVCAGCTEAVKESYISALGGLWHPQCFVCHVCHTPFINGSFFEHEGLPLCETHYHSRRGSLCAGCEQPITGRCVTAMGKKFHPQHLNCTFCLRQLNKGTFREHDEKPYCQACYARLYG | 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-dependent DNA-binding activity.
Sequence Mass (Da): 56001
Sequence Length: 506
Domain: The LIM zinc-binding domains mediate glucocorticoid receptor coactivation and mediates interaction with tcf3 and tcf7l2. The LIM zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to focal adhesions and actin stress fibers. The LIM zinc-binding 4 domain mediates targeting to the nuclear matrix (By similarity).
Subcellular Location: Cell junction
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P36897 | MEAAVAAPRPRLLLLVLAAAAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM | 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 plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation.
PTM: Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
Sequence Mass (Da): 55960
Sequence Length: 503
Subcellular Location: Cell membrane
EC: 2.7.11.30
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Q90999 | MPPRLRPLLLRVSLWVLVGSSSPALLHDRSKENGLQLPRLCKFCDVKATTCSNQDQCKSNCNITSICEKNNEVCAAVWRRNDENVTLETICHDPQKRLYGHMLDDSSSEQCVMKEKKDDGGLMFMCSCTGEECNDVLIFSAIDPHKPEEKDEISKVTIISLVPLLVISVAVIVIFYAYRTHKKRKLNKAWEKNVKPKKHKDCSDVCAIMLDDDHSDISSTCANNINHNTELLPIELDIVVGKGRFAEVYKAKLKQNTSEQYETVAVKIFPYEEYASWKTEKDIFSDVNLKHENILQFLTAEERKTDLGKQYWLITAFHARGNLQEYLTRHIISWEDLWKLGGSLARGIAHLHSDHTPCGRPKTPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPSLSVDDLANSGQVGTARYMAPEVLESRMNLENMESFKQTDVYSMALVLWEMTSRCNGVGEVKEYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSSWLNHQGIQMVCETLIECWDHDPEARLTAQCVAERFSEFKHHDKLSGRSCSEEKIPEDGSVTTAK | 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 of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways (By similarity).
PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
Sequence Mass (Da): 63308
Sequence Length: 557
Subcellular Location: Cell membrane
EC: 2.7.11.30
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P37173 | MGRGLLRGLWPLHIVLWTRIASTIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQVTGISLLPPLGVAISVIIIFYCYRVNRQQKLSSTWETGKTRKLMEFSEHCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSGRSCSEEKIPEDGSLNTTK | 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 physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.
PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
Sequence Mass (Da): 64568
Sequence Length: 567
Subcellular Location: Cell membrane
EC: 2.7.11.30
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Q62312 | MGRGLLRGLWPLHIVLWTRIASTIPPHVPKSVNSDVMASDNGGAVKLPQLCKFCDVRLSTCDNQKSCMSNCSITAICEKPHEVCVAVWRKNDKNITLETVCHDPKLTYHGFTLEDAASPKCVMKEKKRAGETFFMCACNMEECNDYIIFSEEYTTSSPDLLLVIIQVTGVSLLPPLGIAIAVIIIFYCYRVHRQQKLSPSWESSKPRKLMDFSDNCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYSSWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDSVLRDRGRPEIPSFWLNHQGIQIVCETLTECWDHDPEARLTAQCVAERFSELEHPERLSGRSCSQEKIPEDGSLNTTK | 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 of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways (By similarity).
PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
Sequence Mass (Da): 64219
Sequence Length: 567
Subcellular Location: Cell membrane
EC: 2.7.11.30
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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 of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways (By similarity).
PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
Sequence Mass (Da): 33302
Sequence Length: 297
Subcellular Location: Cell membrane
EC: 2.7.11.30
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B8E2N5 | MIFEIIVRDKKTRARLGKLKTFHGEINTPVFMPVGTQGAVKTLSPEEVEKVGAEIILSNTYHLFLRPGHEIVRKGGGLHKFMGWEKPILTDSGGYQVFSLARLRRIDEDGIYFNSHIDGTRYFYTPELVMEIQKSLGSDIIMPLDICLGYGASYWETKEALEITLRWLKRSIDYKNNSNMDHQLLFGIVQGGFYKELRKEAVERMLNIDLPGLALGGISVGEPKDKMYEIIDYTVSLLPEEKPRYLMGVGAPEDLVVGVSMGIDMFDCVLPTRLARHGVFYTSKGRKNIKNAQYKEDFSPLEEDCDCYTCRKFTKAYIRHLFLQHETFSYRLLTIHNLRFLFRLMENIRKSIREGRLEEFKKEFLTEYLRDDRENRLEKEELWSKLLI | 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 mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-aminomethyl-7-carbaguanosine(34) in tRNA + guanine
Sequence Mass (Da): 45138
Sequence Length: 388
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
EC: 2.4.2.29
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Q6P3Z3 | MVICCAAVNCSNRQGKGEKRAVSFHRFPLKDSKRLIQWLKAVQRDNWTPTKYSFLCSEHFTKDSFSKRLEDQHRLLKPTAVPSIFHLSEKKRGAGGHGHARRKTTAAMRGHTSAETGKGTIGSSLSSSDNLMAKPESRKLKRASPQDDAAPKVTPGAVSQEQGQSLEKTPGDDPAAPLARGQEEAQASATEADHQKASSSTDAEGADKSGISMDDFTPPGSGACKFIGSLHSYSFSSKHTRERPSVPREPMDRKRLKREMEPRCSGNSVAQSPPSSSLTATPQKASQSPSAPPTDVTPKPAAEAVQSEHSDASPMSINEVILSASGACKLIDSLHSYCFSARQNKSQVCCLREQVEKKNGELKSLRQKVSRSDSQVRKLREKLDELRRASLPYLPYLSGLLPPSHEPPKLNPVVEPLSWMLGTWLSDPPGVGTFPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPETHKPMHRECGFIRLKPDTNKVAFVSAQNTGIVEVEEGEVNGQELCVSSHSVSRISFAKEPHVEQITRKFRLNSEGKLEQTVSMATTTQPMTQHLHITYKKVTP | 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. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo, possibly modulating the transcriptional activity residing in the N-terminal region.
Catalytic Activity: peroxynitrite = nitrate
Sequence Mass (Da): 62571
Sequence Length: 569
Domain: The C-terminal nitrobindin region coordinates a heme and bears the isomerase activity. The N-terminal zinc finger domain likely binds DNA and may be involved in transcriptional regulation.
Pathway: Nitrogen metabolism.
Subcellular Location: Cytoplasm
EC: 5.99.-.-
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Q7Z6K1 | MPRYCAAICCKNRRGRNNKDRKLSFYPFPLHDKERLEKWLKNMKRDSWVPSKYQFLCSDHFTPDSLDIRWGIRYLKQTAVPTIFSLPEDNQGKDPSKKKSQKKNLEDEKEVCPKAKSEESFVLNETKKNIVNTDVPHQHPELLHSSSLVKPPAPKTGSIQNNMLTLNLVKQHTGKPESTLETSVNQDTGRGGFHTCFENLNSTTITLTTSNSESIHQSLETQEVLEVTTSHLANPNFTSNSMEIKSAQENPFLFSTINQTVEELNTNKESVIAIFVPAENSKPSVNSFISAQKETTEMEDTDIEDSLYKDVDYGTEVLQIEHSYCRQDINKEHLWQKVSKLHSKITLLELKEQQTLGRLKSLEALIRQLKQENWLSEENVKIIENHFTTYEVTMI | 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
Subcellular Location: Nucleus
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P24557 | MEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR | 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 malondialdehyde are formed stoichiometrically in the same amounts as TXA2 . Additionally, displays dehydratase activity, toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) producing 15-KETE and 15-HETE .
Catalytic Activity: prostaglandin H2 = thromboxane A2
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60518
Sequence Length: 533
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.3.99.5
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P36423 | MEVLGLLKFEVSGTIVTVTLLVALLALLKWYSMSAFSRLEKLGIRHPKPSPFVGNLMFFRQGFWESQLELRERYGPLCGYYLGRRMHVVISEPDMIKQVLVENFSNFSNRMASGLEPKMVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPFVQHCRRASTFCIPRPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFLQMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSALGPKNGVYIKIVSR | 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 malondialdehyde are formed stoichiometrically in the same amounts as TXA2. Additionally, displays dehydratase activity, toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) producing 15-KETE and 15-HETE.
Catalytic Activity: prostaglandin H2 = thromboxane A2
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60391
Sequence Length: 533
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.3.99.5
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Q7VFU4 | MRTQWVQQRADDKIRTQLHYAKKGIITKEMEYVANIENISAELIRQEIERGRLIIPANINHTNLKPMGIGIATRTKINSNIGSSSLASSIDEEVEKVKVSIKYGADTIMDLSTGGDLDEIRTAVIQASSVPIGTVPIYQILYDVKNDILQLDIDTMLSVLKKQAKQGVSYFTIHCGFLLSHMPFVAKRKMGIVSRGGSLMASWMMHYHKENPFYEYFDEILKICQEYDVSLSLGDSLRPGCLADASDEAQFAELKVLGELAKRAWKADVQVMIEGPGHVPLNQIERNVELQKQYCNHAPFYVLGPLVTDIAAGYDHIASAIGACVAAWKGVAMLCYVTPKEHLGLPNAKDVREGILAYKIAAHAADIARGRIGARDRDDAMSDARYSFDWNRQFELALDPDRAREYHDEALPQEVFKDAEFCSMCGPKFCSYKISQDIFKAHNAKESEDTQPLASNQ | 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)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 51083
Sequence Length: 457
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
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Q9BWD1 | MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE | 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
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Q72NZ8 | MEPVQKLQIPYKSIRLSDGTEYQSYHTEGALSGKQPADYKNGIPAFRKEWIQKRFNHSNHSQMYFAKKGIITEEMRYAAFRENMEPEFVRSEIACGRAILPSNRNHPELEPMVIGKNFLVKINANIGNSTFSSSIEEEVEKLHWAIKWGADTVMDLSTGKNIHETREWILRNSPVPIGTVPIYQALEKVKGKTENLNIQIFLETLEEQAEQGVDYFTIHAGVLLRYIPLTTNRITGIVSRGGSILAKWCQAHHKENFLYTHFDEILKVMKKYGVSISLGDGLRPGSIADANDKAQFSELETLGELTQLAWKEDIQVMIEGPGHVPMNLIKENVDLQTKICQEAPFYTLGPIVTDIAPGYDHITSAIGAAMIGWYGTAMLCYVTPKEHLGLPNKEDVKQGVIAYKIAAHAADLAKGHPGAIDRDNLLSKARFEFRWEDQFSLSLDPETAKTFHDEMLPQDRMKTAHFCSMCGPHFCSMNLTQELRKFAQEKEIQES | 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)-dependent reaction.
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine
Sequence Mass (Da): 55975
Sequence Length: 495
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.17
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Q57688 | MVILAIGGYDPTSGAGISADIKTAHTLGVYCPTITTSVIPQNNKMVYEKFDLPEENIKNQFKAVFEEFDIEYVKTGVLTKPAIDTLLKYIDKYDLKVICDPVLASTTKFSFVDEKLMEKYIELFNKSFLITPNKEEYKKIMEFIKNNNLMIRNDLYILATGIDDILMKNFKPIKTFKGFRVDKEVHGTGCVYSTAITAFLSKGYDLEEAIKEAKRFVLSSVIYAKKSKFGYNSNPTYINKEKVIKNLSYAIYLLKKMNFTLIPEVGSNIAESLPFPKDFKDVAALTGRIIKNKLGGFYIVGDIEFGASEHIAKIILSASKFNPEIRACMNIKYDGGLIKLLKDKFAVSSFDRKEEPPNVSTMEWGTKIACEKFGGVPDIIYDRGGEGKEPMIRVLGRDAIEVVKKVEVIQKIYNTLM | 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 biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole.
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Q9WZP7 | MVLVVAGFDPSGGAGIIQDVKVLSALGVKTHAVISALTVQNENRVFSVNFRDWEEMRKEIEVLTPPRVIKVGLSAPETVKRLREMFPDSAIVWNVVLESSSGFGFQDPEEVKKFVEYADYVILNSEEAKKLGEYNNFIVTGGHEKGNTVKVKYRDFVFEIPRVPGEFHGTGCAFSSAVSGFLAMSYPVEEAIRSAMELLKKILERSSGVVETEKLLRDWYRYDTLNTLDEILPEFLEIGHLTVPEVGQNVSYALPWAKNEFEVGKFPGRIRLKEGKAVAVSCASFKDRSHTARMAVTMMRYHPHMRCVVNVRYEREYVERAKKRGLKVFHYDRSKEPKEVQEKEGQSMVWMIEQAIAELKSPPDVIYDEGWWGKEAMIRVFGRNPKEVLEKIKLMVRE | 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 biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole.
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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 biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3.
EC: 2.7.1.49
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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 Mass (Da): 29124
Sequence Length: 271
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3.
EC: 2.7.1.49
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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 Mass (Da): 28634
Sequence Length: 266
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3.
EC: 2.7.1.49
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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 biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3.
EC: 2.7.1.49
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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 biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3.
EC: 2.7.1.49
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 23171
Sequence Length: 222
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 24829
Sequence Length: 228
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22249
Sequence Length: 216
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 23261
Sequence Length: 224
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 21361
Sequence Length: 206
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 21409
Sequence Length: 210
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 23859
Sequence Length: 227
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 20427
Sequence Length: 208
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 22793
Sequence Length: 212
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 21639
Sequence Length: 211
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
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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 + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 27652
Sequence Length: 260
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.10
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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 + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 27819
Sequence Length: 257
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.10
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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 + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Sequence Mass (Da): 28873
Sequence Length: 271
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.10
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P30140 | MKTFSDRWRQLDWDDIRLRINGKTAADVERALNASQLTRDDMMALLSPAASGYLEQLAQRAQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNRIKRKTLDEADIARESAAIREMGFEHLLLVTGEHQAKVGMDYFRRHLPALREQFSSLQMEVQPLAETEYAELKQLGLDGVMVYQETYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDNWRVDSYMVAEHLLWLQQHYWQSRYSVSFPRLRPCTGGIEPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDRVIPLAINNVSAFSKTQPGGYADNHPELEQFSPHDDRRPEAVAAALTAQGLQPVWKDWDSYLGRASQRL | 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-methylphenol + 5'-deoxyadenosine + L-methionine + NADP(+)
Sequence Mass (Da): 43320
Sequence Length: 377
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.19
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Q9S498 | MKTFTDRWRQLEWDDIRLRINGKTAADVERALNAAHLSRDDLMALLSPAAADYLEPIAQRAQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNRIKRKTLDEVDIQRECDAIRKLGFEHLLLVTGEHQAKVGMDYFRRHLPTIRRQFSSLQMEVQPLSQENYAELKTLGIDGVMVYQETYHEAIYAQHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDNWRVDCYMVAEHLLWMQKHYWQSRYSVSFPRLRPCTGGVEPASVMDEKQLVQTICAFRLLAPEIELSLSTRESPWFRDHVIPLAINNVSAFSKTQPGGYADDHPELEQFSPHDARRPETVASALSAQGLQPVWKDWDSWLGRASQTR | 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-methylphenol + 5'-deoxyadenosine + L-methionine + NADP(+)
Sequence Mass (Da): 43447
Sequence Length: 377
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 4.1.99.19
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A3DEB6 | MKKVILVRYGEILLKGLNRPIFEDKLMSNIKRAIHKLGKVRITKSQARIYIEPLEENYDFDEALKLLSKVFGIVSVSPVWKIDSDFECIKENSVKMVKDLINREGYKTFKVETKRGNKRFPMDSPEISRQLGGYILRNVPELSVDVKNPDFILYVEVREFTYIYSEIIQAVCGMPLGSNGKAVLLLSGGIDSPVAGWMIAKRGVEIEAVHFYSYPYTSERAKEKVIELTKILATYCQKINLHIVPFTEIQLEINEKCPHEELTIIMRRAMMRIAEIIANKTGALALVTGESVGQVASQTIQSLVVTNAVVSLPVFRPLIGMDKNEVVDIAKKIGTFETSILPYEDCCTVFVAKHPTTKPKLERIQLSESRLNMEELINKAVENTEVLTITRD | 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 thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Catalytic Activity: [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a uridine in tRNA + ATP + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 44402
Sequence Length: 392
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.4
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A9NHG7 | MEKAILIRFGDLVLKGKNKPKFIGQIKKNIRSKLKNVNVEYTFQHDRIYVHFNEVDSDEVIKQLGYVSGIHSFSYIYKTTKDIESIAQLAKEVIQKEVKLPTTFKIETKRTDKNYPLKSLEISQKVASLVLPSFDGLKVEVRNPETVLDIELRSEGTYIYVGKIPALGGFPIGLGGKGLVMLSGGIDSPVAAHLMMKQGIDVELFHFESTPLTPLESVQKVIEIAKKLAYYTPYNKIKLHLVPFTKIHEAILSYVADPYIITIMRRMFYRLGEIYANQHGLDTLINGESVGQVASQTLSSIKVIENVTSIPILRPVITYDKNDIINISKKIDTYDISILPFNDCCSIYVPRNPVTKPTIDQALKEESRFEFKELLEDALKNVQTMIITPTTDFEIALHGFDVKDALSSYTQE | 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 thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Catalytic Activity: [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a uridine in tRNA + ATP + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 46583
Sequence Length: 412
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.4
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Q9YEW8 | MEYNVVLVRYSEIAVKGGYTRSRMERLLLRALEESLAAAGVEAEVERLQGRVLVRLRSPGDAAAAARASARVFGVKSVSPAVEVEYSGIEDLAEKAAEFFGERVRGRVFRVRARRSGVEGFTSKDVERLLGKLLLERGAGGVDLEKPEYTAYVEVRGRRAYFFDTINPGPGGLPVGSEEPSLALYSGGFDSGVAAWMIMRRGSPVHLAFYDFGVPEALEVAVEGAKTLAGEWAWGYRPRLYVVNFRGAALIVNGLVKPSYRTLVLRRLMLLHAQDLAAREGFEALVTGESVGQVASQTVRNLRLISSGLELPVLRPLAGMDKDEIVEKSREIGLYDIARRQVEVCGVDQPPNPRASPQGFRSEFEKVRDIFIPPPRVFDLKGESLHSILKTLGLRG | 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 thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Catalytic Activity: [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a uridine in tRNA + ATP + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 43518
Sequence Length: 396
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.4
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P14611 | MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVPAMTINKVCGSGLKAVMLAANAIMAGDAEIVVAGGQENMSAAPHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGITAENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIVPVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAGTVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAFAAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILVTLLHEMKRRDAKKGLASLCIGGGMGVALAVERK | 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 cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB .
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 40549
Sequence Length: 393
Pathway: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
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Q6AZA0 | MTSRALYSTRSQLCRHLAHKYLSRSYSTRPSLNEVVIVSAVRTPIGSFKGSLSTLPATKLGSIAIKGAIDKAGIPVEEVKEVYMGNVLQAGEGQAPTRQALLGAGLPLSTPATTINKVCASGMKSIMLASQSLMCGHQDVMVAGGMESMSQVPYIMAREAPPYGGVKMEDLIVKDGLTDVYNKFHMGNCAENTAKNSSISREEQDAFAIKSYTLSKAAWESGILAKEVVPVSIPQRGKPDVVVKEDEEYRKVDFSKVPKLKAVFLKENGTVTAANASTLNDGAAALVLMTADAAQRLNVTPLAKIVAFADAAVAPIDFPIAPAFAVPKVLKAAGIKKEDIAMWEINEAFSVVVLANIKMLDIDPDRVNINGGAVSLGHPIGMSGARIVGHMVHNLKSGQYGLAGICNGGGGASSIVIQKF | 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 by two carbon atoms. The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA. Thereby, it plays a major role in ketone body metabolism.
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 44342
Sequence Length: 420
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion
EC: 2.3.1.9
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Q57190 | MAMGEFDLIKRYFQQQILVDDSVQLSIGDDCALVSVPENYQLAITTDTMVENTHFLPTISPEDLAYKAVATNLSDLAAMGAQPKWVSLALTLPNVDENWISTFSQSLLHTLKQYNVTLIGGDTTKGNLSITITAQGFVEKNKGICRHKAQIGDLIYVSSTLGDSAAGLTQILLGKSAVDSDDVFLQQRHLRPTPRIELGQALIGIAHVAIDLSDGLISDLGHILERSQCSAEVELTALPLSSSILNKYDRTQAEQFALSGGEDYELCFTIPPEYKDELELRLKKLNVPCTCIGKINEKCGDFSPRFLRDGKPVNITFSSGFDHFKESK | 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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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P24752 | MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL | 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 by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
PTM: Succinylation at Lys-268, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 45200
Sequence Length: 427
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion
EC: 2.3.1.9
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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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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O27447 | MHDRISSLGEKKLISRIISRARSVFGSSEVMGLGDDAALIDAGEEFLVLTSDLLLETRHFPDPERPRDMGWKTVTVNMSDLAAMGSRPEGFILSVALPDLELEFFDSLMDGVIEACCHYQAPLIGGDTNEADEIILSGTAIGRAEKDMVLMKSGARPGDLVAVTGPLGVGAAGTELILSGRDTGGFENAVERSLRPVARIEEGLILAESGLVSSATDITDGLVSELGELMDASGTGMRIYEDRLPLGREVPEIASILGRDPLELALYYGEDFELVFTAPPTGMEELSDMMELHVIGEVTVGGGIEMVDKDGVTYKLHVRGYEHLSPG | 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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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P9WG70 | MTTKDHSLATESPTLQQLGEFAVIDRLVRGRRQPATVLLGPGDDAALVSAGDGRTVVSTDMLVQDSHFRLDWSTPQDVGRKAIAQNAADIEAMGARATAFVVGFGAPAETPAAQASALVDGMWEEAGRIGAGIVGGDLVSCRQWVVSVTAIGDLDGRAPVLRSGAKAGSVLAVVGELGRSAAGYALWCNGIEDFAELRRRHLVPQPPYGHGAAAAAVGAQAMIDVSDGLLADLRHIAEASGVRIDLSAAALAADRDALTAAATALGTDPWPWVLSGGEDHALVACFVGPVPAGWRTIGRVLDGPARVLVDGEEWTGYAGWQSFGEPDNQGSLG | 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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
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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 diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
EC: 2.7.4.16
|
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 diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
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 diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
|
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
Subcellular Location: Cell inner membrane
EC: 7.6.2.15
|
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
Subcellular Location: Cell inner membrane
EC: 7.6.2.15
|
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
Subcellular Location: Cell inner membrane
EC: 7.6.2.15
|
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
Subcellular Location: Cell inner membrane
EC: 7.6.2.15
|
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
Subcellular Location: Cell inner membrane
EC: 7.6.2.15
|
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: Peripheral membrane protein
Sequence Mass (Da): 25571
Sequence Length: 235
Subcellular Location: Cell inner membrane
EC: 7.6.2.15
|
Q1JPJ8 | MKPPAACTGDALDVVAPCSAVNHLRWDLSAQQIAELTTELIEQTKRVYDCVGAQEPQDVSYENTLKALADVEVSYTVQRNILDFPQHVSPSKDIRTASTEADKKLSEFDVEMSMRQDVYQRIVWLQEKVQKDSLRPEASRYLERLIKLGRRNGLHLPEETQEKIKSIKKKLSLLCIDFNKNLNEDTTFLPFTREELGGLPEDFLNSLEKTEDEKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEENCAILRELVRLRAQKSRLLGFSTHADYVLEMNMAKTSQVVATFLDELAQKLKPLGEQERAVILELKRAECEQRGLAFDGRINAWDMRYYMNQVEETRYRVDQNLLKEYFPMQVVTRGLLGIYQELLGLSFQLEEGAAVWHEDVALYAVRDAASGKLIGKFYLDLYPREGKYGHAACFGLQPGCLRKDGSRQIAIAAMVANFTKPTPDAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFVEAPSQMLENWVWEAEPLLRMSQHYRTGSSIPQELLDKLIKSRQANTGLFNLRQIVLAKVDQALHTQTAADPAKEYARLCQEILGVPATPGTNMPATFGHLAGGYDAQYYGYLWSEVYSADMFHTRFKQEGVLSGKVGMDYRSCILRPGGSEDASVMLKLFLGRDPKQDAFLLSKGLQVEGCEPPAC | 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 of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By similarity).
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.
Sequence Mass (Da): 78139
Sequence Length: 687
Subcellular Location: Cytoplasm
EC: 3.4.24.15
|
P52888 | MKPPAACAGDMADAASPCSVVNDLRWDLSAQQIEERTRELIEQTKRVYDQVGTQEFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPSKDIRTASTEADKKLSEFDVEMSMREDVYQRIVWLQEKVQKDSLRPEAARYLERLIKLGRRNGLHLPRETQENIKRIKKKLSLLCIDFNKNLNEDTTFLPFTLQELGGLPEDFLNSLEKMEDGKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEENCAILKELVTLRAQKSRLLGFHTHADYVLEMNMAKTSQTVATFLDELAQKLKPLGEQERAVILELKRAECERRGLPFDGRIRAWDMRYYMNQVEETRYCVDQNLLKEYFPVQVVTHGLLGIYQELLGLAFHHEEGASAWHEDVRLYTARDAASGEVVGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQIAIAAMVANFTKPTADAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFVEAPSQMLENWVWEQEPLLRMSRHYRTGSAVPRELLEKLIESRQANTGLFNLRQIVLAKVDQALHTQTDADPAEEYARLCQEILGVPATPGTNMPATFGHLAGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLNSKVGMDYRSCILRPGGSEDASAMLRRFLGRDPKQDAFLLSKGLQVGGCEPEPQVC | 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 pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By similarity).
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.
Sequence Mass (Da): 78840
Sequence Length: 689
Subcellular Location: Cytoplasm
EC: 3.4.24.15
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A0QYB5 | MRLGTTAFAIASATALGLGLTACGAGDPAANSDTTRIGVTVYDMSSFITAGKEGMDAYAKDNNIELIWNSANLDVSTQASQVDSMINQGVDAIIVVPVQADSLAPQVASAKAKGIPLVPVNAALDSKDIAGNVQPDDVAAGAQEMQMMADRLGGKGNIVILQGPLGQSGELDRSKGIEQVLAKYPDIKVLAKDTANWKRDEAVNKMKNWISGFGPQIDGVVAQNDDMGLGALQALKESGRTGVPIVGIDGIEDGLNAVKSGDFIGTSLQNGTVELAAGLAVANRLAKGEPVNKEPVYIMPAITKDNVDVAIEHVVTERQQFLDGLTELINKNLETGDIAYEGIPGQKQP | 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
Subcellular Location: Cell membrane
|
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-[(E)-feruloyl]tyramine
Sequence Mass (Da): 25977
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.3.1.110
|
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