ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q3ZBF6 | MAATLLARACGLVRGAPWPWGWRRLHTVYQSVELPETHQMLRQTCRDFAEKELFPIAAQVDKEHRFPAAQVKKMGELGLMAMNVPEELSGAGLDYLAYSIAMEEISRGCASTGVIMSVNNSLYLGPILKFGTKEQKQQWVAPFTSGDKIGCFALSEPGNGSDAGAAATTARADGDSWVLSGTKAWITNAWEASAVVVFASTDRSLHNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDRRIPKDSLLGEPGLGFKIAMQTLDTGRIGIASQALGIAQAALDCAVTYAENRSAFGAPLTKLQAIQFKLADMALALESARLLTWRAAMLKDNKKPFTKEAAMAKLAASEAATAITHQAMQILGGMGYVKEMPAERHYRDARITEIYEGTSEIQRLVVAGHLLKSYRS | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains .
Catalytic Activity: a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 44552
Sequence Length: 412
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.1
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P16219 | MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains .
Catalytic Activity: a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 44297
Sequence Length: 412
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.1
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P79273 | MAAALLARACGPVRGALWPRDCRRLHTIFQSVELPETYQMLRQTCRDFAEKELVPIAAQVDKEHRFPEAQVKKMGELGLMAMDVPEELSGAGLDYLAYTIAMEEISRGCASTGVIMSVNNFLYLGPILKFGSKEQKQQWITPFTSGDKVGCFALSEPGNGSDAGAAATTAQADHDSWVLSGTKAWITNAWEASAAVVFASTDRSLQNKGISAFLVPMPTAGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMKTLDMGRIGIASKALGISQAALDCAVNYAENRRAFGVPLTKLQGIQFKLADMALALESARLLTWRAAMLKDNKKNPFIKEPAMAKLAASEAATAITHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLKSYRS | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains.
Catalytic Activity: a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 44851
Sequence Length: 413
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.1
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P15651 | MAAALLARAGGSLGRALRARDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYRS | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats . The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA . Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains .
Catalytic Activity: a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 44765
Sequence Length: 412
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.1
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P48818 | MRAARMAQSTGRQLLRLRGVSSWPGELLGQPRPGPARRPYASGVAQAAVDQSDSQPSEASTREKRANSVSKSFAVGTFKGQLTTDQVFPYPSVLNEDQTQFLKELVGPVTRFFEEVNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPVTDTATGAVKEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGNALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGIVHQELSRSGELAVQALEQFATVVEAKLIKHKKDIINEQFLLQRLADSAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDSWCIEAAARIRENMTALQSDPQQQELFRNFKSISKALVERGGVVTSNPLGF | Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains.
PTM: S-nitrosylation at Cys-237 in liver improves catalytic efficiency.
Location Topology: Peripheral membrane protein
Catalytic Activity: a very-long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 70649
Sequence Length: 655
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion inner membrane
EC: 1.3.8.9
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P49748 | MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRALEQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF | Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats . The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA . Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains .
PTM: S-nitrosylation at Cys-237 in liver improves catalytic efficiency.
Location Topology: Peripheral membrane protein
Catalytic Activity: a very-long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 70390
Sequence Length: 655
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion inner membrane
EC: 1.3.8.9
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P50544 | MQSARMTPSVGRQLLRLGARSSRSTTVLQGQPRPISAQRLYAREATQAVLDKPETLSSDASTREKPARAESKSFAVGMFKGQLTIDQVFPYPSVLSEEQAQFLKELVGPVARFFEEVNDPAKNDALEKVEDDTLQGLKELGAFGLQVPSELGGLGLSNTQYARLAEIVGMHDLGVSVTLGAHQSIGFKGILLYGTKAQREKYLPRVASGQALAAFCLTEPSSGSDVASIRSSAIPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPIKDAATGAVKEKITAFVVERSFGGVTHGLPEKKMGIKASNTSEVYFDGVKVPSENVLGEVGDGFKVAVNILNNGRFGMAATLAGTMKSLIAKAVDHATNRTQFGDKIHNFGVIQEKLARMAILQYVTESMAYMLSANMDQGFKDFQIEAAISKIFCSEAAWKVADECIQIMGGMGFMKEPGVERVLRDIRIFRIFEGANDILRLFVALQGCMDKGKELTGLGNALKNPFGNVGLLMGEAGKQLRRRTGIGSGLSLSGIVHPELSRSGELAVQALDQFATVVEAKLVKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGYPTAQHEKMLCDSWCIEAATRIRENMASLQSSPQHQELFRNFRSISKAMVENGGLVTGNPLGI | Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains.
PTM: S-nitrosylation at Cys-238 in liver improves catalytic efficiency.
Location Topology: Peripheral membrane protein
Catalytic Activity: a very-long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 70875
Sequence Length: 656
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion inner membrane
EC: 1.3.8.9
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A5PK26 | MTVKLDFEECLKDSPRFRASVELVEAEVSELETRLEKLLKLGNGLLESGRHYLAASRAFIVGICDLAHLGPPEPMMAECLDKFTQSLSHKLDSHAELLDATQHTLQRQIQTLVKEGLRSFREAGRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALKVARAGYRGRALDYALQINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSQLAQYRKELGGQLHQLVLNSAREKRDMEQRHVLLKQKELGGEEPEPSLKEGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKRYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSPSKSCLLQSDSERLMQLWVSAVQSSIATAFSQARLDDSPRGLGQGSGHLAISSAATLGPGGLTRGREPGGVGHVAAQVQSVDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVVINQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGPPRGHPPVPPKPGLIRPKPGSFRSKPEPPSEDLQSLHPGALLFRAAGHPPSLPTMADALAHGADVNWVNGGQENATPLIQATAAVRVLNSLLACEFLLQNGANVNQVDNQGRGPLHHATILGHTGLACLFLKRGADLGVRDSEGRDPLTIAVETANADIVTLLRLAKMREADAAQGQAGDETYLDIFRDFSLMASDDPEKLSRRSHDLHTL | Function: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration (By similarity).
PTM: Phosphorylation at Ser-555 by PKB is required for interaction with ITGB1, export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 82129
Sequence Length: 745
Domain: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate ACAP1-binding to PIP2 or PIP3 containing membranes. Only one PH domain of one ACAP1 dimer inserts into the membrane, while the other PH domain acts primaryly to interact with adjacent ACAP1 dimers (By similarity).
Subcellular Location: Recycling endosome membrane
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B8ID69 | MRSYLDFEKPVAELEAKLEELRALGARDGAVAISDDVSRLESKAAAALAELYATLTPWQKTQVARHPQRPHFVDYCAGLIEEFTPLAGDRSFGEDEAVVGGFGRFRGRPVCVIGQEKGATTEARIRHNFGMARPEGYRKAVRLMELAGRFGLPVLTFVDTAGAYPGIEAEERGQAEAIARSTEACLALGTPNVALVIGEGGSGGAIALATANRVLMLEHAIYSVISPEGAASILWRDAGRAQDAATAMKITAQDLLRLGVIDGIVPEPTGGAHREPEAAIRAAGDALAEALTGLADLDADALREQRAQKFLEIGRRL | Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 33727
Sequence Length: 317
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
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B5YIK7 | MTYYLDFEKPIQELEIKIEELKKLSDGSDIDLTQEIKRLNKKLKELKTEVFSNLTPWQKTQIARHPERPYTLDYISIIFEDFIELHGDRRFGDDPAVIAGIGKIDGDPYALVGHQKGRTIKERIYRNFGQAHPEGYRKALRVMKLAEKFSIPVITMIDTPGAFPGIGAEERGQAEAIANNLMEMSLLKIPLIGFVIGEGGSGGALALSVCDKIFMLEHAIYSVISPEGCAAILWKKNSDVGVEDYMRAAEELKLTAQDLKKFGIIDDIISEPLGGAHREPQEVGKRIKAKIVSVATELIKIPPDELIKKRYEKFRKIGNFWGSSNRRK | Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 36957
Sequence Length: 328
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
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Q3SL76 | MKTTFLDFEQPIAELEAKIEELRFVQDDSALDISEEIRRLQKKSQALTKDIYAKLNAWQVSQVARHPQRPYTLDYIQGLFTDFVELHGDRAYADDAAIVGGMARFNGEPVMVIGHQKGRDTKEKIFRNFGMPRPEGYRKALRLMRLAEKFRLPILTFIDTPGAYPGIGAEERGQSEAIARNLYVMAELQTPIVCTIVGEGGSGGALAIGVGDRTLILQYSTYSVISPEGCASILWKSADKASVAAETLGITADRLKANGLVDRIIEEPLGGAQRDWDAMFQSMRRALTDTLAELRKQPTEAMLGARYQRLRAYGSFKEAPAR | Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 35850
Sequence Length: 322
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
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Q73Q55 | MSNKDQTNLLNNLKDIAQKAGLDISEELAKINAKLESSTALSKTWERVELARHSDRPRTLDYINLIFDNFTELHGDRFFGDDPAMIGGIGFIDGMPVTVIGTQKGRNLRETIDRNGGMANPEGYRKAMRLAKQAEKFKRPIITFIDTQGAYPGLGAEERGIGEAIAFNLREFSRLKTPIICIIIGEGGSGGALGIGVGDKIYMLENAIFSVISPEGCASILLRDSSRAKDAAAMLKITSQEVLDLKVINGIIPEPEKGAHTDPKKTADAIKEQILKDLADLTKRDPAVLVKYRSKKIRSIGKYSE | Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 33417
Sequence Length: 305
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
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B9DY13 | MLNKFFKKTKYITVSQRALGDIHDDFTKKPSIPNGMWVKCDGCGKVLYKNDMEKNNKVCYHCGYHFRMNALERLELILDKESFYEFDKDITAANPIEFKGYEDKIKNMQNKTNIKEAVITGKGTIGREEAVVCIMDSNFMMGSMGSVVGEKITRAVEKSIELKLPLIIFTTSGGARMQEGIFSLMQMAKVSGAISRLNEEGLLYLSVLTDPTTGGVTASFAMIGDIILAEPGALIGFAGKRVIEQTIKQKLPEGFQKAEFLLQHGFIDNIVSRENLKETLRKILVIHGRGN | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 32521
Sequence Length: 291
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
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Q8XLG6 | MIKNLLNKRKYITVSSVELNDTELSEDEKPNIPSGMWSKCEKCAKILYTEDLRENFNVCPNCGHHFKLGAYERIKYLTDENTFVEFDKKMIGRNPLDFNGYEEKIKGYQKKSHVIEGVVTGEAYIAQRKVVLCVMDSNFMMGSMGTAVGEKITRAIEYATKNRLPLIIFTCSGGARMQEGIYSLMQMAKVSGAIYRHGRENLLYITVLTNPTTGGVTASFAMEGDIILSEPGCLVGFAGRRVIEGTINEKLPDDFQTAEFLLEKGFIDKIVQRKDLKQVITSLLRMHEVDYE | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 33017
Sequence Length: 292
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
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B1VKF0 | MCEENENKDSEYIETTPVENGYNSERFKHLWFLCENCETLIYKKSLLEQKGVCAECGATLQMTSSERIELLIDNGTWRSINTKLSSIDVLEKKHTTFDIKMVRKVSILLYKVISGKYFYKEFFKNKYYNKALRILVAYNNTLVNILKVALGSKFIKYLNLDSKETIKILQDIIDTGLKTAQFALFEIRKKIKNEFYRFALLNKAFENKQISSLLAQNLEDRRDDESEIISIEFDRMAFRVQTFLILESLLKLNTQLADVKEQLLSQDKFLKAVATSLVKKELYFPEDKRKTRKIKKIFPFYPGTDPETDYFLWLRTHMAISLMERYLVLKEFKYWFRNRYCGLLEEEFPRFGSDILIEYVKKQDRYESYNMIDHIMQDDLHTSTNSVELFQQINLLFHHKNNEKDCDNNFLSYTENTKGIYFCLLEIMKQFSTLTLDSKDKFPKKKGRDTKDTEDIEDIDEEDIEEEYPLTYDSLTKEEKEYVDANIELIKSTFNLGKEEFIETEEQSYQDYNTSYQKETGLPDAIQTGVGEINGISVALGVMDFQFMGGSMGSVVGEKITRLIQFATENFLPLILVCASGGARMQEGSFSLMQMNKIAAMLHTYQKEKNLLYISVLTSPTTGGVTASFGMLANVTIVEPNAYIAFAGKRVIEQTLNQIVDDEDQISDSLFDFGMFDSMVPRALLKNVLSETIEIYMYGD | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 81325
Sequence Length: 700
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Plastid
EC: 2.1.3.15
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Q2QD80 | MEKRWLNSMLSKGELEYRCRLSKSINSLGPIESEGSIINNMNKNIPSHSDSYNSSYSTVDDLVGIRNFVSDDTFLVRDSNSSSYSIYLDIENQIFEIDNDPSFVSELESSFYSFRNSTYQNNISKNDDSHYDRYMYDTKYSWNNHINSCIDSYLRTQICIDSYILSGSHNYSDSYIYSYICGEGGNSSESESFSIRTSTHGNNLTITESSNDLDNDRTTNYSDFWVICENCHKFNYKRLFKSKMNICEECGYHLKMNSSDRIELLIDPGTWEPMDEDMVSVDPIEWDSEVDPIQWKSQVDPIEGDSEVDLIEGDSEEYKDSSYKDRISSSQIETGLPEAIQTGTGKLNGIPVAIGVMEFEFMGGSMGSVVGEKITRLIDYASNQFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYKYQSNKKLFYVAILTSPTTGGVTASFAMLGDIIIAEPNAYIAFAGKRIIEETLKMEVPEGSQKTEPLFEKGLLDLIVPRNPLKDVVSELFQLHAFVPSNQNSIK | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 59002
Sequence Length: 523
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Plastid
EC: 2.1.3.15
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A7M907 | MQNWIDNSFQAEFEQESYFGSLGENSTNPSSGGDRYPEALIIRDITGKTSAIYFDITDDILENDPHQTILLSPIENDIWTEKDVIIDTYRYINELIFCDEKSQQKQKDRTEFIKKEQLQLISNRNPDHYRNLWNQCENCFIPNYKKVLKSNMQICEECGSYFKMTSSDRIDLLIDEGTWNPLDQDMVSLDSSEFDSEAELECYEDNIKEWNEEMCQAFMRKLSKDLKEGQALERTANLIEEPWLPEYIQPEEKVEEWTKPDLDEGEESQDEERWIWELDKGEESQEIEDSEANDEDDDDAPYVERLAFYKKETGLLDAVQTGVGQLNGRPVALGVMDFRFLAGSMGCVVGEKITRLIEYATNNLLPLIILSASGGARVHEGSLSLMQMAKISAALYDYQSNKRLFYISILTSPTTGGVTASFAMLGDIIITEPGTFVAFAGPRVVQQILNETIPEEEQEAEALFEKGFFDLIVPRHLLKNVISELLNLHAL | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 56198
Sequence Length: 491
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Plastid
EC: 2.1.3.15
|
P31562 | MERREGGRDNSSCSNVNQLFGVKDSESLLYDDVFIVRDRNGDSYFAYWDIEKNTFLSEPFYSYRSRNSSYLPKIKAFMSEDRSQIHEVKNGFRSEDHSKINKINGVENLFHNYNMNVLTDDYNFKMGMNGFHRPQSKIHINRFIDSYLQSQICIATTPGSGSDNDSYIHGSRVYGESESYTRSEGRSSSIRTRTKGVELTLRERPGILDRTKKYMYLWLQCDNCYGLNYKKVLKSKMTICEQCGYHLQMSSSDRIELLIDPGTWDPMDEDMVSRDPIKFDSGGGEAYKDRLYFYQRKTGLTEAVQTGIGQLNGIPVAIGVMDFKFMGGSMGSVVGEKITRLIEHATNKFLPLIIVSASGGARMQEGSLSLMQMAKISSALYDYQSNKRLVYVSILTSPTAGGVTASFGMLGDIIIVEPRAYVAFAGKRVIEQTLNQTIPNDSQEAEFLFHKGLFDLIIPRHLLKSVISELFTLHDLFPLNQNSNQYSQYRALLNPIF | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 56481
Sequence Length: 497
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Plastid
EC: 2.1.3.15
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Q9TLW3 | MPNGTKLAKSFLWKKCDSCNILISKFDFYKHDKVCPECNYHFPMYSSERINHIIDLKSWIPLYNNLLSGDPLGFCDKKPYITRLAENQKITGLDEAVQTGIGRINNISASVAVMDFNFMGGSMGSAVGEKITRLVEFSTKEELPIVIISASGGARMQEGILSLMQMAKISAALERLQSKGLLYISILSSPTTGGVFASFAMLGDIILAEPKAVVGFAGKRVVEQTLNEKLPPNFQSAEYLLDNGFVDLIVKRKQLKKTIHMILDLHN | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 29570
Sequence Length: 267
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Plastid
EC: 2.1.3.15
|
Q87YI2 | MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCDAVLYRPELEKTLDVCPKCNHHMRIGARARLNIFLDVDGREELGVDLEPVDRLKFRDGKKYKDRLTAAQKQTGEKDALISMSGTLLGMPVVASAFEFSFMGGSMGAIVGERFVRAANYALENRCPMICFAASGGARMQEALISLMQMAKTSAVLARLREEGLPFISVLTDPVYGGVSASLAMLGDVIVAEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLDHGAIDMIIARSELRPRLGNLLAQMMNLPTPRFVAPVIEPIIVPPAPATI | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 33534
Sequence Length: 306
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
A5WDG8 | MTKNNNDLSNSSSNPPSNRPVAGKEAELEIQRETHAAQSGQSESWLSRPIPTVKRNSLPQLTAVETEPSTECPQCHSMITNTALIFNAYVCPHCDHHLAMTARERLTGFLDHIEAELGQEFSASDPLKFVDSKPYPQRMEQMQTKTGETEALIVLQGKLRDMDVVACAFDFRFMGGSMGSVVGDRFVQAAEVALTNKAPLICFAASGGARMQEGVLSLMQMARTSAAIERLRLAGIPYIVVLTNPVYGGVTASLAMLGDIHIAEPKAMIGFAGKRVIEQTVRETLEEPFQRAEYLLEHGVIDQVVHRHQMNDTVYRLLAKLTHV | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 35677
Sequence Length: 324
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
Q9S7D9 | METRCSLLFLSLILLYLPKPGSGFGSSGPIAASFGGSAFFCAIDASGRQDVICWGKNYSSPSSPSSSSSSSSIASSTSASYNIPSMAVLSGGDGFLCGILSNTSQAFCFSSLGSSSGMDLVPLAYRTTAYSQIAAGNSHVCAVRGAYYSDHDSGTIDCWEITRATNNNSLIAKENPNFYDQIVSNLVFNNIVSGDGFSCGGIRDGGMLCFGPNSSNLGFNTTSDNFQVLAAGKNSVCAILNLSREVKCWGEDESFVNSPMNDSRFVSLTAGPRHFCGIREDNHEVECWGNSNFSLIPKGSGFKAIASSDFIVCGIREEDLVLDCWMVNGSSTLAYDPPLELCSPGMCRAGPCNEKEFAFNASILNEPDLTSLCVRKELMVCSPCGSDCSHGFFLSSSCTANSDRICTPCSLCQNSSCSDICKLHNSNFPDKHWHQLQRLVLIIGSCASALLIIIIGCCVVPRIVTSPNKEDGAANQFKSCIGKPDLDTDQPLENVSPAPSVTPFAQVFRLSELKDATNGFKEFNELGRGSYGFVYKAVLADGRQVAVKRANAATIIHTNTREFETELEILCNIRHCNIVNLLGYSTEMGERLLVYEYMPHGTLHDHLHSGFSPLSWSLRIKIAMQTAKGLEYLHNEAEPRIIHGDVKSSNVLLDSEWVARVADFGLVTSSNEKNLDIKRDVYDFGVVLLEILTGRKRYDRDCDPPEIVEWTVPVIREGKAAAIVDTYIALPRNVEPLLKLADVAELCVREDPNQQPTMSELANWLEHVARDALIF | Function: Serine/threonine-protein kinase with low activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 84185
Sequence Length: 775
Subcellular Location: Membrane
EC: 2.7.11.1
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O80963 | MQPNSHIFVIITISSLIITVSAYGSTGTIAAAFGENGFFCAIDASGKQEVICWDRGNTNRSLNRPPGEISGYSPPMTSLSGGEGFLCAITSNTSRAFCWNLEDPSENLVPRAFQYNSYLQIASGNNHVCAISGLYYSGPDYGPVHCWEYSDNTNFTSGLLWNSSFHNPYIDSLMFRKIVSGDGFSCGVTKDGDLVCWGPKSNLLNFSNNEEFEVLASGRNSVCGVSKDSGQLHCFGDETEFGSLPNRPRFIALSAGANHYCGIREDDHGVECWGRNLNSSSSSSAPNTSGFVAISSSDSTTCGVRELDLVLDCWRVHDSSKADYSPPLELCSPGMCSPRGNCGDGWFAFNASILKESELTSLCSFHNLNICLRCGISCLEGYFPSSTCNPNADRVCTPCSLCQNSSCYGICKIRATKSKEHEQKEQREVRRLVIIIGCSVLGFLVMLIGLSFIPKMTKGSKRDDEERSKMTCCFCFDKNSVEADPDPVPHQSVLLPTAVSLGETKIFRLSELKDATHGFKEFNELGRGSFGFVYKAVLSDGIHVAVKRANAATIIHSNNRGFESELEILCKIRHNNIVNLLGYCSEMGERLLVYEYMPHGTLHDHLHGDLSQLDWSMRLKIMLQAARGLDYLHNEVDPPIIHRDVKTSNILLDGEMCARIADFGLVSSNERDSSNSDREGDVYDFGIVLLEILSGRKAIDRESDPAGIAEWAVPLIRKGKAAAIIDRNICLPRNVEPLLKLAELAELAVRENSNERPNIRNILCFLDLIVKSGLTF | Function: Serine/threonine-protein kinase with low activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85303
Sequence Length: 776
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9LY50 | MKRFINSTVTFSVTVTIAVIIFFLLSPVTSLGSGSTYAVVYGSDTVCALISGQPTQRILCYDTRLNINVTLNPGVSFSSIAAGDNFLCGIRSGGYSLLCWDNIGSYSPNRKRIYQNDNVLLETLSVGDKQICATVNGTNSLKCWRGSVSDQSKPPNERFRSISSGVGFSCGVSIRNNRILCWGTDPVKSNQIQTGFGNTPMVTISAGKSHACGLNTTGNLICIGNNDSGQLNVIAPDQPNLYSSSLSLGSNFTCAMRISNNSVVCWGGGAERFNNVTDSISFESISSGPGLICGLISSNLSIMCWNPTNFSRIFLPFPEVLPGPCVESSSSSLCSCGVYPQSDKLCSGTGSICKSCPIQFPASPPSQFPLPPPPPPPPPSPSTSSPPSKALTRGLLAFAIVGSVGAFAGICSVVYCLWTGVCLGKKKVHNSVQPTITRGGSNSRSNSSNSRSLSIRRQGSRMLSMRRQRSGTSSMKHADKAEEFSFSELASATGNFSLENKIGSGSFGVVYRGKLNDGREVAIKRGEVNAKMKKFQEKETAFDSEIAFLSRLHHKHLVRLVGYCEEREEKLLVYDYMKNGALYDHLHDKNNVEKHSSLINSWKMRIKIALDAARGIEYLHNYAVPPIIHRDIKSSNILLDSNWVARVSDFGLSLMGPVLGKDHNPYQRPTKAAGTVGYIDPEYYSLNVLTDKSDVYGLGVVLLELLTGKRAIFRNNGDVEEEEGCVPVHLVDYSVPAITADELSTILDPRVGSPELGEGDAVELVAYTAMHCVNAEGRNRPTMTDIVGNLERALDLCGDSHGSISSGICSIVSD | Function: Serine/threonine-protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 87682
Sequence Length: 814
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9FIJ6 | MALTISISCFSSYFVSLLLLVLSSFSFVCFSLSTVSISHISNQTLVCALNNHSYLQCSSFPLNSIPFSLTGNLRNRRFSGVVSGNGFVCGLISRLDSNTSTLLCWRFSVDGTNMLHKRIYHGPELEELEAGNFRICGVERVSRRLRCWQPYYLPRPDNYRSIALGDNFFCGLSQPPGMISCEGIAKVPSGDHYIAIAAGSRQACAITVDNDVECWGQTQSLPREKFLALAVGEDRGCGVRWSNGTVVCWGNNNNFSLPQTLKDIHFTSIYAKGPMFCGVATRNYTLICWGNENFKSGVFTPFQGLISQVVMPGPCRRECPYRPLSGSQSLCGNELMICDLKRNDGEFPDTRAQNSKNKTWSRRNIAFLVVGCVGTFSLLLVISFLIFKSHCRCRVHDSGRLDDTRTIDIPKLEKRLCTLASLGNPGQLMEFSIDELALATDGFSVRFHLGIGSFGSVYQGVLSDGRHVAIKRAELTNPTLSGTTMRHRRADKDSAFVNELESMSRLNHKNLVRLLGFYEDTEERILVYEYMKNGSLADHLHNPQFDPLSWQTRLMIALDAARGIQYLHEFIVPPVIHRDIKSSNILLDATWTAKVSDFGLSQMGPTEEDDVSHLSLHAAGTLGYIDPEYYKFQQLTTKSDVYSFGVVLLELLSGHKAIHNNEDENPRNLVEYVVPYILLDEAHRILDQRIPPPTPYEIEAVAHVGYLAAECLMPCSRKRPSMVEVVSKLESALAACLTAPKTETVSRSNTY | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 83774
Sequence Length: 751
Subcellular Location: Membrane
EC: 2.7.11.1
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Q8S4Y1 | MAHTSESVNPRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL | Function: Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA . Generates the bulk of the acetoacetyl-CoA precursor required for the cytosol-localized, mevalonate-derived isoprenoid biosynthesis . The generated isoprenoids are required for normal growth and development . Essential protein during embryogenesis .
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 41412
Sequence Length: 403
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
|
Q709F0 | MKPGATGESDLAEVLPQHKFDSKSLEAYLNQHLSGFGAEREATLTIAQYRAGKSNPTFYLQKGFQTYVLRKKPPGSLLPKAHQIDREFKVQKALFSIGFPVPKPILYCSDTSVIGTEFYVMEHVQGRIFRDLTIPGLSPAERSAIYVATVETLAQLHSLNIQSLQLEGYGIGAGYCKRQVSTWTKQYQAAAHQDIPAMQQLSEWLMKNLPDNDNEENLIHGDFRLDNIVFHPKECRVIAVLDWELSTIGHPLSDLAHFSLFYFWPRTVPMINQGSYSENSGIPSMEELISIYCRCRGINSILPNWNFFLALSYFKMAGIAQGVYSRYLLGNNSSEDSFLFANIVQPLAETGLQLSKRTFSTVLPQIDTTGQLFVQTRKGQEVLIKVKHFMKQHILPAEKEVTEFYVQNENSVDKWGKPLVIDKLKEMAKVEGLWNLFLPAVSGLSHVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDVASSDATNIECSIQRDEDSYVINGKKWWSSGAGNPKCKIAIVLGRTQNTSLSRHKQHSMILVPMNTPGVKIIRPLSVFGYTDNFHGGHFEIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGAKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELRDQAKRLTAKI | Function: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA . Probably participates in beta-oxydation and energy production but could also play a role in the metabolism of specific fatty acids to control fatty acids composition of cellular lipids in brain (Probable).
Catalytic Activity: a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 87264
Sequence Length: 780
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Peroxisome
EC: 1.3.8.-
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B3DMA2 | MEMDVTRDTVEVLPQHKFDIRSLEAYLNQHLPGFGSDHRAVLTVTQYRSGQSNPTFFLQKGSQAYVLRKKPPGSLLPKAHKIDREFKVQKALFSVGFPVPKPLLYCSNASIIGTEFYVMEHVQGRIFRDFSIPGVSPAERAAIYVSLVETLAWLHSLDIHSLGLDRYGTGVGYCKRQVSTWTKQYQASAHQSIPAMDQLSTWLMRNLPDSDNEECLVHGDFKLDNIVFHPKECRVIAVLDWELSTFGHPLSDLAHLSLFYFWPRTLPMINRGSHIQENTGIPLMEELISIYCRRRGIDPNLPNWNFFMALSFFKLAGIAQGVYSRYLMGNNSSEDSFLTANTVQPLAETGLQLSRRTLSTVPPQADAKSRLFAQSRRGQEVLTRVKQFMKQHVFPAEKEVAEYYAQNGNSAEKWEHPLVIEKLKEMAKAEGLWNLFLPAVSGLSQVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEQQKQQWLEPLLRGDITSVFCMTEPNVSSSDATNMECSIQRDGGSYIVHGKKWWSSGAGNPKCKIAVVLGRTESPSVSRHKVHSMILVPMDTPGVELIRPLSVFGYMDNVHGGHWEVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRSVGLAERILQIMCDRAVQREAFGKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTLGSAAARKEIAMIKVAAPKAVCKIADRAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAKMELQDQARQLKARM | Function: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. Probably participates in beta-oxydation and energy production but could also play a role in the metabolism of specific fatty acids to control fatty acids composition of cellular lipids in brain.
Catalytic Activity: a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 87371
Sequence Length: 779
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Peroxisome
EC: 1.3.8.-
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O29057 | MERLFYPKVVAVIGASPQEGKVGNTIMKNLRNFSGTVYAVNPKYREILGFPCYPSVLKIPENVDLAIIVVPAKLVPKAVEECGRKDVEGAVVISAGFKEAGIEGAKLERELVEVAERYGVKLVGPNCLGMINTEIAMNATFSRVAPEKGRIAFLSQSGAFILAVLEWSKRNGVGFSKVVSLGNKAMLDESDFLEYLAKDDSTDVILIYMEGVEDGRKFMRVAKSVARRKPVVVMKAGKSQSGAKAASSHTGSLAGSYEAYRAAFRQSGVIEASSVEELFDFALLLLKYRKAGNLAILTNSGGPGVMAADACDQFGVPLANFNFETIRKLKEFLPAESNFYNPVDILGDASAERFSRSLQILSEDENVDIVLTILTPTAQMDFLKAAESVVGKNAVCCFMGGESVDESERILRSSGIPNFFDPVRAVRAISVLGRYSKISAKERVKEDLDVSVEREKAEEIIEKLLESGGRVVGAEGLPVLEAYGIEVAPYGIARNVDEARDIAESIGYPVVLKVVSPDVVHKSDVGGVKLNVGENDLEKAFFEILSNVEGRMPKARIEGVLVQKMVDGGKELIVGMKRDPQFGPMIMFGMGGVYVEVLKDVSFRIAPITRREAHEMVREVKAYRILRGLRGEKPADIDAIADLLLRVSKLSLDHPEVLEMDLNPVKVFESGYAVVDFRMVLGEEV | Function: Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + ADP + phosphate
Sequence Mass (Da): 74698
Sequence Length: 685
EC: 6.2.1.13
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Q6BZP5 | MLRTRFINSVNSARAMSRNINTLSQFPYPTLQQEESFFKSQVEDIEKWWASPRYEGIKRPYTAEKVAIHRGTLPQTYASSVQAEKLFNIFTERGKQGLPVHTTGSVDPVQMTQSAPHQEVVYISGWACSSLLTTTNEVSPDFGDYPYDTVPNQVDRIFRAQGLHDKKAWHEWMSLSHEERVKRDQEGKGRIDYLRPIIADADTGHGGLSAVMKLAKLFAERGAAAIHLEDQLHGGKKCGHLAGKVIVPTGSHISRLNATRMQWDIMGCSNLVIARTDSESAKLLSSAADPSDHEYILGVVKPIKPLAEVLLTAEANGATADMVNKLELEWTKEAEMMTYDEAVQRALTEAGKSDKIEEYLTKAKGKSNFEARQIADELAGKHIFFDWDAPKTREGHYHVQCGIEPAIKRALAFAPYADLIWLETKTPDLAQAQAFAKRIREKFPGKWLVYNLSPSFNWSAHGYSDEQLKSFVWDLAKSGFVMQLISLAGLHSNAVATHELSTRFKTEGMKAYVDLVQRKEKELGCDVLTHQKWSGANYLDSIISTVQSGSSGTSSTGGDSTENQF | Function: Component of the methylcitrate cycle that catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA.
Catalytic Activity: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Sequence Mass (Da): 63005
Sequence Length: 565
Pathway: Organic acid metabolism; propanoate degradation.
Subcellular Location: Mitochondrion matrix
EC: 4.1.3.30
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Q12031 | MITMINNKTFNRKTTGTLKKLVLSSDKSLRRSFNGASSTKDFVFSESSKVEEWWESARFKNISRPYSATDVVKHRGSLPANTSIYPSSYQARKLFNLLEENFKNGTPLHTLGVIDPVQMSQLARCRNIKVAYISGWACSSTLVGSTNEVSPDFGDYPYDTVPNQVERIFKAQQLHDRKAFLEASIKGSTPVDYLKPIIADADMGHGGPTTVMKVAKLFAEKGAAGIHLEDQMVGGKRCGHLSGAVLVPTATHLMRLISTRFQWDIMGTENLVIARTDSCNGKLLSSSSDPRDHEFIRGIIRDNVVPWSEKLIEMEDKKIPNSAIADMEKEWYHENELFTFEEALEKQFTASEFESYKEKKEDLMVNKLGRAYLSLREMKLLAQEVTPLKKIIFDWDAPRTKEGYYMFNGCIEAAIRRSLVFAPYSDMIWLETKTPDLEQARSFSRKIHKQLPATKLVYNLSPSFNWSAHGFDDKALKSFVWDLAKEGFTLQLVSLAGLHSDGVSFWELANSFQSDGMKAYVEKVQKREKETNCDIMTHQLWSGAEYVDSLMKVVQNGASSQTLSTSGESFTETQF | Function: Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate.
Catalytic Activity: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Sequence Mass (Da): 64976
Sequence Length: 575
Pathway: Organic acid metabolism; propanoate degradation.
Subcellular Location: Mitochondrion matrix
EC: 4.1.3.30
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Q3IKY9 | MPDTITNKLQNSTVQDVIATKLARAVFAGFEAMFATFLNITLGAQSRFEQRQYHEVQSAMRERLQVYERQVKSVSEAVKVIAYAELSCPQTWQLAKNIYGNMVKNHENEPIAHTFFNSTFGAIWDDKKIRTVHLFVLKAKYRTQPRPYDSLVKRISLQHGFNSAIKTLITNQVFRVPFSNLNQDVATLQATLTQGAKQQCRQVYELINLNDGYIEYAYSHFYRNKACYLIGRCIAKNGDNMPFAIAILNTPKGLKIDAVMMGADQLSLLFGFARTYFMVDTDQPARYVDYLSVLMPHKQRFELFNAIGFIKHAKTEFYRYKVDTTKNSPASFKYVAAPGTPGMVMLVFTIAGSDHVYKVIKDKFSAPKTATKAQVKEKYNFVKQADRVGRLVDTHEFRYLAFDLSRFSEQLLQQMKEHIGSSLIISGKALILKHVYVERKMTPLNLYINDCDSKALAQVMLDYGRAIKDLAGANIFPGDMLMKNFGVTRWGRVVFYDYDEICPLTDCNFREVPQTQNALEELSSDSYFDIEPNDIFPSQFKVFFSANELAFNAFNSHHSDLFNAQFWQTCQQQVQQGYLPDVYPYKQSWRFK | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
Catalytic Activity: ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase]
Sequence Mass (Da): 68071
Sequence Length: 592
Subcellular Location: Cytoplasm
EC: 2.7.11.5
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Q3IHD9 | MQPRHIAELILTGFKKHYLLFQKTTAKAPLAFAKRDWQAINDISRLRISHYDDRVNETTATLRQQQTEQLDEQLWLEVKKLYQHFLCFHPQAELAETFYNSVFCRLYHRRYFHNDFIFVEATLKDAPAVPVEAEYRSYFPVVDGLKPTIKQIINHFDFKAPFVNLERDIRLLVKAFYKQAPDTHHKAWQMRFDILHTPFYRNKAAYIVGRVVSQSGVQPFIIAVLHHEDKGLYLDALLTKSSQMRVIFGFARAYFMVETHAPCALVRFLNQLMPNKTIAELYNAIGFHKQGKTEFYREFLNHLTHSNDEFTIAPGTPGMVMMVFTLPSFGYVFKVIKDKFGESKPFGRDTVLKRYQLVKKHDRVGRMADTIEYSNVVFPLARFDSNLLQQLHQTIGSSMVIEGDWLIIKHLYIERRMTPLNLFLENADDASAADAIEEYGQALKEMIAVNIFPGDMLLKNFGVSKHKRIIFYDYDEVQYLTDMNFRALPKAKTYDDYLMDEQSYSVAPQDVFPEQLCTFVMPNPIYKQFLMSTHPELIDVNFWKQAQQNIKNGQVSHIYPYPTAQRFIHHW | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
Catalytic Activity: ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase]
Sequence Mass (Da): 66954
Sequence Length: 571
Subcellular Location: Cytoplasm
EC: 2.7.11.5
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Q2IJI0 | MLDERGALARGAAEAIRAGYEAYQAERARITARARGRFEARDWAGAQRDARERLDLRDGVVHRTVGEVRAELGGAVQDREVWRRAKEAFEAVAAARPDAEIAGSFFNSVTRRVLTTVGVDPAIEFLAADAPPPREDPPQHRAFAREATTEALLARILRAAPISAPFEDLARDARLAALELDAHVRGLPDRQPIDAVELARPVFYRGKGAYLVGRIRRGRHLTPLVLALAHGDRGVALDAVLFTEEDVSIVFGFTRSYFHVALERPRAMVAFLSTLLPLKRRSELYTGLGYHKHGKAELYREVAQHLAEGDDRFVPARGDRGLVMCVFTLPGLDVIFKVIRDRFAPPKQTTRREVMDRYRHVFRHDRAGRLVDAQEYEHLAFPAARFSPALLEELRTECGDGVRVAGGEVAIRHLYAERRVTPLNLFVREADEWTARQAVLDFGCALRDLAATDTFPGDLLLKNFGVTRHGRVIFYDYDELTRVTDCNFRDLPGAGPGDGDDGWGGGPDAGYDGGDPPFYVGPADVFPEELLPFLGLTGRLREVFLRAHGELLTGRWWRDIQARLRAGEIVDIFPYREEQRLRHAHP | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
Catalytic Activity: ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase]
Sequence Mass (Da): 65597
Sequence Length: 586
Subcellular Location: Cytoplasm
EC: 2.7.11.5
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Q7WDP2 | MIYSGDVQRIEPAPVAGPAPLDVAHLILAGFDRHYALFRYSAQRAKSLFESGDWHGMQRLSRERIEYYDMRVRECATQLDSALRGSDARTADGSRANGSAALSEAQTAFWQAVKQEFVGLLADHRQPECAETFFNSVSCRILHRDYFHNDFLFVRPAIATDYLDSRIPSYRVYYPVAEGLHKSLIRMVADFGLAVPYADLPRDARLLARAAVRQLRGQLPRHAGPRLASDCQIQVLGSLFFRNTGAYIVGRLINQGTVYPFAVALRRNPAGQVCLDALLLGADDLSTLFSFTRAYFLVDMETPAAVVNFLASLLPRKPKAELYTMLGLQKQGKTLFYRDFLHHLTHSRDAFDIAPGIRGMVMCVFTLPSYPYVFKLIKDRIDKDGMDHATVRRKYQMVKLHDRVGRMADTWEYSQVALPRSRFAPRLLEELRRLVPSLIEENGDTVVIRHVYIERRMMPLNLYLRHASDPLLEVAVREYGDAIRQLATANIFPGDMLYKNFGVTRLGRVVFYDYDEIQRMTEMNFRAIPPAPNEEAELSSEPWYAVGPNDVFPEEFGRFLLGDPRVRQAFLRHHADLLAPQWWQACRARVAQGRIEEFFPYDTDRRLHPQAAPPPRTAA | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
Catalytic Activity: ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase]
Sequence Mass (Da): 70681
Sequence Length: 619
Subcellular Location: Cytoplasm
EC: 2.7.11.5
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Q0BBE2 | MNHFPKLLSSQIGFDVAQTMLENFDRHYRIFREAAVDAKTLYERADWHGLQRLARERITSYDDRVQECVEVLQDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAATLERIVTNFQLEPPFEDLTRDIGCVMQAITDEFGEFDAAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGLLALDTLLLRRDLLQIIFSFSHSYFLVDMGVPSAYVEFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTREQIMEKYQLVKRHDRLGRMADTLEYSSVALPISRLDHALVRELEKEVPSLLEYEDGNLVIKHLYIERRMIPLNLYLQNGTDAEIEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRAVFMKHHADFFEASLWQASKDKLLQGELPDFFPYDVSLRFSVRYPDRFDATPDAGDGDSAGNAQRAA | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
Catalytic Activity: ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase]
Sequence Mass (Da): 70231
Sequence Length: 608
Subcellular Location: Cytoplasm
EC: 2.7.11.5
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Q86GC8 | MEIRGLITRLLGPCHLRHLILCSLGLYSILVQSVHCRHHDIGSSVAHQLGSKYSQSSSLSSSSQSSSSLAEEATLNKDSDAFFTPYIGHGDSVRIVDAELGTLEREHIHSTTTRRRGLTRRESSSDATDSDPLVITTDKGKIRGTTLEAPSGKKVDAWMGIPYAQPPLGPLRFRHPRPAERWTGVLNATKPPNSCVQIVDTVFGDFPGATMWNPNTPLSEDCLYINVVVPRPRPKNAAVMLWIFGGGFYSGTATLDVYDHRTLASEENVIVVSLQYRVASLGFLFLGTPEAPGNAGLFDQNLALRWVRDNIHRFGGDPSRVTLFGESAGAVSVSLHLLSALSRDLFQRAILQSGSPTAPWALVSREEATLRALRLAEAVNCPHDATKLSDAVECLRTKDPNELVDNEWGTLGICEFPFVPVVDGAFLDETPQRSLASGRFKKTDILTGSNTEEGYYFIIYYLTELLRKEEGVTVTREEFLQAVRELNPYVNGAARQAIVFEYTDWIEPDNPNSNRDALDKMVGDYHFTCNVNEFAQRYAEEGNNVFMYLYTHRSKGNPWPRWTGVMHGDEINYVFGEPLNSALGYQDDEKDFSRKIMRYWSNFAKTGNPNPSTPSVDLPEWPKHTAHGRHYLELGLNTTFVGRGPRLRQCAFWKKYLPQLVAATSNLQVTPAPSVPCESSSTSYRSTLLLIVTLLLVTRFKI | Function: Rapidly hydrolyzes choline released into the synapse.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 78179
Sequence Length: 702
Subcellular Location: Synapse
EC: 3.1.1.7
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P07140 | MAISCRQSRVLPMSLPLPLTIPLPLVLVLSLHLSGVCGVIDRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEPWHGVLDATGLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPAKARLRHGRGANGGEHPNGKQADTDHLIHNGNPQNTTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFGFLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFGESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEIGKALINDCNCNASMLKTNPAHVMSCMRSVDAKTISVQQWNSYSGILSFPSAPTIDGAFLPADPMTLMKTADLKDYDILMGNVRDEGTYFLLYDFIDYFDKDDATALPRDKYLEIMNNIFGKATQAEREAIIFQYTSWEGNPGYQNQQQIGRAVGDHFFTCPTNEYAQALAERGASVHYYYFTHRTSTSLWGEWMGVLHGDEIEYFFGQPLNNSLQYRPVERELGKRMLSAVIEFAKTGNPAQDGEEWPNFSKEDPVYYIFSTDDKIEKLARGPLAARCSFWNDYLPKVRSWAGTCDGDSGSASISPRLQLLGIAALIYICAALRTKRVF | Function: Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.
PTM: Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell.
Location Topology: Lipid-anchor
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Sequence Mass (Da): 71785
Sequence Length: 649
Subcellular Location: Synapse
EC: 3.1.1.7
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P22303 | MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL | Function: Hydrolyzes rapidly the acetylcholine neurotransmitter released into the synaptic cleft allowing to terminate the signal transduction at the neuromuscular junction. Role in neuronal apoptosis.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67796
Sequence Length: 614
Subcellular Location: Synapse
EC: 3.1.1.7
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Q27677 | MGQLSILCLFVTVCASVCGYSWPSDETTTKPSQFKDFHTDPLVVETTSGLVRGYSKTVLGREVHVFTGIPFAKPPIEQLRFKKPVPIDPWHGILDATKQPNSCFQERYEYFPGFEGEEMWNPNTNISEDCLYLNIWVPQRLRIRHHADKPTIDRPKVPVLIWIYGGGYMSGTATLDVYDADIIAATSDVIVASMQYRLGSFGFLYLNRYFPRGSDETPGNMGLWDQILAIRWIKDNAAAFGGDPDLITLFGESAGGGSISIHLISPVTKGLVRRGIMQSGTMNAPWSYMSGERAEQIGKILIQDCGCNVSLLENSPRKVMDCMRAVDAKTISLQQWNSYSGILGFPSTPTIEGVLLPKHPMDMLAEGDYEDMEILLGSNHDEGTYFLLYDFIDFFEKDGPSFLQREKYHDIIDTIFKNMSRLERDAIVFQYTNWEHVHDGYLNQKMIGDVVGDYFFVCPTNNFAEVAADRGMKVFYYYFTHRTSTSLWGEWMGVIHGDEVEYVFGHPLNMSLQFNSRERELSLKIMQAFARFATTGKPVTDDVNWPLYTKDQPQYFIFNADKNGIGKGPRATACAFWNDFLPKLRDNSGSEEAPCVNTYLSKIRSSSNELLPPSTSLVLIWIMTLLNAL | Function: Rapidly hydrolyzes choline released into the synapse.
PTM: The N-terminus is blocked.
Location Topology: Lipid-anchor
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Sequence Mass (Da): 71142
Sequence Length: 629
Subcellular Location: Synapse
EC: 3.1.1.7
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Q92081 | VPSPRPQNATVMVWIFGGGFAYGTSSLNVYDGRYLAQAEGAIVVSMNYRVGALGFLSLPGSPVPGNAGLFDQQLALRWVHGNIHRFGGNPQSVTLFGESAGSASVAPHLLSRHSQQFFQRAILQSGTLNAPWATVEDTEARRRAEALAQALGCPTDDDNELLNCLYARPPQEIVSKEGDVVIEPSIFRFPFVPVVDGHFIIDSPIVLLQQGIFKKTDLLLGVNRNEGSFFLIYGAPGFSKDHESLISREDFLENIPMIVPQGNEVSVDAIVLQYTDWLAQNDALKNRDAIEDIVGDYNVICPVVEMATRYAEFGNNVYFYFFNQRASNLPWPQWMGVI | Function: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37300
Sequence Length: 338
Subcellular Location: Synapse
EC: 3.1.1.7
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Q7LZG1 | SELKVATQTGFVRGLSLPVLAGHVSAHLGVPFAEPFLRPEPVKPGAEMWNPNLNIWVPSGRVGAFXFLTVTLFGESAGAASVGMXLLSTQRAILQSGAPNAPWAQVQPAESRFPFVPVIDGEFFPLGVNKDEGSFGVPGFSKXXESLINQAVPHANDIYTDWQDQDNGGLPLTGNPTXPHN | Function: In venom, its toxic role is unclear: it could result in less musculatory control by rapidly hydrolyzing acetylcholine, or that it works synergistically with alkaline phosphatase (ALP) in paralyzing prey through hypotension. In muscle, it terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. In liver, its function is unclear: it could serve as a safeguard against any diffusion of acetylcholine from synapses into the circulation.
PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Sequence Mass (Da): 19255
Sequence Length: 181
Subcellular Location: Synapse
EC: 3.1.1.7
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P04058 | MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF | Function: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
PTM: An interchain disulfide bond is present in what becomes position 593 of the T isoform.
Location Topology: Lipid-anchor
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Sequence Mass (Da): 65906
Sequence Length: 586
Subcellular Location: Cell membrane
EC: 3.1.1.7
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W4VSJ0 | MMLPRCFVTVLLMSSVLYIGGETSSEVLGPVVSTEAGSFQGMELTTHGERVIYAFLGIPYAKPPTGLLRFKKPQPADFIQGTYKATEKPPSCFQLDSDLQLPWADPDSPMKEDCLFLNLWTPASLSTEEEELKSVMVWIHGGGYTSGSSALDVYDGQTLSSSGDVVVVTMNYRLDAFGFLNSLTEDAPGNMALYDQLLALQWVHTNIKYFGGDPNKVTLFGESVGAFATSFLALSPLTKGLFQKIMLESGSAYNKLTVNSIDQAKNNNQLATLVGCANETFTLISNPEEVVACMREVAPAKFTQTYYKELGSEREKINFIFWPHFGDDILPTRTAELIKEKNLTALFAGVNSVEGSALSVFFFPEVYQMFVESNLTLTKAYATILMNEFFKVFNFQDSAKAIEFYLGDVEDDDEEGIRSALFGVVGDYIITCPTIYLADKYSERGANVQFYRFDRRPSTSQWPPEWMGAAHNDEIQFVFGMPVRYPEKYTEEERTLSEYMTRTWTNFVKSEDLKLKNGSQWPSYSLSEPQFATLQTNEQIIGSGQRKAECDFWRPYFDI | Function: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Sequence Mass (Da): 62782
Sequence Length: 559
Subcellular Location: Secreted
EC: 3.1.1.7
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Q6I681 | MGLGLGVRAAPFTYAAHALAVAAAAMVLVWSIQFRGGLAIESTNKNLIFNVHPVLMLIGYVIIGGEAIMVYRVLPTSNHDTTKLIHLILHGIALVLGAVGIYFAFKNHNESGIANLYSLHSWIGIGTITLYGIQWIIGFVTFFFPGAAPNVKKGVLPWHVLFGLFVYILALANAELGFLEKLTFLESSGLDKYGTEAFLVNFTALVVVLFGASVVVAAIAPVRLEEPQGYDPIPEN | Cofactor: Binds 2 heme b groups non-covalently.
Function: Two-heme-containing cytochrome. Catalyzes ascorbate-dependent trans-membrane electron transfer by utilizing a concerted H(+)/e(-) transfer mechanism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25425
Sequence Length: 236
Subcellular Location: Membrane
EC: 1.-.-.-
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Q5DZD2 | MNNEYVLVINSGSSSLKFAVIDSVSGDAVLSGLGECFGLEDARMSWKYQGQKTEIAIEGNENHHKIAIGKLVGLTEELGFTDGIVAIGHRIVHGGEKFTKTVRINEEVTKEIESLSDLAPLHNPAGAIGIRAAVEAFPSLPQFAVFDTAFHQTMPKRAYTGAIAKELYTDFGVRRYGFHGTSHYFVSREAAKMINKPIEESNFISVHLGNGASVCAIKDGNSVDTSMGFTPLSGLMMGTRCGDLDPGIIEYLLKKGWSQEQVFNSLNKESGFLGVSGLTSDARGILEAMEEGHEGATLAFQVFTYRVAKYVASYLAALDSLDGIIFTGGIGENSLPIRREILSNLKILGFVEDVAGNEGARFGADGIIAKSEMLNAVAMVIPTNEEFVIAQQSVELL | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 42742
Sequence Length: 397
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q9CE36 | MEKTLAVNAGSSSLKWQLYEMPEETVIAKGIFERIGLSGSISTTKFNNEEHFRKQEIVDHRQAVLLLMDELIHFKLIHEFREITGIGHRVVAGGEFFKTSTVISPEVLAEIKNLSTLAPLHNPANVLGIEAFQRLLPDALAVAVFDTAFHSTLPEKAYRYPIPTKYYEDYSIRKYGAHGTSHMYVAQEAEKVLGKPLEDLKLITAHIGNGASITAIEAGKSVDTSMGFTPLAGVMMGTRAGEMDASVIPYMLESDPSLRNAQDVIDILNKDSGVLGVSELSSDMRDLSEAVAKGNPKAILAYEMYVDRLKKFIAQYFGVLNGADALIFTAGVGENDTAVRTDVVNGLSWFGMEIDESKNVRGAFGIISKPESKVKVLVVPTNEELVIARDVEAAK | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 43225
Sequence Length: 395
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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A5FE24 | MKILIINSGSSSIKYQLMVMPANEVICSGMIDRIGLETSNITFKTVSNSFEEILPVPTHKVGLQKVADMLLDAETGVIKTTSEITAVGHRVVHGGSYFSNTTVITEEVKEKIKELSELAPLHNPAHLVGINVAEEIFASAKQVAVFDTAFHQTIPVEAHKYAIPNFLLTEHKVRVYGFHGTSHKYVSEKAINYLEKGSKIITIHLGNGCSMTAVKDGKSIDTTMGFSPANGLVMGTRAGDIDQSVIFYMVKSLGYTPDEVNSILLKQSGMLGLTGYSDLRDIESKASEGNKDCQLALLMNAYRIRKTIGSYAAALNGLDAIVFTAGIGENSSFMRNLICTDMDYFGIEIDKEKNQIRSKELREINTPNSIVKILVVPTDEEFEIANQVYQLLEN | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 43237
Sequence Length: 394
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q0BPA5 | MSEILVLNCGSSSVKFALINPHTSQSLVTGLAENIATKNCKVVFKAEHKIEKYLENGSYKDVFEMLKDFLVENKHLEKIVAIGHRVVHGGQYFSKSVLINADSLEKIKACIALAPLHNPAHIEGIRFCQQIFPELPQVAVFDTAFHQTVPSYIAEYAIPYELTHKHNIRKYGAHGTSHKYVSEQAAKILTQQKANVIVAHLGNGCSITAVVDGKSIDTSMGLTPLDGLVMGTRSGCIDPSIFAYIISDNLGWSVTEITNMLNKQSGLLGICGHNDMREVSQLAAKGDSLAKLAIEIFSHRVAKFVASYMIYFNKLDALVFTGGIGENAANIRKNIISKLANLGFMIDHQKNSNSETFINSKNSHNIMVIATNEELMIAQETQNLI | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 42303
Sequence Length: 385
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q8RED7 | MKILVINCGSSSLKYQLINPETEEVFAKGLCERIGIDGSKLEYEVVAKDFEKKLETPMPSHKEALELVISHLTDKEIGVIASVDEVDAIGHRVVHGGEEFAQSVLINDAVLKAIEANNDLAPLHNPANLMGIRTCMELMPGKKNVAVFDTAFHQTMKPEAFMYPLPYEDYKELKVRKYGFHGTSHLYVSGIMREIMGNPEHSKIIVCHLGNGASITAVKDGKSVDTSMGLTPLQGLMMGTRCGDIDPAAVLFVKNKRGLTDAQMDDRMNKKSGILGLFGKSSDCRDLENAVVEGDERAILAESVSMHRLRSYIGAYAAIMGGVDAICFTGGIGENSSMTREKALEGLEFLGVELDKEINSVRKKGNVKLSKDSSKVLIYKIPTNEELVIARDTFRLAK | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 43625
Sequence Length: 398
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q7NLW9 | MKVLVLNAGSSSQKSCLYDLPHTQLPQEPPQPLWEAQIDWPHGGDGAKLKIKTVHHRHEKTLQGGSRSEDSARMLETLYSGETRVIADPSEIEMVGHRVVHGGEAYRESTRITPEVKAAIDQLARFAPVHNPANLAGIEALEALLGPQVPQIAVFDTAFHSRLPAAAYVYPGPYEWLDQGIRRYGFHGISHRYCAERAAQILGRDLAQLRLITCHLGNGCSLAAVQGGFSIDTTMGFTPLEGLMMGSRSGSVDPGILIHLMRQADYTVDKLDHILNQASGLEGVSGISNDLRPLFKAIDEGNARAKLALDIYIHRLRAGIGAMAVSLGGLDALIFTAGVGENAAPVRAGACEALGFLGVALDPQKNNGRPRDADIAAADSAVRVLVIHTQEDWAIARECWQHLRR | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 43835
Sequence Length: 405
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q16570 | MGNCLHRAELSPSTENSSQLDFEDVWNSSYGVNDSFPDGDYGANLEAAAPCHSCNLLDDSALPFFILTSVLGILASSTVLFMLFRPLFRWQLCPGWPVLAQLAVGSALFSIVVPVLAPGLGSTRSSALCSLGYCVWYGSAFAQALLLGCHASLGHRLGAGQVPGLTLGLTVGIWGVAALLTLPVTLASGASGGLCTLIYSTELKALQATHTVACLAIFVLLPLGLFGAKGLKKALGMGPGPWMNILWAWFIFWWPHGVVLGLDFLVRSKLLLLSTCLAQQALDLLLNLAEALAILHCVATPLLLALFCHQATRTLLPSLPLPEGWSSHLDTLGSKS | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1, TARC and also for the malaria parasites P.vivax and P.knowlesi. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35553
Sequence Length: 336
Subcellular Location: Early endosome
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Q9QUI6 | MGNCLYPVETLSLDKNGTQFTFDSWNYSFEDNYSYELSSDYSLTPAAPCYSCNLLDRSSLPFFMLTSVLGMLASGSILFAILRPFFHWQICPSWPILAELAVGSALFSIAVPILAPGLHSAHSTALCNLGYWVWYTSAFAQALLIGCYACLNPRLNIGQLRGFTLGLSVGLWGAAALSGLPVALASDVYNGFCTFPSSRDMEALKYTHYAICFTIFTVLPLTLLAAKGLKIALSKGPGPWVSVLWIWFIFWWPHGMVLIFDALVRSKTVLLYTCQSQKILDAMLNVTEALSMLHCVATPLLLALFCHQTTRRSLSSLSLPTRQASQMDALAGKS | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1 and TARC. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36694
Sequence Length: 334
Subcellular Location: Early endosome
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O00590 | MAATASPQPLATEDADSENSSFYYYDYLDEVAFMLCRKDAVVSFGKVFLPVFYSLIFVLGLSGNLLLLMVLLRYVPRRRMVEIYLLNLAISNLLFLVTLPFWGISVAWHWVFGSFLCKMVSTLYTINFYSGIFFISCMSLDKYLEIVHAQPYHRLRTRAKSLLLATIVWAVSLAVSIPDMVFVQTHENPKGVWNCHADFGGHGTIWKLFLRFQQNLLGFLLPLLAMIFFYSRIGCVLVRLRPAGQGRALKIAAALVVAFFVLWFPYNLTLFLHTLLDLQVFGNCEVSQHLDYALQVTESIAFLHCCFSPILYAFSSHRFRQYLKAFLAAVLGWHLAPGTAQASLSSCSESSILTAQEEMTGMNDLGERQSENYPNKEDVGNKSA | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs.
PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43443
Sequence Length: 384
Domain: The C-terminal cytoplasmic tail controls its phosphorylation, stability, intracellular trafficking itinerary, and chemokine scavenging properties.
Subcellular Location: Early endosome
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O08707 | MPTVASPLPLTTVGSENSSSIYDYDYLDDMTILVCRKDEVLSFGRVFLPVVYSLIFVLGLAGNLLLLVVLLHSAPRRRTMELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVISTLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKAQFRNLLLIVMVWITSLAISVPEMVFVQIHQTLDGVWHCYADFGGHATIWKLYLRFQLNLLGFLLPLLAMIFFYSRIGCVLVRLRPPGQGRALRMAAALVIVFFMLWFPYNLTLFLHSLLDLHVFGNCEISHRLDYTLQVTESLAFSHCCFTPVLYAFCSHRFRRYLKAFLSVMLRWHQAPGTPSSNHSESSRVTAQEDVVSMNDLGERQSEDSLNKGEMGNT | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs.
PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43207
Sequence Length: 378
Domain: The C-terminal cytoplasmic tail controls its phosphorylation, stability, intracellular trafficking itinerary, and chemokine scavenging properties.
Subcellular Location: Early endosome
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P25106 | MDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCKVTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARAISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQSTK | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1 . Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway . Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness . In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival . Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration . Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12 . Required for heart valve development . Regulates axon guidance in the oculomotor system through the regulation of CXCL12 levels .
PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41493
Sequence Length: 362
Domain: The C-terminal cytoplasmic tail, plays a key role in: correct trafficking to the cell membrane, recruitment of beta-arrestin, ubiquitination, and in chemokine scavenging and signaling functions. The Ser/Thr residues and the Lys residues in the C-terminal cytoplasmic tail are essential for beta-arrestin recruitment and ubiquitination respectively.
Subcellular Location: Cell membrane
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P56485 | MDVHLFDYAEPGNYSDINWPCNSSDCIVVDTVQCPTMPNKNVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVITIPVWVVSLVQHNQWPMGELTCKITHLIFSINLFGSIFFLACMSVDRYLSITYFTGTSSYKKKMVRRVVCILVWLLAFFVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVILGFAVPFTIIAIFYFLLARAMSASGDQEKHSSRKIIFSYVVVFLVCWLPYHFVVLLDIFSILHYIPFTCQLENVLFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQNTK | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Regulates axon guidance in the oculomotor system through the regulation of CXCL12 levels .
PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41636
Sequence Length: 362
Domain: The C-terminal cytoplasmic tail, plays a key role in: correct trafficking to the cell membrane, recruitment of beta-arrestin, ubiquitination, and in chemokine scavenging and signaling functions. The Ser/Thr residues and the Lys residues in the C-terminal cytoplasmic tail are essential for beta-arrestin recruitment and ubiquitination respectively.
Subcellular Location: Cell membrane
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Q9NPB9 | MALEQNQSTDYYYEENEMNGTYDYSQYELICIKEDVREFAKVFLPVFLTIVFVIGLAGNSMVVAIYAYYKKQRTKTDVYILNLAVADLLLLFTLPFWAVNAVHGWVLGKIMCKITSALYTLNFVSGMQFLACISIDRYVAVTKVPSQSGVGKPCWIICFCVWMAAILLSIPQLVFYTVNDNARCIPIFPRYLGTSMKALIQMLEICIGFVVPFLIMGVCYFITARTLMKMPNIKISRPLKVLLTVVIVFIVTQLPYNIVKFCRAIDIIYSLITSCNMSKRMDIAIQVTESIALFHSCLNPILYVFMGASFKNYVMKVAKKYGSWRRQRQSVEEFPFDSEGPTEPTSTFSI | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization. Plays an important role in controlling the migration of immune and cancer cells that express chemokine receptors CCR7 and CCR9, by reducing the availability of CCL19, CCL21, and CCL25 through internalization. Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell development in the thymus.
PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39914
Sequence Length: 350
Subcellular Location: Early endosome
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A5D6U8 | MAAAPPPPPPLLLLLLCVCAVFADVPIGTQPEQVHISYPGVQNSMLVTWSSANKTDSVVEYGLWGGKLFSHSATGNSSIFINEGAEYRVMYIHRVLLTDLRPAASYVYHCGSGAGWSELFFFTALNESVFFSPGFALFGDLGNENPQSLSRLQKETQIGTYDVILHIGDFAYDLYEDNGRIGDEFMKQIQSIAAYVPYMTCPGNHEWAFNFSQYRARFSMPGDTEGLWYSWNVGPAHIISFSTEVYFYYLEYGLDLLFRQYEWLRADLQEANRPENRAERPWIITMGHRPMYCSNDDDDDCTHFQSYVRLGRNDTKPPAPGLEELFYQYGVDLELWAHEHTYERLWPVYDYKVFNGSSEEPYVNPKAPVHIITGSAGCREKHDGFIPKPRDWSAFRSTDYGYTRLQLINNTHLYLEQVSDDQYGKVIDQMTLVKEKHGPDAWR | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 50745
Sequence Length: 443
Subcellular Location: Secreted
EC: 3.1.3.2
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Q6ZNF0 | MHPLPGYWSCYCLLLLFSLGVQGSLGAPSAAPEQVHLSYPGEPGSMTVTWTTWVPTRSEVQFGLQPSGPLPLRAQGTFVPFVDGGILRRKLYIHRVTLRKLLPGVQYVYRCGSAQGWSRRFRFRALKNGAHWSPRLAVFGDLGADNPKAVPRLRRDTQQGMYDAVLHVGDFAYNLDQDNARVGDRFMRLIEPVAASLPYMTCPGNHEERYNFSNYKARFSMPGDNEGLWYSWDLGPAHIISFSTEVYFFLHYGRHLVQRQFRWLESDLQKANKNRAARPWIITMGHRPMYCSNADLDDCTRHESKVRKGLQGKLYGLEDLFYKYGVDLQLWAHEHSYERLWPIYNYQVFNGSREMPYTNPRGPVHIITGSAGCEERLTPFAVFPRPWSAVRVKEYGYTRLHILNGTHIHIQQVSDDQDGKIVDDVWVVRPLFGRRMYL | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 50480
Sequence Length: 438
Subcellular Location: Secreted
EC: 3.1.3.2
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Q5B2K4 | MSAEQNHGLEKDVGGPAAPAAAAPNAPAAAPGAPPAGMSAEEHRSRFGYGPLSHVNTKEAILPPFGGEFQPGLYKSVEARKFANPAPLGLSAFALTTFVLSCINMGARDITHPNIVIALAFGYGGLVQLLAGMWEMAVGNTFGATALSSYGGFWIAFAIVLTPGGFNIQTALTAENGDEAMFYNSFGLFLMGWFIFTTIMLFCTLRSTVAFFLLFLFLDLAFLLLGVGYIQRDDAGQPNPPVIKAGGFFGLLAAFAAWYNALAGIADSSNSFFIIPVAHFPWSPTGRARREKTERETV | Function: High affinity monocarboxylate transporter (MCT) involved in acetate uptake. Unlike other activities involved in acetate utilization, acpA is dispensable for growth on the acetate precursor ethanol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31646
Sequence Length: 298
Subcellular Location: Cell membrane
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Q5BLY5 | MSVIAILAMVVGVQAELKQINVIFRHGDRIPDEKNEMYPKDPYLYYDFYPLERGELTNSGKMREYQLGQFLRERYGDFLGDIYTEESVSALSSFYDRTKMSLQLVLAALYPPNKLQQWNEDLNWQPIATKYLRRYEDNIFLPEDCLLFTIELDRVLESPRGKYEFSKYDKLKKKLEEWTGKNITTPWDYYYIYHTLVAEQSYGLTLPSWTNNIFPRGELFDATVFTYNITNSTPLLKKLYGGPLLRIFTKHMLDVVSGTQKKKRKIYLFSGHESNIASVLHALQLYYPHVPEYSSSIIMELHNIEGTHYVKIVYYLGIPSEARELQLPGCEVLCPLYKYLQLIENVIPSNEELICDKRFVDESANNLSIEELDFVKLNLIRIAGTENK | Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 45389
Sequence Length: 388
Subcellular Location: Secreted
EC: 3.1.3.2
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P80227 | MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGRYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGSTGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDISGSDDEMARPKKPDQAIKGDQFLFYEDWGENMVSKGSPVLCVLDIESGNISVLEGVPESVSPGQAFWAPGDTGVVFAGWWHEPFRLGIRFCTNRRSALYYVDLTGGNCELLSDDSLAVTSPRLSPDQCRIVYLQFPSLVPHQQCGQLCLYDWYTRVTVVVVDVVPRQLGENFSGIYCSLLPLGCWSADSQRVVFDTAQRSRQDLFAVDTQMGTVTPLTAGGSGGSWKLLTIDRDLMVAQFSTPNLPPCLKVGFLPPAGMEQEVVWVSLEEAEPIPDISWSIRVLQPPPEQEHAQYVGLDFEAILIQPSNPPDKTQVPMVVMPHGGPHSSFVTSWMLLPAMLCKMGFAALLVNYRGSTGFGQDSILSLPGNVGSQDVKDVQFAVEQVLQEEHFDAGRVALLGGSHGGFLSCHLIGQYPETYGACVVRNPVINIASMMGSTDIPDWCVVEAGYLYSSDCLPDPNVWSEMLNKSPIKYTPQVKTPVLLMLGQEDRRVPFKQGMEYYRALKARNVPVRLLLYPKSTHSLSEVEVESDSFMNAVIWMCTHLGH | Function: This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus . It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity). Also, involved in the degradation of oxidized and glycated proteins (By similarity).
Catalytic Activity: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
Sequence Mass (Da): 81093
Sequence Length: 730
Subcellular Location: Cytoplasm
EC: 3.4.19.1
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Q97HJ4 | MRELTSEIKKEIRDIVYDFFSEECEVDINELNDNTSVVDDLDGDSLMLIELVDILKKKYSLNIQLQSIGKYLLKNPAETLEKVVQTTYLLYEYENDITNVGEK | Function: Acyl carrier protein.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the apo-ACP-like protein.
Sequence Mass (Da): 12000
Sequence Length: 103
Subcellular Location: Cytoplasm
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A8FA63 | MIKGIGLDIVEINRLAHVLSRQPRLPERILTLNEQDIFHALSEKRQLEFLAGRFAAKEAFAKAYGTGIGRHLSFHDIEIQKDEHGKPFIKSEKTKDDQVHVSITHTKEYAAAQVLIERLSS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13757
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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P96618 | MIYGIGLDITELKRIASMAGRQKRFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKDQNGKPYIICTKLSQAAVHVSITHTKEYAAAQVVIERLSS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-alanyl carrier protein but fails to recognize PCP and AcpK, an acyl carrier protein of secondary metabolism.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13718
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A7Z1L9 | MIFGIGIDIVELHRIENMLSRQARFPQRILTEAEYARFTLLSDKRKIEFLAGRFAAKEAFSKAYGTGIGKELSFQDIETGNDKAGKPVLACAKLDCATVHVSITHTKEYAAAQVVIERLSR | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13503
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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B8DVV4 | MLGLGHDVVDVGAFAEQLEMPGTRMTRLFSARECRQASLRASIKHDGEALHLAAKWAAKESVVKAWCEALVGRGITERPYTVDDTPWSRIEIVDDATGCPRVVMAAEVHVELCRSLAVTESAEPVWHVSISHDGGIASAVAVLDMRE | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 15978
Sequence Length: 147
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A1A005 | MLGLGHDVVDVPAFAKQLNEPGTRMRNLFSMREIWQTAQRSQLKHDDEAVHLAARWAGKEAFLKAWCAAISRHAKDGAEVAYPYTLDNFPWVRIEILDDSHGVPRVILSSEVQRKVQQSLGLPLDPVCQSYDISISISHDGPIASAVVMLEI | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 16959
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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O51043 | MKSIGCDIIKVERFKNFLENKKKMERFFTHKEIENFKLKGGSIIESLAGKFAAKESLIKALSPLLQYKINYTLKDIEVIKSLKGNAEFCLHNEVEKFAIKMNLKLYLTISHEKEYAIAFVIVEN | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14376
Sequence Length: 124
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q7NE72 | MAGQTFLHRIGTDLVHIPRIEGMLERYGKQFLNRVYTEGEQHYCLASKPHRANRLAGRWAAKEAVTKALGTGWRGVGYRDIEVVRLASGEPTICLNGRAVLLVERFGRLDWQVSFSHDREYAVATVSVIGFF | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14919
Sequence Length: 132
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q0BTG4 | MIIGIGSDICDIRRIETVLERHGERFLSRVFTTAERAKAERRNGRMRMGTYAKRFAAKEACAKALGTGFAGGVFMSDLGVVNLSSGQPTLRLTGGAAARLSAMTPSGMGAQVLLTMTDEYPYAYAQVVISAVPLPTSLIGGRGLP | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 15398
Sequence Length: 145
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q9KFG1 | MIIGTGIDIVELERIQSMVEKHPRFVKKILTENEQEVFARLSRRRRLEYIAGRFAAKEAFVKAVGTGISAEYGWHDLEVLSDERGKPVLSVNLDATIHVSISHSQSYAIAQVILERLSS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13421
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A1WT13 | MIAGIGTDIVAVVRLERALERHGERFAQRILAPTELLNFREGGATAAFLARRFAAKEAASKALGTGFSDGVTLRDLEVVHDVRGQPSLRFHGAAAERAVALGVSEAALSLSDEREYAVAFVILVTG | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13389
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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B8D0V9 | MIRGIGIDIVEVNRISDMVDKWGERFLNKVYTPYEVNYCKFKSNTYECLAGRFAAKEAFVKMLGTGFKHIYFKDIEVRSDEKGKPYLRIKGNADRLTKESGIKRIHLSISHERKFAIAFVVGEEG | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14429
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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O25488 | MIGIDIVSIARIEKCVKRFKMKFLERFLSPSEIVLCKDKSSSIAGFFALKEACSKALQVGIGKELSFLDIKISKSPKNAPLITLSKEKMDYFNIQSLSASISHDAGFAIAVVVVSSSNE | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13004
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A9B2B6 | MLVTGVDLIEIDRINQAVSRWGQRFARRVWTEAEWLRCRDSAQSLAARWAAKEAAAKALGVGLKGIGHPACAVAWREIEVANDTQGKPLLRLHGAAQQRANELGIRHWSVSLSHSGDQAIAFVVGMG | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13865
Sequence Length: 127
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q31HN9 | MIVGIGTDLVEIARIAALMTKRNEVFAKRILAQQELERFKQHGQPEKFLAKRWAAKEAISKALGTGFTQGVCFTDMIIGHTDQGQPLIELTGKTAEIAQQLGIENWSISISDEAHYAVAFVIAESRS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14000
Sequence Length: 127
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
B4U7U7 | MLGIDIIKNIRIAKALERFGYHFLNRVYTEYEINLCKMNVECLSGRFAAKEASIKAFSFLSIRRFSFRDFEVVKSKNGIPELRIKDAYINDFLKAQKLKPFISISHEKEFSVAVCYITKEERIC | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14526
Sequence Length: 124
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
G2TRL9 | MGLGIDILKISRISRLIQRSPEWEKNFLKKCLCENEIKKYNLIKSNSSLPRLSEQAKWLAVRWCVKEAVFKALQPNFRVYMSMMEYVRTPTGYPSVVIHDPRFPLSPVMVSVSHEEDLVVANALYLPSMPKT | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 15271
Sequence Length: 132
EC: 2.7.8.7
|
Q12KI5 | MAIIGIGTDIVEIERIREQRDRLGDKLAKRVLTLDELAIYAAVNMPERYLAKRFAAKEAAAKALGTGIGRGVSFQHIHISNDDNGAPLVNFTDGAALRLAQLGGCKGHISIADEKHYAIATVILES | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13581
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q8EH77 | MAIVGLGTDIVEIERISAHVARSGDKLAKRVLTEAEFEIYQQHSQPSRYLAKRFAAKEAAAKALGTGIGRGVSFQHIHIGNTPDGAPTIDFTEGAQQRLTLLNGVVGHISIADEKSYAIATVILESR | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13639
Sequence Length: 127
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
P80643 | MADTLERVTKIIVDRLGVDEADVKLEASFKEDLGADSLDVVELVMELEDEFDMEISDEDAEKIATVGDAVNYIQNQQ | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8591
Sequence Length: 77
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
|
A1US60 | MSDTEERVKKIIVEHLGVDADKVVQNASFIDDLGADSLDTVELVMAFEEEFGIEIPDDAAETIFTVNDAVKFIDKASS | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8548
Sequence Length: 78
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
|
Q7V9R0 | MSQEAILEKVRSIVAEQLSVEASEIKPDSNFQNDLGADSLDTVELVMALEEAFDIEIPDEAAEGITTVGDAVKYIEDKQS | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8701
Sequence Length: 80
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
|
P80923 | MSTIEERVKKIVAEQLGVKSEEVVNTASFVEDLGADSLDTVELVMALEEEFETEIPDEEAEKITTVQAAIDYVNSHQA | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8614
Sequence Length: 78
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
|
Q8NEB7 | MRKPAAGFLPSLLKVLLLPLAPAAAQDSTQASTPGSPLSPTEYERFFALLTPTWKAETTCRLRATHGCRNPTLVQLDQYENHGLVPDGAVCSNLPYASWFESFCQFTHYRCSNHVYYAKRVLCSQPVSILSPNTLKEIEASAEVSPTTMTSPISPHFTVTERQTFQPWPERLSNNVEELLQSSLSLGGQEQAPEHKQEQGVEHRQEPTQEHKQEEGQKQEEQEEEQEEEGKQEEGQGTKEGREAVSQLQTDSEPKFHSESLSSNPSSFAPRVREVESTPMIMENIQELIRSAQEIDEMNEIYDENSYWRNQNPGSLLQLPHTEALLVLCYSIVENTCIITPTAKAWKYMEEEILGFGKSVCDSLGRRHMSTCALCDFCSLKLEQCHSEASLQRQQCDTSHKTPFVSPLLASQSLSIGNQVGSPESGRFYGLDLYGGLHMDFWCARLATKGCEDVRVSGWLQTEFLSFQDGDFPTKICDTDYIQYPNYCSFKSQQCLMRNRNRKVSRMRCLQNETYSALSPGKSEDVVLRWSQEFSTLTLGQFG | Function: Acrosomal protein that maintains proacrosin (pro-ACR) as an enzymatically inactive zymogen in the acrosome. Involved also in the acrosome formation.
PTM: Phosphorylated on Tyr residues in capacitated sperm.
Sequence Mass (Da): 61359
Sequence Length: 543
Subcellular Location: Secreted
|
Q3V140 | MMNLAAGFLLMLLEVLLLPGTPLSAEESPASTPGSPLSSTEYERFFALLTPTWKAETTCRLRATHGCRNPTLVQLDQYENHGLVPDGAVCSDLPYASWFESFCQFAQYRCSNHVYYAKRVRCSQPVSILSPNTLKEVESSAEVPPTSMTTPIVSHATATEHQAFQPWPERLNNNVEELLQSSLSLGGKDQQSSRRPGQEQRKQEQIQEHKLEEAQEQEEQEEEEEEEEAKQEEGQGTEAGLESVSRLQSDSEPKFQSQSLSSNPSFFTPRVREVESAPLMMKNIQELIRSAQEMDEMNELYDDSWRSQSTGSLQQLPHMETLMVLCYSIMENTCTMTPTAKAWSYMEEEILGFGDSVCDNLGRRHTAACPLCAFCSLKLEQCHSEASVLRQKCDASHKIPFISPLLSAQSISTGNQARIPDKGRFAGLEMYGGLSSEFWCNRLAMKGCEDDRVSNWLKAEFLSFQEGDFPTKICDTNYIQYPNYCSFKSQQCLLRNQNRKMSRMRCMLNERYNVLSLAKSEEVILRWSQEFSTLAIGQFG | Function: Acrosomal protein that maintains proacrosin (pro-ACR) as an enzymatically inactive zymogen in the acrosome. Involved also in the acrosome formation.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 61141
Sequence Length: 540
Subcellular Location: Cytoplasmic vesicle
|
Q876Q0 | MPRSSATARKSHSNRQDHGGGGSGKKPSKQKSSGHLNATYNGTAGSETGPSSQVDWPSHRSGDQSIAAAAAKSNGPVDSLKADTNGRGYPGGYAKGNADMSYGQTNGGVSPNGGLAGPASRRTDKSVTGTKRTTSNASVNPFQLASTILRSCPMYDTIAILIFLLQLPPMVLTLVQFLFASLTFMPPSGTASGSFTSNFDIFQGPAGTPSLGTMIAMDGFCLLVWGLFMWTWAQNFALDLAHVQVAITLGGGGAGKNGGVNALCVGIVLILHLIRSKGIQDFVVGHLVSAKIISPDLLSHYSYLMPAEFKRTESQSSPSWIRSLLAVHILAQAGTAMARRSMTKNRTPAPSRSGKRVDTEASAGSQTQIDSAFESAASVSSYLGPDGQIITAAHKDGRDRLISAKKRRRQANQVRSRQPFWAALASTKVTVMREYEHSRALSKTARGLATTEDDLQGVSLDDGLVWITYVDSSTIKFAAGDFASSDDHSASGVCEAGRVSSEDAEPFYVCVNGAPWATVVITKEHDPSKASNTIYWRGEISGLAPNCAYTCSFVKCDTDEEICAMSVKTPAANDAEQANSVPAPPQPSYRPSSPTTTLKNSIINAEAKLNEKRARLRKAKNDHKLAISKIKKELDNYTNRLQSGTDENRQKQRSLQLERNIRQTEEATAALDNQIDNLGNVPDDEYQEWVEQKAKYERELELLKSAKAEIAATRTANARELSSLESELNSTTQRRERLQGRRTRVNEQYERIISANAQGLNERERRAAEQFAREQDQSKLEQSFNEQFASISQSVQDYQLRTSQLWQQCTAVEQALQQQLLMEPAPLTPEGELPGTSTFADAPSVPLGTLASNMPSHRSLLGQSFPPLKSSPLQHYASPIGTAPSHPTSPIAAPSYQPFSSSPFGNAASFLDPDFVYRDRSFSNRSARSSLYGSEFPDAITARRVPFGVDPFELGNEKRRGSGSDSTPLNGPSGLRPISSPFQRAASRASGTGSGGSGGSGSGSGSPSSARGKGN | Function: component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Involved in resistance to acriflavine, and required for normal growth on a range of sole carbon sources, including fructose, cellobiose, raffinose, and starch, and reduced utilization of amino acids, including GABA and beta-alanine, as sole carbon and nitrogen sources.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108927
Sequence Length: 1015
Subcellular Location: Membrane
|
Q9X928 | MSNESLANLLKEERRFAPPADLAANANVTAEAYEQAKADRLGFWAEQARRLTWAKEPTETLDWSNPPFAKWFKDGTLNVAYNCVDRHVEAGNGDRVAIHFEGESGDSRALTYAQLKDEVSKAANALLELGVQKGDRVAIYMPMIPETAIAMLACARIGAAHSVVFGGFSSDALATRIQDADARVVITADGGYRRGKPSALKPAVDEAVERAGIVEHVLVVRRTGQDVAWDDSRDKWWHETVDGQSAEHTPEAFDAEHPLFILYTSGTTGKPKGILHTSGGYLTQTAYTHWAVFDLKPETDVFWCTADVGWVTGHSYIVYGPLANGATQVMYEGTPDTPHQGRFWEIVQKYGVTILYTAPTAIRTFMKWGDDIPAKFDLSSLRVLGSVGEPINPEAWIWYRKNIGADATPVVDTWWQTETGAMMITPLPGVTHAKPGSAQRPLPGISATVVDDEANEVPNGGGGYLVLTEPWPSMLRTIWGDDQRFIDTYWSRFEGKYFAGDGAKKDDDGDIWLLGRVDDVMLVSGHNISTTEVESALVSHPSVAEAAVVGATDETTGQAIVAFVILRGTTAESEDLVAELRNHVGATLGPIAKPKRILPVSELPKTRSGKIMRRLLRDVAENRQVGDVTTLADSTVMDLIQTKLPAAPSED | Function: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Sequence Mass (Da): 71045
Sequence Length: 651
EC: 6.2.1.1
|
Q55404 | MSDTIESILQEERLFDPPTEFSERAYVRSGREYEQLYSRAASNPEKFWGELAEQELHWFKKWDQVLDWQPPFAKWFVGGQLNISHNCLDRHLTTWRRNKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKCPIVDTWWQTETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEISGDTSTLEDRTVLDKLREG | Function: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Sequence Mass (Da): 73052
Sequence Length: 653
EC: 6.2.1.1
|
Q5SIW6 | MDRLESVLKEERVFYPSEEFRKQAHIKSEEEYQRLYEESVRDPEGFWGRVASELHWFEPWRKVLEGDLPHPKWFVGGKTNLSYNALDRHVKTWRRNKAAIVWEGEPGEERVLTYHDLWREVQRFANVLKRLGVKKGDRVTIYLPMIPEAAIAMLACTRIGAVHSVVFGGFSAGALADRIKDAEAKVLITADGGFRRGGIVPLKQNADEALKDATSVEHVVVVRRTGEEVPWTPGRDHWWHELMEAAPDRCDPEPMEAEEPLFILYTSGSTGKPKGVLHTTGGYMTYVYYTTKLVFDLKDEDVYWCTADVGWITGHSYVVYGPLLNGATTVMYEGAPNWPEPDRFWRIVDKYGVTVFYTAPTAIRSFMKWGEGWPGKHRLDSLRLLGTVGEPINPEAWLWYYHVIGKGRCPIVDTWWQTETGGIMITTLPGAHAMKPGHAGKPFFGVVPEILDGEHRPVENPDEGGHLCITRPWPSMLRTVWGDPERFLQQYFSQHPGVYFSGDGAKRDKDGYYMILGRVDDVLNVAGHRLGTMEIESALVAHPAVAEAAVVGRPDPVKGEAIVAFVTLKEGHTPSDALKEELRAHVAKVIGPIARPDEIRFTDALPKTRSGKIMRRLLRQIAAGEKEIKGDTSTLEDRSVVERLKEGA | Function: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Sequence Mass (Da): 73086
Sequence Length: 648
EC: 6.2.1.1
|
Q9Y896 | MDDEIQAVVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGVMVGLSNKDSYVGDEAQAKRGVLTLKYPIEHGTVTNWDDMEKIWHHTYYNELRVAPEEHPVLLTEAPLNPKTNREKMTQIMFETFNVPAFHVSIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGFSLPHAIQRLDLAGRDLTERLVLHLTERGYTFTTSAEKEVVRDIKERLCYVALDFDQELITAAQSSALEKNYELPDGQIITIGNERFRAPEVFFQPSFAGMESGGIADLVYTSIQRCDLDIRRELYGNIVMSGGTTMFPGISDRMQRELSNMAPANMKVKIVAPPERKYSVWIGGSILASLSTFQNMWCSKQEYDESGPGIVHRKCL | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 41794
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
Q96483 | AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYDGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDNLMKILTERGYMFTTTAEREIVRDMKEKLAYVALDYEQEIETARSSSSIEKNYELPDGQVITIGAERFGCPEVLFQPSMIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQ | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 37175
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P93374 | AGFAGDDAPRAVFPSIVGRPRYTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPLLLTEAPLNPKANREKMTEIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTAAEREIVRDLKEKLAYVSLVFEQELETSKNSKDVEKSYELPDGQIITIGAERFRCPEVLFQPSFIGMEAVGIHETTYNSIMKCDVDIRKDLYGNVVLSGGSTMFPGITDRMSKEISALAPNSMKIKVVAPPERKYSVWIGGSILASLSTFQQ | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 37370
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P20399 | MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF | Function: Actins are highly conserved proteins that are involved in various types of cell motility.
PTM: Oxidation of Met-46 and Met-49 by MICALs (mical1, mical2 or mical3) to form methionine sulfoxide promotes actin filament depolymerization. Mical1 and mical2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by msrb1 and msrb2, which promote actin repolymerization (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 42033
Sequence Length: 377
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P18602 | QKDSYVGDEAQSKRGILTLKYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYTFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQIITIGNERFRCPEALFQPSFLGMETCGIHETAYNSIMKCDVDIRKDLYANTVLSGGTTMFPGIADRMQKEITMLAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 36891
Sequence Length: 327
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P45886 | MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMESSGIHETVYNSIMKCDVDIRKDLYANIVMSGGTTMYPGIADRMQKEITALAPSTIKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVHRKCF | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-45 to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 41816
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
Q8BFZ3 | MVDDELTALVVDNGSGMCKAGFGGDDAPRAVFPSMVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILTLKYPIEHGVVTNWDDMEKIWYHTFYNELRVAPDEHPILLTEAPLNPKINREKMTQIMFEAFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYNFTTTAEREIVRDVKEKLCYVALDFEQEMVTAAASSSLERSYELPDGQVITIGNERFRCPEAIFQPSFLGIESRGIHETTFNSIMKCDVDIRKDLFANTVLSGGSTMYPGIADRMQKEIVTLAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPPIVHRKCF | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization.
Sequence Mass (Da): 42004
Sequence Length: 376
Subcellular Location: Cytoplasm
|
P84856 | MCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVYNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANLEKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERYGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
PTM: ISGylated.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 40445
Sequence Length: 361
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
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