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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccA family.
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MAAPVTKKPILLEFEKPLVELEERITQIRTLAADNQVDVSGQIQQLEARAIQLRREIFSNLSPAQRIQVARHPRRPSTLDYIQAISDEWIELHGDRNGSDDLALVGGVGALDGQPVVFLGHQKGRDTKDNVLRNFGMASPGGYRKALRLMEHADRFGMPILTFIDTPGAYAGVSAEELGQGEAIAVNLREMFRFSVPILCTVIGEGGSGGALGIGVGDRLLMFEHSVYTVASPEACASILWRDAGKAAQAAEALKITARDLKQLGILDEIITEPLGGAHSAPLETAQSLRQVLLRHLKDLQALSPAQLREQRYQKFRQLGVFLESSD
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccA family.
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MPKTERRTFLLDFEKPLSELESRIHQIRDLAAENNVDVSEQIQQLEARADQLREEIFSTLTPAQRLQLARHPRRPSTLDYVQMMADEWFELHGDRGGSDDPALIGGVARFDGQPVMMLGHQKGRDTKDNVARNFGMPAPGGYRKAMRLMDHANRFGMPILTFIDTPGAWAGLEAEKLGQGEAIAFNLREMFSLDVPIICTVIGEGGSGGALGIGVGDRVLMLKNSVYTVATPEACAAILWKDAGKSEQAAAALKITAEDLKSLEIIDEIVPEPASCAHADPIGAAQLLKAAIQDNLQALLKLTPERRRELRYQRFRKIGVFLESS
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccA family.
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MAAPVTKKPILLEFEKPLVELEERITQIRTLAADNQVDVSGQIQQLEARAIQLRREIFSNLSPAQRIQVARHPRRPSTLDYIQAISDEWIELHGDRNGSDDLALVGGVGALDGQPVVFLGHQKGRDTKDNVLRNFGMASPGGYRKALRLMEHADRFGMPILTFIDTPGAYAGVSAEELGQGEAIAVNLREMFRFSVPILCTVIGEGGSGGALGIGVGDRLLMFEHSVYTVASPEACASILWRDAGKAAQAAEALKITARDLKQLGILDEIITEPLGGAHSAPLETAQSLRQVLLRHLKDLQALSPAQLREQRYQKFRQLGVFLESSD
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MKEFFRLSRKGFTGREDQDSAQIPDDLWVKCSSCRELIYKKQLNDNLKVCPKCGHHMRLSAHEWLGLLDVGSFREMDANLLPTDPLGFVTDEESYAAKLAKTQQRTGMADAVIAGIGAISNMQICVAVADFSFMGASMGSVYGEKMARSAERAAELGVPLLTINTSGGARQQEGVIGLMQMAKVTMALTRLADAGQPHIALLVDPCYGGVTASYPSVADIIIAEPGANIGFAGKRLIEQIMRQKLPAGFQTAEFMLEHGMIDMVVPRSEMRDTLARILRLYRQRSTSPAKAELAGRRATLPQPIM
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MKEFFRLSRKGFTGRDDVDSAQIPDDLWVKCSACRELIYKKQLNDNLKVCPKCGHHMRMSAHEWIGLLDVGSFREMDSNLLPTDPLGFVAADESYATKLAKTQQRTGMTDAVISGVGAISGIRLCIAVADFSFMGASMGSVYGEKMARAAERAAELGIPLLTINTSGGARQQEGVIGLMQMAKITMALTRLAEAGQPHIALLVDPCYGGVTASYPSVADIIIAEPGANIGFAGKRLIEQIMRQKLPAGFQTAEFMLEHGMIDMVVPRSEMRETLARILKHYQQRQAPAAKADLAARRATLPQPIM
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSWFNRVKPSISSTAKRDVPEGLWWKCEECGAALHKKQMEASDHTCPQCGYHFRISPYKYFSLLFDNQKYVEFDDHLRAADPLHFVDTKKYPDRVSDTIEKSGKTEACRNAHGLCGGETLVISAMDFSFIGGSMGSVVGEKISRAVDKAIELQSPLLVISQSGGARMMEGAFSLMQMAKTAAKLSLLSEHRLPYISLMTDPTMGGITASFAMLGDINISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLLEHGFIDRIIPRRELKSDLTTLLSLMKL
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MVWFKRVKPSIRTTDKRDVPEGLWWKCEECGAMIHKKQLEDHVYTCSDCGYHFRISPYRYFSILFDNDTYQEFDDALRAGDPLGFTDTKKYSDRVHDTIGKSGKTEACRNAWGEVGGNPLVVSAMDFGFIGGSMGSVVGEKISRAVDKAVELNAPLLVISQSGGARMMEGAFSLMQMAKTSARLTLLSEKRLPFFSLMTDPTMGGITASFAMLGDVNLSEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLHEQGFVDCIVHRKELKSQIVRLAGMLKV
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MVWFKRVKPFIRTTDRRDVPEGLWSKCEDCGAMLHRRQLEENLNTCNECGHHFRISPYRYFSILFDNEEFTEFDDCLRAADPLTFVDTKKYPDRVHDTIEKSGKTEACRNAFGKSAGADLVISAMDFGFIGGSMGSVVGEKISRAADKAIELNAPLIVISQSGGARMMEGAFSLMQMAKTAARLTRLGENRLPFISLMTDPTMGGISASFAMLGDLNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLQEHGFVDMIVHRKELKQRLAKTLAMMRVEG
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MVWFKRGIPSIKTTDKRDTPEGLWSKCDECGAALHKKQLEDHLYTCPECGHHFRISPDLYFSFLFDDGAWDEFDGQLRAADPLTFVDTKKYPDRVRDTMQKSGKSEACRNATGSMGGSAAVISAMDFGFIGGSMGSVVGEKISRAADKSVELNAPLILISQSGGARMMEGAFSLMQMAKTSARLTRLGERNIPFISLMTDPTMGGISASYAMLGDLNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLKEHGFVDMIVHRKDLRLQLIKLFKHLRG
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MVWFKRAKPAIRTTDRRDMPEGMWWKCDECGAMLHKKQLEDNFYTCSECGYHFRISPYKYFSLLFDGDKYQEFEDQLRSADPLGFTDTKKYLDRVHDIIEKSGKTEACRNAFGEADGRMLVVSAMDFGFIGGSMGSVVGEKIARAVDKAIDLNAPLLVISQSGGARMMEGAFSLMQMAKTAARLTRLSEKKLPFFSLMTDPTMGGITASFAMLGDVNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLLEHGFLDLIVHRRELKTQIVRLMTMLAP
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MAWFKRVTPSIRTTDKRDTPEGMWAKCDSCGAMLHKKQLEDNLFTCPQCAHHFRIAPYKYFSLLFDEGECTEFDQNLRAADPLSFTDTKHYPDRVHDTIEKSGKTEAVRNAYGKCEGADLVVSAMDFGFIGGSMGSVVGEKIARAADRAIQLDAPLLVISQSGGARMMEGAFSLMQMAKTAARLTRLGEKKLPFISLMTDPTMGGISASFAMLGDLNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLLEHGFVDMIVHRKELKQRLAKTLAMMRVEV
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). Belongs to the AccD/PCCB family.
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MEKWWFNSMLSNEELEHRWGLSKSMESLGPIGNTRGSEDPIINDTDKNIHSYSWSDSGSYSCSNVDHFFGVSDIWSFISDETFLVRDSNGKGYSVYFDIENRIFEIDNDSSFLSELESSFSSYLSNGSKNDNRYYDSYMYDTKYSWNNHMNSCIDSYLRSEISIDSYISTGSDNFSDSYIYSYIFSEKVSGSDSESSSIRTSGNDSNFNVRERDNDFDRNQKYGRLWVQCENCYELNYRSFFRSKMNICEQCGYHLKMNSLDRIELSIDSGTWNPMDDDMVSMDPIEFHSMEEPYRDRIDSYQRNTGLTEAVQTGIGQLNGIPIAIGVMDFQFMGGSMGSVVGEKITRLIEYATNESIPVIMVCASGGARMQEGSLSLMQMAKISSASYNYQLNKKLFYVSILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTVPDGSQVAEYSFHKGLFDPIVPRNPLKGVLSELFQLHGFFPLNQNSSGARGSVICSE
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MKEFFRLSRKGFTGREDQDSAQIPDDLWVKCSSCRELIYKKQLNDNLKVCPKCGHHMRLSAHEWLGLLDVGSFREMDANLLPTDPLGFVTDEESYAAKLAKTQQRTGMADAVIAGIGAISNMQICVAVADFSFMGASMGSVYGEKMARSAERAAELGVPLLTINTSGGARQQEGVIGLMQMAKVTMALTRLADAGQPHIALLVDPCYGGVTASYPSVADIIIAEPGANIGFAGKRLIEQIMRQKLPAGFQTAEFMLEHGMIDMVVPRSEMRDTLARILRLYRQRSTSPAKAELAGRRATLPQPIM
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MVWFKRAIPSIRTKDKRDTPEGLWSKCDSCGAALHKKQLEDHLYTCPHCGFHFRISPDLYFSFLFDDGKWEEFDAQLRAADPLKFVDTKPYPERVRSTMQKSGKSEACRNATGKLGGSDAVISGMDFGFIGGSMGSVVGEKIARAADKSVELNAPLIVISQSGGARMMEGAFSLMQMAKTSARLTRLGERGIPFISLMTDPTMGGISASFAMLGDLNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLQKHGFVDTIVHRKDLRAQLIKLLGHMK
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). Belongs to the AccD/PCCB family.
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MSILSWIENQRKLKLLNAPKYNHPESDVSQGLWTRCDHCGVILYIKHLKENQRVCFGCGYHLQMSSTERIESLVDANTWRPFDEMVSPCDPLEFRDQKAYTERLKDAQERTGLQDAVQTGTGLLDGIPIALGVMDFHFMGGSMGSVVGEKITRLIEYATQEGLPVILVCASGGARMQEGILSLMQMAKISAALHIHQNCAKLLYISVLTSPTTGGVTASFAMLGDLLFAEPKALIGFAGRRVIEQTLQEQLPDDFQTAEYLLHHGLLDLIVPRSFLKQALSETLTLYKEAPLKEQGRIPYGERGPLTKTREEQLRRFLKSSKTPEYLHIVNDLKELLGFLGQTQTTLYPEKLEFLNNLKTQEQFLQKNDNFFEELLTSTTVKKALNLACGTQTRLNWLNYKLTEFRIRPKF
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSWLDKIVPSMSRTQRADRRKSVPDGLWRKCPNCEAVLYLPELERHQSVCPKCDHHLRLTARKRLNWFLDTEGREEIAADLQPVDRLKFRDSKKYKDRLAAAQKETDENDALIAMRGKLDGLPVVAVAFEFSFMGGSMGAVVGEKFVRAATQAREEGVPLVCFAASGGARMQEALFSLMQMAKTSAALEKLKQEGVPYISVLTDPVFGGVSASLAMLGDINVAEPNALIGFAGPRVIEQTVREQLPEGFQRSEFLLEHGTVDMIVHRHDMRERLGSVMRKLTHQPHQDRDAEPDDTASQSTLDEFSQADH
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). Belongs to the AccD/PCCB family.
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MEKWWFNSMLFNKKLEYRCGLSKSIDSFGPIEKKSEEPSIVTDNDSYSHVDYLVDVSNRQNFLSDKTFLVRDRNSYSYSIFFAIENKILEIDYDSQFNWKNIINSCIENYLRSQICIDSDILDNSFKYNDNDSDVYSYICGKVTNSSQSTSTDVITITNDSEKESFNDDDDFTQKYKHLWVQCESCYGLNYKKFFKSKMNICEHCGDHLKMSSSDRIELLIDPGTWNPRDEDMVSLDPIEFDPIELDPIELDPIELDSEDEPYKTRLDSYQKRTGLSEAVQTGTGQINGIPVAIGIMDFQFMGGSMGSVVGEKITRLIEYATNQLLPLIIVCASGGARMQEGSLSLMQMAKISSALYNYQINQKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNTEVPEGSQSAEFLFEKGLFDSIVPRNLLKEVLGELFQFHGFFPLTQNGN
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MAWFKRDNPPQAKGPAHRVKVPEGLWTKCVSCGETIYTKDIENNLNVCPKCNHHYRVSSKKRLELLLDEGSFTEFDAGVVSVDFLEFKDSKSYQDRIDQALAKGGSKDAIICGSGRIEGTPVQICVFDFSFMGGSMGSVVGEKITRGIERALSDRTPCIIVSASGGARMQESILSLMQMAKTSAALAKLREAGLPFVSILTDPTTGGVTASFAMLGDINMAEPKALIGFAGPRVIEQTIRQKLPQGFQRSEYLLDHGMVDVIVERSKMKSQLSSILTMLYRP
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSWIERIKSNITPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMSARNRLHSLLDEGSLVELGSELEPKDVLKFRDSKKYKDRLASAQKETGEKDALVVMKGTLHDMPIVAAAFEFSFMGGSMGSVVGARFVRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKTSAALAKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFAGPRVIEQTVREKLPPGFQRSEFLIEKGAIDMIVRRPEMRLKLASVLAKLMNLPAPNPDAPREGEVVPPVPDQEPEA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). Belongs to the AccD/PCCB family.
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MKKWWFNSMLSKGKGELEYRCWLSKSMESPGPIKNPSVSEELIRNDKNKNIHSSSDSDSSSYSKLAGVRDIHNFISDDTFFVKDSNRDSYSIYFDIENQILELDNAHSFLSELESSFYSFRNYSSRNNGSKSADPDSDRYMYDTKSSWNNHIHNCLDSYLHSQICIDSHVLSSSDNYSASYIYNFICSESESSNIQSSTNGSDLTISESSNESESSNESDVTQKYRHLWVQCENCYGLNYKKFLKSKMYLCEQCGYHLKMISSDRIDLLVDPGTWDPMDDDMVSIDPIEFDSEEEPYKNRIDSYQSKTGLTEAVQTGTGQLNGIPIAIGVMDFQFMGGSMGSVVGEKITRLIEYAANKFLPLLLVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYVSILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTVPEGSQEAEYLFDKGLFDPIVPRNPLKGVLSELFLFHGRFPLNQN
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MGLFKKRKYITVSSKNLDENNDVENQPTIPDGMWIKCSKCGKILYKSDVDDNFKVCPKCNAHLRMNARERIEFIIDEGTFIEFDKNMMAANPLEFPNYEAKIKSMQEKTGLKDGVVTGLGNINGYKTVIAVMDSNFMMGSMGSVVGEKITRAIEEATERKLPVIIFTTSGGARMQEGMFSLMQMAKTSAALAKHNEAGLLYVSVLTDPTTGGVTASFAMLGDIILAEPKTLIGFAGRRVIEQTINQKLPSDFQTSEFLFKHGFIDMIVERKELKVTLGNILRMHS
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MLKNLFRKTKYITVSQKNIENYKRENTPTIPDGMWVKCNKCGEILYQNDLEKNYMVCNLCGNHFRIGVKERIKYLFDKDTFKEWDYKIKTENPLDFKGYDEKIEHIKEKTNLSEAVTTGKCKIAGMEVVVCIMDSKFMMGSMGSVVGEKITRAIERAIGLRLPVIIFTASGGARMQEGILSLMQMAKVSSALAKLDEEGLLYICVLTDPTTGGVTASFAMLGDIILAEPDALIGFAGKRVIEQTINEKLPEDFQKSEFLLEHGFIDKIVPRSDLRKVLAKLINMHQNSF
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MLKNLFRKTKYITVSQKNIENYKRENTPTIPDGMWVKCNKCGEILYQNDLEKNYMVCNLCGNHFRIGAKERIKYLFDKDTFKEWDYKVKTENPLNFKGYDEKIENIKEETNLSEAVTTGKGKIAGMEVVVCIMDSKFMMGSMGSVVGEKITRAIERAIELRMPVIIFTVSGGARMQEGILSLMQMAKVSSALAKLDEEGLLYICVLTDPTTGGVTASFAMLGDIILAEPDALIGFAGKRVIEQTINEKLPEDFQKSEFLLEHGFIDKIVPRSDLRKVLAKLINMHKNSF
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSLIDWFAARRKDQFVGKVSQDTEESDGLWVKCSECGQVAYRKDLISNFNVCSNCSHHNRINSDERINIIADKDSFKEFDDSLSPTDPLKFKDRRSYSDRIKESQEGTGLKDGVITGICSINSMPLALAVMDFRFMGGSMGSVVGEKITRIIEKATIENYPIVIVCASGGARMQEGMLSLMQMAKISGALKKHRAKNLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLLEHGFVDVIVNRKELKSTLTSILKIHGVKDLMGAN
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSLIDWFAARRKDQFVGKVSQDTDEGDGLWVKCSECSQVAYRKDLISNFNVCSNCGHHNRINSDERINIIADKNSFKEFDSSLSPTDPLGFKDRRSYADRIKESQAGTGLRDGVITGFCSVNSMPLALAVMDFRFMGGSMGSVVGEKITRIIERATIENYPILIVCASGGARMQEGMLSLMQMAKISGALKKHKEKNLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLLEHGFVDVIVKRKDLKTTLTKILKIHGVKELAEANI
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSLFDWFAARRKDQFVGKVIQETEESDGLWGKCPECGQVVYRKDLLTNANVCSNCGHHSRINSEERIKLIVDQGSFIALDKNLAPIDPLGFKDRRAYADRLRESQASTGLKDGVTTGVCRVEEIPLALAVMDFRFMGGSMGSVVGEKITRLIEKATSKKLPLLIVCASGGARMQEGMLSLMQMAKISGALERHREANLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPENFQTAEYLLEHGFVDKIIPRTELRKTLGKLLRLHGFQKITIST
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSWIEKILNKSNITSSRKANIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRISARRRLETFLDTGSTTELGSELEPKDILKFRDSKKYKDRIAAAQKQTHEKDALVVMKGTLKEMPVVAASFEFAFMGGSMASVVGARFVRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKTSAALAKMQERGLPYISVMTDPTMGGVSASLAMLGDINVAEPKALIGFAGPRVIEQTVREKLPAGFQRSEFLLEKGAIDMIVRRPEMRDELAELLAKLTQYDLAKDEDELLGEEMIADDIESSDNEPEINIETNKKEDV
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSLFDWFADRRKGQFVGKVSQETEESDGLWVKCPECGQVVYRKDLHANASVCSNCGYHHRIDSDERIVLIADQGSFKSLDRNLSPTDPLGFKDRRAYADRLRESQASTGMKDGVVTGLCQVEGMPMAMAVMDFRFMGGSMGSVVGEKITRLVERATAQGLPLLIVCASGGARMQEGMLSLMQMAKISGALERHREAELLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLQEHGFVDTIVPRTQLRKTLASLLLLHGCKAKKAAGK
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSLIDWFAARRKDQFVGKVSQDPEESDGLWVKCSECGQVAYRKDLISNFNVCSNCGHHNRINSDERINIIADKDSFKEFDESLSPTDPLKFKDRRSYSERIKESQQGTGLKDGVITGLCSVNSMPLALAVMDFRFMGGSMGSVVGEKITRIVETATIKNYPILIVCASGGARMQEGMLSLMQMAKISGALKKHRAKNLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLLEHGFVDVIVNRKELKSTLTKLLKIHGVKELVQTN
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSLIDWFAARRKDQFVGKVSQDTDEGDGLWVKCSECSQVAYRKDLISNFNVCNNCGHHNRINSDERINIIADKNSFKEFDSLLSPTDPLGFKDRRAYADRIKESQAGTGLRDGVVTGICSVNSMPLALAVMDFRFMGGSMGSVVGEKITRIIERATLENFPILIVCASGGARMQEGMLSLMQMAKISGALKKHKEKNLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLLEHGFVDVIVKRKDLKDTLTKILKIHGVKELAEANT
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSLFDWFADRRKGQFVGKVTQESEESDGLWEKCPECGQVVYRKDLIDNCSVCSNCGHHNRIDSKERIRLISDPNTFKSINNHLTPVDPLGFKDRRAYADRLRESQAGTGLKDGVLTGTCEVNSIPMALAVMDFRFMGGSMGSVVGEKITRLIEHSTKEKLPLLIVCASGGARMQEGMLSLMQMAKISGALERHRDAQLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLQDHGFVDTIVPRTELKETLAKILRLHKTQVVKLQTNA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCNHHMRIGARARLNIFLDVEGREELGADLEPVDRLKFRDGKKYKDRLTAAQKQTGEMDALISMSGTLLGMPVVASAFEFSFMGGSMGAIVGERFVRAANYALENRCPMICFAASGGARMQEALISLMQMAKTSAVLARLREEGLPFISVLTDPVYGGVSASLAMLGDVIVAEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLDHGAIDMIISRSELRPRLGNLLAQMMNLPTPRFVAPVIEPIVVPPAPATI
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSWIEKILPRTKSPTKSNVPEGIWTKCGQCDAVLYKTELEKQLGVCPKCNHHMRVSARARLNQFLDQGERTELGSELEPKDLLKFKDSKKYKDRLVAAQKATNEKDALVVMQGKLKGMPVVVAAFEFAFMGGSMASVVGARFVKAVEACLEHNMPLICFSTSGGARMQEALLSLMQMAKTSAALAKMSEKGLPYISVMTDPTMGGVSASLAMLGDVNVAEPRALIGFAGPRVIEQTVRETLPEGFQRSEFLLEKGAIDVIIDRREMRDRLHSMLSKLHHQQA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSESQKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCDHHMRINARTRLDIFLDEEGREELGADLEPVDRLKFRDSKKYKDRLSAAQKDTGEKDALIAMSGKLEGMPVVACAFEFSFMGGSMGAIVGERFVRAANVALEQRCPLICFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFVSVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDMIVHRGELRPRLARLLSAFTHSPSPVSA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSESQKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCDHHMRINARTRLDIFLDEDGREELGADLEPVDRLKFRDSKKYKDRLAAAQKDTGEKDALIAMSGKLQGMPVVACAFEFSFMGGSMGAIVGERFVRAANVALEKRCPLICFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFVSVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDMIVHRAELRPRLANLLSAFTHSPSPVSA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Inhibited by pyrrolidine dione antibiotic moiramide B (CPD1); in vivo the effects are not seen unless the efflux MexAB-OprM system is inactive. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSESQKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCDHHMRINARTRLDIFLDEDGREELGADLEPVDRLKFRDSKKYKDRLAAAQKDTGEKDALIAMSGKLQGMPVVACAFEFSFMGGSMGAIVGERFVRAANVALEKRCPLICFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFVSVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDMIVHRAELRPRLANLLSAFTHSPSPVSA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCNHHMRIGARARIDIFLDKDGRAELGADLEPVDRLKFRDGKKYKDRLTAAQKQTGEKDALISMSGNLMGLPVVVSAFEFSFMGGSMGAIVGERFVRAANYALENRCPMICFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFISVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDLIISRDELRPRLARLLAQMTGQPTPEAAKEVAAVA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCNHHMRIGARARIDIFLDAEGRAELGADLEPVDRLKFRDGKKYKDRLTAAQKQTGEKDALISMSGTLLGMPVVVSAFEFSFMGGSMGAIVGERFVRAANYALEKRCPMICFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFISVLTDPVYGGVSASLAMLGDVIVAEPKALVGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDMIISRQELRPRLGNLLAQLMGLPTPEFVAAPVEPIVVPPAPANL
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCDAVLYRPELEKTLDVCPKCNHHMRIGARARLDIFLDQDGREEIGADLEPVDRLKFRDSKKYKDRLAAAQKQTGEKDALIAMSGTLEGMPIAVCAFEFSFMGGSMGAIVGERFVQAANVALEQRCPLVCFSASGGARMQEALISLMQMAKTSAALARLREEGLPFISVLTDPVYGGVSASLAMLGDVIVAEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDMIIPRNELRPRLARLLAQLMNRPSPVALPVTA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCNHHMRIGARARIDIFLDAEGRAELGADLEPVDRLKFRDGKKYKDRLTAAQKQTGEKDALISMSGTLMGMPIVVSAFEFSFMGGSMGAIVGERFVRAANYALENRCPMVCFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFISVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDLIISRGELRPRLARLLAQMTGQQTPEEAREAAAVA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCNHHMRIGARARIDIFLDAEGRTELGADLEPVDRLKFRDGKKYKDRLVAAQKQTGEKDALVSMSGTLLGMPVVVSAFEFSFMGGSMGAIVGERFVRAANYALENRCPMVCFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFISVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDLIIDRRELRPRLGNLLAQLTGKPTPKFVAAPIEPIVVPPVPANV
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCNHHMRIGARARIDIFLDAEGRAELGADLEPVDRLKFRDGKKYKDRLTGAQKQTGEKDALISMSGTLMGMPIVVSAFEFSFMGGSMGAIVGERFVRAANYALEHRCPMVCFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFISVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDLIISRGELRPRLARLLAQMTGQDTPEQAREAAAVA
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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. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.
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MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCEAVLYRPELEKTLDVCPKCNHHMRIGARARIDIFLDAEGRAELGADLEPVDRLKFRDGKKYKDRLTAAQKQTGEKDALISMSGTLMGMPIVVSAFEFSFMGGSMGAIVGERFVRAANYALENRCPMVCFSASGGARMQEALISLMQMAKTSAVLARLREEGIPFISVLTDPVYGGVSASLAMLGDVIVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDLIISRGELRPRLARLLAQMTGQQTPEEAREAAAVA
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. Belongs to the Ni-containing carbon monoxide dehydrogenase family. This protein lacks several conserved Cys residues that bind [4Fe-4S] clusters in other CODHs. Therefore, it is not clear whether this protein is active. However, the protein would be able to bind a [Ni-4Fe-4S] cluster, which is the active site of CO oxidation.
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MGIEWEGVKVEIGELVVEGDSESEMEGPTRRELLPWDRTLASVYDLAVVPGDSEEERREVARTIVTLCCEGTAGLISTARLVVELLRQTGENLDPGFDAETPLPLYETLLGSSPECADDLEAGLSYAERELTSSVSELLRSHSLKGYESVAMHAGAIGLLAMEIADATPSTLMEVTESEEVFEIGTDDLPRRPTVLLVGHLPLLGHIITEELGTLARQVELVGLTHTAWPNREDHVRVVGPLSMYHEYLSSGFADVVVVDGACPGEDVIEAAREGGSKLVATVGARVADLLDVTDYPVEEAVEVLVTEEDAVYVEEPIKAVEIAAWAALRVEGSRDRREPPRRAFRVGPPTRLTDVVIRNVGVPVVAGNIPGIVVLVSCPEKSADVEEPAKIAEVLLERGYLVLVPGCLAVALGSYLDDDGKTLYERYPDTLLNTGPCTSAAHLVGACIRVGVIFGKLPIRGEFVRVADYVLNRVGACVIAWGGEYSEHLVSAAYGVTRWGIPVVLGPDPEAGSLLVEKNPKVIDACSGEEVEDPTPEHLRCVVSDWKEAAITAARLCMRPNDTPEGRQNKVESYVELYRELYGELPPDLDLLIRDESDIPVTLRSEIRELLEETGWTPRSRASDPTLLPEG
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 7 [4Fe-4S] clusters per heterotetramer. Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. One-carbon metabolism; methanogenesis from acetate. Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8). Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. Belongs to the Ni-containing carbon monoxide dehydrogenase family.
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MSKLTTGSFSIEDLESVQITINNIVGAAKEAAEEKAKELVKAGPTLFPGLESYRDDWNFKLLDRYEPVVTPMCDQCCYCTYGPCDLSGNKRGACGIDMMGHNGREFFLRVITGTACHAAHGRHLLDHLIETFGEDLPLNLGQSNVLTPNITISTGLSPKNLGEVKPAMEFVEEQLTQLLATVHAGQESAEIDYDSKALFSGSLDHVGMEISDVVQVAAYDFPKADPEAPLIEIGMGTIDKSKPFLCVIGHNVGGVTYMMDYMEENNLTDKMEIAGLCCTAIDLTRYKEADRRPPYAKVIGSMAKELKVIRSGMPDVIVVDEQCVRGDIVPEAQKLKIPVIASNAKIMFGLPNRTDADVNETIEELKSGAIPGCVMLDYEKLGELCIRLTMEMAPIRDASGITAIPTDEELANWVAKCADCGACLIACPEELDIPEAMGFAKEGDYSYLEGLHDICIGCRRCEQVCKKEIPILNIIEKVSQKQIAEEKGWMRAGRGQVSDAEIRAEGLNLVMGTTPGIIAIIGCPNYAEGTKDVYYIAEEFLKRNFIVVTTGCGAMDIGMFKDDDGKTLYERYPGGFQCGGLVNIGSCVSNAHITGAAEKVAAIFAQRTLEGNLAEIADYILNRVGACGLAWGAFSQKASSIGTGCNILGIPAVLGPHSSKYRRALIAKTYEEDKWKVYDARNGQEMPIPPAPEFLLTTAETWQEAIPMMAKACIRPSDNSMGRAIKLTHWMELHKKYLGGSEPEDWWKFVRNEADLPLANREALLKKLEAERGWEIDWKKKKIISGPKIKFDVSAQPTNLKRLCKEA
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 7 [4Fe-4S] clusters per heterotetramer. Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. One-carbon metabolism; methanogenesis from acetate. Heterotetramer of two alpha and two epsilon subunits (PubMed:10600570, PubMed:12657792). The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity). Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. Belongs to the Ni-containing carbon monoxide dehydrogenase family.
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MAKLTTGSFSIEDLESVQITINNIVGAAKEAAEKAEEELGPMGPTPFPTAATVRDWSFTLFDRYEPVYTPMCDQCCYCTFGPCNLEGNRRGACGLDMKGQAAREFFLRCITGCACHSAHGRHLLDHIISIFGEDMPINMGASNVIAPNIQLITGRQPKTLGDLKPIMEYVEEELGQLLATVHAGQEGAAIDYDNKAMLAGILDHVGMEVSDIAQVTALGFPKSDPEAPLVEVGMGTLDASKPVIIAIGHNVAGVTYIMDYMEDNNLTDKMEIGGLCCTAFDMTRYKREDRKPPYAKIVGTISKELKVVRSGIPDVIVIDEQCVRADLVEEGKKLKIPVIASNEKVMYGLPDRTNDDVDAIIEDIKTGKIPGCVMLDYEKLGELVPRLAMEMAPLREGISAIPSDEEMASLVAKCVACGECALACPEELDIPDAIQAAKEGDFTALDFLHDLCVGCRRCEQVCNKEIPILSVIDKAAQKAIAEEKGLVRAGRGQVSDAEIRAEGLNLVMGTTPGVIAIIGCANYPAGSKDVYRIAEEFLNRNYIVAVSGCSAMDIGMYKDADGKTLYERFPGRFERGNILNTGSCVSNSHISGTCHKVAAIFAGRNLSGNLAEIADYTLNRVGAVGLAWGAYSQKAAAIGTGCNMYGIPAVLGPHSGKYRRALIAKTYDENKWKVYDSRNGSELDIPPSPEFLITTAETWQEACVLLAKNCIRPSDNNMGRSIKLTHWIELSEKYLGVLPEDWWKFVRHEADLPLSRREELLKKLETEHGWEIDWKKKKIISGPKIKFDVSSQPTNLKRLCKEA
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Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as phenylacetyl-CoA, indoleacetyl-CoA and isobutyryl-CoA, but not succinyl-CoA. Seems to be involved primarily in the degradation of aryl-CoA esters to the corresponding acids. Participates in the conversion of acetyl-CoA to acetate and in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. acetate + ATP + CoA = acetyl-CoA + ADP + phosphate kcat is 115 sec(-1) for ADP. kcat is 21 sec(-1) for GDP. kcat is 117 sec(-1) for phosphate. kcat is 42 sec(-1) for acetyl-CoA. kcat is 8 sec(-1) for isobutyryl-CoA. kcat is 138 sec(-1) for phenylacetyl-CoA. kcat is 68 sec(-1) for ATP. kcat is 27 sec(-1) for GTP. kcat is 70 sec(-1) for CoA. kcat is 67 sec(-1) for acetate. kcat is 22 sec(-1) for isobutyrate. kcat is 66 sec(-1) for indoleacetate. kcat is 89 sec(-1) for phenylacetate. Optimum pH is 9.0 (at 80 degrees Celsius). Optimum temperature is above 90 degrees Celsius (at pH 8.0). Heterotetramer of two alpha and two beta subunits. Belongs to the acetate CoA ligase alpha subunit family.
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MLDYFFNPRGIAVIGASNDPKKLGYEVFKNLKEYQGGKVYPVNVREEEVQGVKAYKSVKEIPGEVDLAIIVVPKKFVKQTLIECGEKGVKGVVIITAGFGETGEEGKREEKELVEIAHKYGMRIIGPNCVGIMNTHANLNATFITVAKKGNVAFISQSGALGAGIVYKTIKEDIGFSKFISVGNMADLDFADLMEYLADTQEDKAIALYIEGIKDGRRFIEVAKKVTKKKPVIALKAGKSESGSRAAASHTGSLAGSWKIYEAAFKQSGVLVANTIDEMLSMARAFTQPLPKGNRVAIMTNAGGPGVLTADEIDKRGLKLANLEEKTIEELRSFLPPMAAVKNPVDMIASARGEDYYRTAKLLLQDPNVDILIAICVVPTFAGMTPTEHAEGIIRAVKEVNNGKPVLALFMAGYVSEKAKELLEKNGIPTYERPEDVAAAAYALVQQAKNVGGGVNG
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 7 [4Fe-4S] clusters per heterotetramer. Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. One-carbon metabolism; methanogenesis from acetate. Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8). Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. Belongs to the Ni-containing carbon monoxide dehydrogenase family.
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MSKLTTGSFSIEDLESVQITINNIVGAAKEAAEEKAKELGPMGPTAMAGLASYRSWNLLLLDRYEPVLTPMCDQCCYCTYGPCDLSGNKRGACGIDMAGQTGREFFLRVITGTACHAAHGRHLLDHVIEVFGEDLPLNLGESNVLTPNVTICTGLSPKTLGECRAPMEYVEEQLTQLLATIHAGQESAEIDYDSKALFSGSLDHVGMEVSDIAQVSAYDFPKADPEAPLIEIGMGSIDKSKPLIVAIGHNVAGVTYIMDYMEENNLTDKMEIAGLCCTAFDMTRYKEADRRAPYAKIVGSLAKELKVIRSGMPDVIVVDEQCVRGDVLSESMKLKIPVIASNEKIMMGLPDRTDADVDSIVEEIKSGAIPGCVMLDYDKLGELIPKIAEVMAPIRDAEGITAIPTDEEFKVYIDKCVKCGECMLACPEELDIPEALEYAAKGSYEYLEALHDVCIGCRRCEQVCKKEIPILNVLEKAAQKSISEEKGWVRSGRGQASDAEIRAEGLNLVMGTTPGIIAIIGCPNYPAGTKDVYNIAEEFLKRNYLVVVSGCSAMDIGMYKDDDGKTLYERYPGTFSGGGLLNTGSCVSNAHITGAAEKVAGIFAQRTLAGNLAEVADYTLNRVGACGLAWGAYSQKAASIGTGCNIYGIPAVLGPHSSKYRRALIAKTYEEDKWKVFDARDGSEMNIPPAPEFLLTTAETWQEALPMMAKACIRPSDNNMGRSIKLTHWMELSKKYLGVEPEDWWKFVRNEADLPLAKREELLKRLEAEQGWEIDWKRKKIISGPKIKFDVSAQPTNLKRLCKEA
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Catalyzes the deacetylation of N-acetyl-L-citrulline to produce L-citrulline. This is a step in an alternative arginine biosynthesis pathway (PubMed:16585758, PubMed:16511126). Is also able to catalyze the deacetylation of N-acetylornithine in vitro, with almost equal velocity. However, this reaction may be not relevant in vivo since Xanthomonas does not possess the canonical argF gene and cannot convert ornithine to citrulline via ArgF' (PubMed:16585758). H2O + N(2)-acetyl-L-citrulline = acetate + L-citrulline H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine Binds 1 Co(2+) ion per subunit. Amino-acid biosynthesis; L-arginine biosynthesis. Forms homodimers in the crystal, but higher order oligomers may form in solution. Consists of two domains, a catalytic domain (formed by residues 1-166 and 286-365 from the N and C termini, respectively) and a dimerization domain (residues 167-285). Belongs to the peptidase M20A family. N-acetylcitrulline deacetylase subfamily.
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MTDLLASTLEHLETLVSFDTRNPPRAIAAEGGIFDYLRAQLPGFQVEVIDHGDGAVSLYAVRGTPKYLFNVHLDTVPDSPHWSADPHVMRRTEDRVIGLGVCDIKGAAAALVAAANAGDGDAAFLFSSDEEANDPRCIAAFLARGLPYDAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQDPAASALHQAMRWGGKALDHVESLAHARFGGLTGLRFNIGRVDGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFADPAAAHFEETFRGPSLPSGDIARAEERRLAARDVADALDLPIGNAVDFWTEASLFSAGGYTALVYGPGDIAQAHTADEFVTLAQLQRYVESVNRIINGSH
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Involved in the degradation of long-chain fatty acids. A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2 Lipid metabolism; fatty acid beta-oxidation. Repressed by FadR in the absence of LCFAs (fatty acids of 14-20 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs, which antagonize FadR as to its binding to fadR boxes on target DNA and thus derepress transcription. Belongs to the acyl-CoA dehydrogenase family.
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MNFSLSEEHEMIRKLVRDFAKHEVAPTAAERDEQERFDRELFREMANLGLTGIPWPEDYGGIGSDYLAYVIAVEELSKVCASTGVTLSAHISLCSWPLFAFGTEEQKTEYLTQLALGEKIGAFALTEAGSGSDAGSMKTTAERIGDDYVLNGSKVFITNGGVADIYIVFAVTDPEKKKKGVTAFIVEKDFEGFFTGKKEKKLGIRSSPTTEIMFEDCVVPASKRLGEEGEGFKIAMKTLDGGRNGIAAQAVGIAQGALDAALQYAKERKQFGKSIAEQQGIAFKLADMATMIEASRLLTYQAAWLESSGLPYGKASAMSKLMAGDTAMKVTTEAVQIFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLAD
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Essential for the reductive metabolism of L-phenylalanine, L-tyrosine and L-tryptophan (PubMed:29168502). Catalyzes the reduction of phenylacrylic acid to phenylpropionic acid, 4-hydroxy-phenylacrylic acid to 4-hydroxy-phenylpropionic acid, and indoleacrylic acid to indolepropionic acid (PubMed:29168502). 3-phenylpropanoate + H(+) + oxidized [electron-transfer flavoprotein] = (E)-cinnamate + reduced [electron-transfer flavoprotein] H(+) + oxidized [electron-transfer flavoprotein] + phloretate = (E)-4-coumarate + reduced [electron-transfer flavoprotein] 3-(1H-indol-3-yl)propanoate + H(+) + oxidized [electron-transfer flavoprotein] = (E)-3-(indol-3-yl)acrylate + reduced [electron-transfer flavoprotein] Amino-acid degradation. Mutants are deficient in reductive metabolism of phenylalanine, tyrosine and tryptophan, and exhibit growth defects when cultured with amino acids as the sole carbon source. Belongs to the acyl-CoA dehydrogenase family.
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MFFTEQHELIRKLARDFAEQEIEPIADEVDKTAEFPKEIVKKMAQNGFFGIKMPKEYGGAGADNRAYVTIMEEISRASGVAGIYLSSPNSLLGTPFLLVGTDEQKEKYLKPMIRGEKTLAFALTEPGAGSDAGAVATTAREEGDYYILNGRKTFITGAPISDNIIVFAKTDMSKGTKGITTFIVDSKQEGVSFGKPEDKMGMIGCPTSDIILENVKVHKSDILGELNKGFITAMKTLSVGRIGVAAQALGIAQAAVDEAVKYAKQRKQFNRPIAKFQAIQFKLANMETKLNAAKLLVYNAAYKMDCGEKADKEASMAKYFAAESAIQIVNDALQIHGGYGYIKDYKIERLYRDVRVIAIYEGTSEVQQMVIASNLLK
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 7 [4Fe-4S] clusters per heterotetramer. Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. One-carbon metabolism; methanogenesis from acetate. Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8). Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. Belongs to the Ni-containing carbon monoxide dehydrogenase family.
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MSELTTGRFSISDLDNVQITINNIVGAIEKQSDDIDVEMGPTVKPGVSSLRDWDHNILDRYNPVYTPMCDQCCYCTFGPCDLSGNKEGACGINLEGHNAREFMLRVITGAAAHSGHGRHLLHHLIGLYGKDHPLDVGATNIIAPNVQLVTGVQPKTLGDLDSVLSYVEEQITQLLAAIHVGQEGAAIDFESKALHGGMIDHVGMEISDIAQISCLDFPKSDEEAPLADIGMGCLDASKPTLIVIGHNVAAVTDIIDYMEDKGLNDKIELGGLCCTALDMTRYKTGDRTLPRAKVVGTLAKELKTIRSGIPDVIIVDEQCIRADVLKEASKLMIPVITTNDKVMYGLKDRSNDSIEDILEDLTTGKEKGALMFDYVKLGELAPRLTMMMSEIRKQKGIKALPTDEELKELADSCVHCLKCEVACPNSLPISEAMTALSEGDLSKFELLHDKCIACGRCEYACPKDIDIVNVIEKSSQRVISEEVGKVRVGRGPISDPEIREEGVNLVLGTTPGIVALVGCSNYPDGTKDLFTIADEMLRRSYIVVVSGCSAMDLGMYKGEDGLTLYEKYPSRFKSGGLLNTGSCVSNAHITGAVIKVASIFAQKNISGNYEEIADYTLNRVGAVGVAWGAYSQKAASIGTGCSRLGIPVILGPHGSKYRRALIAKPYEEEKWKVYDARNGSEMQIPAAPDYLLTTAETVEEMMPMLAKSCIRPSDNNMGRMIKLTHYMELSQKYLGIMPEDWYKFVRTETDLPLAKREKLLKILEEEHGWEIDWKRKKILSGPTMKSDVSAQPTNLKRLCKEA
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 7 [4Fe-4S] clusters per heterotetramer. Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8). Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. Belongs to the Ni-containing carbon monoxide dehydrogenase family.
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MVMGNNVEMDIKKLLTPLVKMKNANISMSIKFGEEEEEEWEPMGPTPMPKIPTLRHWDFKLLERYPPFYMPICDLCCLCTFGKCDLSRGKKGACGLNIKAQQARIVLIACCIGAACHAGHSRHLVHHLIETLGRDYPIDLGNEIEVEAPIARTVTGIKPKTLGDLEKILDYCEEQITHLLSAAHTGQEGDYLDFESKALHAGMIDDLAREAGDLAQIVAYNMPKGDEDAPLIELGFGCIDKSKPVILCIGHNVVPGSYILEYLEENSMEDEVEVCGICCTAIDITRVSDKPKVVGPLSRQLMFVRSGVADVVIVDEQCIRTDILEEVLKTGAVLIATNEKMCLGLEDVSHMDEDEIIGYLLRNRAALLLDEKKVGKVAVEVAKIVAKERKDRKTLPDLNEVVELAKQCTECGWCNRNCPNAFKVKEAMALAKQGNFKGFIDLYKRCYGCGRCEAICPRNLPIVSMTTKVGEAYYKDLKFKMRAGRGPIKDVEIRSVGAPIVFGDIPGVVALVGCSNHPNGEEEVAMIAKEFLERKYIVVATGCAAMAIGMWKDKDGKTLYEKYPGEFRAGGLVNCGSCLSNCHITGAAIKIANIFAKVPLRGNYAEVADYILNKVGAVGVAWGAMSQKAAAIATGVNRWGIPVILGPHGAKYRRLYLSNGEKFKVKDKKTGEILEIEPAPEHLIVTAENVKECICMIPKLCMRPNDTPKGRANKIYHYVDVYEKYFGRMPPDLEKFVRTEKDIPFMMKDKIMAYLEEKGWKPLEKYPQDPTILY
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 6 [4Fe-4S] clusters per heterotetramer. Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8). Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. Belongs to the Ni-containing carbon monoxide dehydrogenase family. This protein lacks the conserved Cys in positions 52 and 56; they are replaced by an Asp and a Thr, respectively. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form heterotetramers.
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MKNVQINIGAVVKEEDEWDQEMGPFPKPGVATLRDWDFKICNRYKIMYSPADDTCTLCTYGPCDLTGNKKGACGIDMAAACGKIVLVAVLMGTCAHTAHGRHLYHWCLDKFGDMPFDMGSEILVDAPLYRTILGKKPKSLKDFGEALEYCEEEIVQLLAACHTGQEGHYMDFESKSLHSGMIDSLGKEICDMLQTVAYDMPRGAADAPLVEIGMGTLDQNKGVLIAYGHNLAAGAEAMIYTEEHNLWDKVDIGGVCCTAIDLTRITETGRESKIPANLGPKAKVAGAMGWWRKMVRAGIMDTVIVDEQCVFCDVLEDCQQRHIPVIASNDKIMLGLPDRTNDSADAIVEDLVSFKMPGVAILDPVKAGEVAIRTAVAVKPKREQYKKESLFTEQQFKDTLATCTECNQCAFVCPPHIRISEMISEALKGNLEPFSSTYEVCVGCQRCEQTCPQEIPILKLYEYANREYIRNQKFKMRAGRGPVLDTEIRKVGAPLVLGQIPGVIALVGCSNYPNGTKECYDIAKEFVDRGYIVVATGCMAMDMSLYKDEDGKTIWEQYEGAFDGRNICNIGSCVANAHIHGAAIKVATIFAHRNERANYDDIADYIMSKVGACGVAWGAYSQKAASIATGVNRIGIPVVVQPSSVIYRRTFMGRTDKPEDWMVIDAKNGNMQQIEPAPEAMLYIAETKEEAMLEMAKLCFRPSDNTQGRGIKLTHYCDISMKYFGKLPDDWHLFVRDVKDLPLNYQTQMMKELEEKHGWKIDWKAKKFISGPLRPADVSFDPTNIPRKIRAKK
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Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 7 [4Fe-4S] clusters per heterotetramer. Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8). Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. Belongs to the Ni-containing carbon monoxide dehydrogenase family.
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MIDVAPESKKAKDLKGDFWDAKNIQISIGEIITEEKPPEEEVKGPKPRPHVTDLRSWDMKLLERYEPFYAPFCDMCCLCTYGKCELLGKKGACGIDAATQQARTVLLACLIGTAAHAGHARHLVDHLIERLGEDYKIDLGSNVDIEAPITRTVMGKRPATLGDLREVMDYAEEQMSHLLSACHTGQEGDSKDFESKAFHAGLMDDLTREVADLAQIVALDLPKGDEDAPLVELGFGTIDTEKPVVLCIGHNVLPGADIVDYLDENEMEDQVEVCGICCAAIDVTRYNEAAKVVGPLSKQLRFIRSGVADVIVVDEQCVRTDVLEEALKNRSAVIATTDKMCLGLPDMTDEDPDKIVNDLINGNIEGALILDPEKVGEVAVKTAMKLAPIRKSLKKLPDIDEIIELASECTDCGWCQRVCPNSLPVMDAVKKAADGDLSKLEEMAIEELCYTCGRCEQECERNIPIVSMVTKAGERRVKDEKYRIRAGRGPAQDVEIRRVGAPIVLGDIPGVVAFVGCSNYPEGGKDVALMAKEFLERNYIVVTTGCGAMSIGEYRDEDGQTLYEKYGGQFDAKGLVNMGSCVSNAHVSGAAIKIANIFAQKPLEGNFEEIADYILNRVGACGVAWGAYSQKAAAIATGVNRWGIPVVLGPHGSKYRRLFLGRADDEEKWKLKDLRTGEVIDGEPAPEHLLYAAENREEATVMIAKLCIRPTDTPKGRQMKLSNYIDLHRKYLGTIPDDIDRFIRTEKDIPIVYKRDVMKILEEKNWKPRELPKEPSLLER
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Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein] Binds 1 [Ni-Fe-S] cluster. One-carbon metabolism; methanogenesis from acetate. Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). Belongs to the CdhC family.
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MVEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAKPMDEIEDDKVTIVGPDLKEMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGQAVMMLFKTELPFIEKMQVTFYTEQAEVEKQMETAKEIFKARDERTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRVSLCGAINWFDGRAAAKVDPEGPQFEIAKGDLLDANTGEYTGVNDIAKKLSAGEFDKIKLHSFFDSPHTSCGCFEVVGFYIPEVDGIGWVNREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGINYFYSPKFIQADGGWNRVVWLPSMLKDKIIDTIPEDLKDKIATENDSTDIESLKAFLQEKGHPVVATWAAEEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDKMIISEKKEKK
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Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein] Binds 1 [Ni-Fe-S] cluster. Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). Belongs to the CdhC family.
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MKIRLYGETMVVGNIIEGGKTVLNLTKEILEKEDENLKVSYPGTNYNLPIIYGLLGKKIETVKDLKELINSLEIKDEETLENALDAGVVTLICAEAIEALKYAKSEKPYKEPYVGFIPDEILRGLGVPLVEGKIPAILVVIGKVGDKEKLKKLIDDIKKRNILALLVGDIVKEMDEADIEYGLDKLLVPVGNEITSAIHAANLAIRAPLIFGGIEPGKTEEIIDYLKNRVPAVVVALGELDNITLAAGAGCIKAGVPVITNNEVPVIKGALESSDIDNIVENALKMKGVKVKVVEFDIPVSVGPMNEGERVRGPDMYVELAGPKSYGFELVKVVNKAEDKVEIIGKDIDEMEEGSRNPFAIIVEVSGSNLEEDLEGVLERRIHEFLNYIEGVMHLNQRDQVWIRINKNSFNKGLRLKHIGEVVKQLFKEHFPIVEKCNVIIITDPDKVKEELEKAKEIYKKRDEKTKSIREEDVDVFYGCVMCQSFAPTHVCIITPDRPSLCGSINYLDARAAAKIDPNGPIFEIPKGECLDEKLGIYTGVNEVVRERSQGSVEEMALHSALTNPCTSCGCFEAIVFYIPEVDGFGVAHRNFRGETPFGLPFSTLAGQCSGGKQVPGFVGISISYMKSPKFLQGDGGWERVVWLPKELKERVKDAIPEELYDKIATEEDVKTTDELIKFLKEKGHPIVKKTEEEVVEEVEEEKEEVKATEEEKEGIEVGELITKLAKEGGIQIIMKNVKIVINLNVKR
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Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein] Binds 1 [Ni-Fe-S] cluster. One-carbon metabolism; methanogenesis from acetate. Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). Belongs to the CdhC family.
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MAEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAADMDAIEDDKVTIIGPDLKDMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTDKDEVEKQMETAKEIFKARDARTKDLHDEDVEVFYGCTLCQSFAPTNVCVVSPDRISLCGAINWFDGRAAAKVDPEGPQFEIAKGDLLDAVTGEYTGVNEIAKKLSSGEFDKIKLHSFFDSPHTSCGCFEVVGFYIPEVDGIGWVDREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGVNYFYSPKFIQADGGWNRVVWLPSKLKEKIDEAIPADLKDKIATENDASDIESLKAFLQEKNHPVVATWAAAEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDRMIISEKKEKK
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Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein] Binds 1 [Ni-Fe-S] cluster. One-carbon metabolism; methanogenesis from acetate. Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). Belongs to the CdhC family.
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MAEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAADMDAIEDDKVTIVGPDLKDMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAGKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTGKEEVEKQMELAKEIFKARDARTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRISLCGAINWFDGRAAAKVDPEGPQFEIAKGDLLDAVTGEYTGVNEIAKKLSSGEFDKIKLHSFFDSPHTSCGCFEVVGFYIPEVDGIGWVDREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGVNYFYSPKFIQADGGWNRVVWLPSGLKAKIDEAIPADLKDKIATENDATDIASLKDFLEAKNHPVVATWAAAEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSGGGIKLTFKNAKITIDKLVISEKKEKK
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Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-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. acetate + ATP + CoA = acetyl-CoA + ADP + phosphate Activity is dependent on magnesium. kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1) for CoA. kcat is 65 sec(-1) for acetate. kcat is 55 sec(-1) for isobutyrate. Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684). Optimum pH is 7.0 (at 55 degrees Celsius) (PubMed:9119024). Optimum temperature is above 90 degrees Celsius. Heterotetramer of two alpha and two beta subunits. Belongs to the acetate CoA ligase beta subunit family.
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MDRVAKAREIIEKAKAENRPLVEPEAKEILKLYGIPVPEFKVARNEEEAVKFSGEIGYPVVMKIVSPQIIHKSDAGGVKINIKNDEEAREAFRTIMQNARNYKPDADLWGVIIYRMLPLGREVIVGMIRDPQFGPAVMFGLGGIFVEILKDVSFRVAPITKEDALEMIREIKAYPILAGARGEKPVNIEALADIIVKVGELALELPEIKEIDINPIFAYEDSAIAVDARMIL
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Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein] Binds 1 [Ni-Fe-S] cluster. One-carbon metabolism; methanogenesis from acetate. Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). Belongs to the CdhC family.
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MAEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAKPMDEIEDDKVTIVGPDLKEMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGQAVMMLFKTELPFIEKMQVTFYTEQAEVEKQLEEAKAIFKARDERTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRVSLCGAINWFDGRAAAKVDPEGPQFEITKGDLIDAEKGEYTGVNDIAKKLSAGEFDKIKLHSFFDAPHTSCGCFEVVGFYIPEVDGIGWVNREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGINYFYSPKFIQADGGWNRVVWLPSMLKDKIAETIPEDLKDKIATENDATDIESLKAFLQEKGHPVVATWAAAEEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDKMIISEKKEKK
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Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein] Binds 1 [Ni-Fe-S] cluster. Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). Belongs to the CdhC family.
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MFDDIPVSVGPMNEGERVRGPDMYVELAGPKSYGFELVKVVNKAEDKVEIIGKDIDEMEEGSRNPFAIIVEVSGSNLEEDLEGVLERRIHEFLNYIEGVMHLNQRDQVWIRINKDSFNKGLRLKHIGKVVQRLFKAEFPFIEKCDVTIITDPEKVKEELEKAREIYNKRDEKTKALHEEDVDVFYGCVMCQSFAPTHVCVITPDRPALCGGINYLDARAAAKIDPNGPIFEIPKGECLDEKLGIYSGVNEVVRERSQGTVEEVTLHSALEKPCTSCGCFEAIVFYIPEVDGFGIAHRGYKGETPMGIPFSTLAGQCSGGKQVPGFVGISISYMKSPKFLQGDGGWERVVWLPKELKERVKDAIPEELYDKIATEEDVKTTDELIKFLKEKGHPCAERIGAEVEEEAIEEEEVEEEMEEVEGIEVPTMTLPGTFAGLPPGIKIVLYNAVIKAEKIIITKEEPEKKKKKKK
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Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein] Binds 1 [Ni-Fe-S] cluster. One-carbon metabolism; methanogenesis from acetate. Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). Belongs to the CdhC family.
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MADEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAADMDAIEDDKVTIIGPDLKDMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTDKDEVEKQMETAKEIFKARDARTKDLHDEDVEVFYGCTLCQSFAPTNVCVVSPDRISLCGAINWFDGRAAAKVDPEGPQFEIAKGDLIDAVTGEYTGVNEIAKKLSSGEFDKIKLHSFFDCPHTSCGCFEVVGFYIPEVDGIGWVDREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGVNYFYSPKFIQADGGWNRVVWLPSKLKEKIDEAIPADLKDKIATENDASDIESLKAFLQEKNHPVVATWAAAEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDRMIISEKKEKK
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Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate Organic acid metabolism; propanoate degradation. Impairs growth with propionate as the sole carbon and energy source. Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
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MLRSIPRRVPRRLPIFTTTATAGGPSRLAQRAFTCGYLRMSPSSLPPVQPPVSSTLPSDSYQLLSTADKAGDAEDALYEQQIKDVEAWWNSPRFEGIKRPYSAADVVSKRGSLQQTYPSSLMARKLFNLLNERAAENKPVHTMGAIDPVQMTQQAPNQEVLYVSGWACSSVLTTTNEVSPDFGDYPYNTVPNQVQRLFKAQQLHDRKHWDARRKMTPEQRKSTPYIDYMRPIIADGDTGHGGLTAVLKLAKLFAENGAAAVHFEDQMHGGKKCGHLAGKVLVPIGEHINRLVATRFQWDMMGVENLVIARTDSESGKLLSSAIDVRDHEFILGVTEESEPLAETLQAMEREGAAPSEIDAFELDWVKRHKLVTFDEAVDAHLEAEGAPQAARDAYKKRVKENPDLSITRRRELANDYTKTPVVWSCDIPRTREGFYHYRAGFPAATKRAKEFGPYADLLWVETGDPNVEKAAKLAGEVRAALPGKKLVYNLSPSFNWMGQGFDEASLKSFIWDLAQHGFVLQLISLAGLHSGATITAELSRAFKDEGMLAYVRLIQAREKELGVDVLTHQKWSGAPYMDGIVGAIQSGSSSSKSMGEGNTEKGEFNPLVF
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Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA. acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+) AceB requires a high salt concentration for activity, the optimum being around 3.0 M KCl. Replacement of KCl by NaCl causes a decrease in activity (about 2-fold). Optimum pH is between 8 and 9. Optimum temperature is between 45 and 65 degrees Celsius. The activity of the enzyme at 80 degrees Celsius is half of the maximum. Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. Homotrimer and homohexamer in equilibrium. Belongs to the HpcH/HpaI aldolase family.
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MTERRHDREFVRTFFTSPTAVEGEDDSAKMLRRAAGLRGMQAPDVWVPDNEDATAPSMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHMLDITDPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAMSVIIESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPTGELPAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGMLGIWSLTPGQVVEANTSPLPPKTGSWLLDADGEEVELASEDGVEAYDGDRLSLEATDGGYELRVGGDARELTADELREELLGLTSYVPSMDDIVDSMEEFEAAKEAGRGAIAMTQSATLRIGGTEIDIEKDRMWDEATYQAAMTPISLFQDVYENRPDQHEELEERYGAGVVERAMEVGL
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Component of the methylcitrate cycle that catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA (By similarity). Plays an important role for growth and development, but also in antagonism, root colonization and induction of defense responses in plants (PubMed:24100269). (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate Organic acid metabolism; propanoate degradation. Abolishes growth and conidial germination when propionate is the sole carbon source. Reduces growth rate and numbers of germinating conidia on butyrate, ethanol, citrate and Tween 20. Leads also to delayed conidial pigmentation when grown on non-fermentable carbon compounds as the sole carbon source. Results in decreased tolerance to osmotic stress, shows reduced in vitro antagonism against Botryotinia fuckeliana, and delays root colonization. Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
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MAASAPSNSLPPADSYQLLPEAQKAGAAEDALYEAQVKEIEEWWASPRFAGIRRPYSAADVASKRGSQHFRYPSSVMATKLFNLIREREAKGEPIHTMGAIDPVQMTQQAPHQEVLYISGWACSSVLTSTNEVSPDFGDYPYNTVPNQVQRLAKAQSMHDRKQWDTRRKMSPDERSKTPYTDYLRPIIADGDTGHGGLSAVLKLAKLFAENGAAAVHFEDQLHGGKKCGHLAGKVLVPTGEHINRLNAARFQWDVMGSENLVIARTDSESGRLISSAIDVRDHEFILGIADPAVEPLAETLQSMEARGATGAEIDVFEAKWVKSSTLVTFDEAAVAHMKKEGVSQAKIDEYLSATALDRDMGISRRRALASQFTETPVYFNWDVPRTREGYYHFRAGMEAATKRALAFAPYADLLWVETGDPNVEVAAKLGRAVRSVNPGKSLVYNLSPSFNWMAHGFSEEGLKSFIWDIAKEGFTLQLISLAGLHSTATITNELAKKFKTDGMKAYVEVVQRREKELGCDVLTHQKWSGASYIDGILGAIQSGNSSSRSMGEGNTEGQFD
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Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate (By similarity). (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate Organic acid metabolism; propanoate degradation. Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
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MTTDMDLEQLEYEKEVEEIEKWWATPKQSQIKRPYTASTVAVLSEVTKAYYPSSQQALKLYDLLREHRNKGTATLTYGVVDPVLASQASKAGLETIFVSGCLCGLSSVDEPGMDHADYPWDTVPKAVDRIFRSQNWHARRQKQFHLMKPAEERKQLPKYDYLLPIIADGDMGFGSVTSTMKMTKRFVESGVAMIHLDDLAIGLKRFTVGQGRTVVPTSEYLRRLTAVRLQFDIMKAETMLLCRCDTDHAEFITSVVDPRDHAYVLGATTKIESLIKALKDAESTGVSMKKARENWIERAKLMTFDEAVKSTATPKEYENYISAISKKPFHSISERQELAEKYLSNEVFFDWELPRSSDGQYFFKPTVQTVIERAIAAAPLGEMTWARMDYPKWQDIKAFHEGVRAVYPDRMFAFGFTGNYDFKAAGFSEEQLRNLTSDMAKLGVCWQVQPYFTCQVLNKASVDYSNIWKKDGIFGYVKTVQEPALKEDVDGFENEWCGTYFADKLLSAAGSSDKTIPY
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Component of the methylcitrate cycle that catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate Inhibited in the presence of NADH and NADPH. When Mg(2+) is present, Cu(2+), Hg(2+) and Zn(2+) inhibit the enzyme activity in some extent. Optimum pH is 7.3-7.8. Optimum temperature is 40 degrees Celsius. Organic acid metabolism; propanoate degradation. Repressed by glucose. Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
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MLRTRFINSVNSARAMSRNINTLSQFPYPTLQQEESFFKSQVEDIEKWWASPRYEGIKRPYTAEKVAIHRGTLPQTYASSVQAEKLFNIFTERGKQGLPVHTTGSVDPVQMTQSAPHQEVVYISGWACSSLLTTTNEVSPDFGDYPYDTVPNQVDRIFRAQGLHDKKAWHEWMSLSHEERVKRDQEGKGRIDYLRPIIADADTGHGGLSAVMKLAKLFAERGAAAIHLEDQLHGGKKCGHLAGKVIVPTGSHISRLNATRMQWDIMGCSNLVIARTDSESAKLLSSAADPSDHEYILGVVKPIKPLAEVLLTAEANGATADMVNKLELEWTKEAEMMTYDEAVQRALTEAGKSDKIEEYLTKAKGKSNFEARQIADELAGKHIFFDWDAPKTREGHYHVQCGIEPAIKRALAFAPYADLIWLETKTPDLAQAQAFAKRIREKFPGKWLVYNLSPSFNWSAHGYSDEQLKSFVWDLAKSGFVMQLISLAGLHSNAVATHELSTRFKTEGMKAYVDLVQRKEKELGCDVLTHQKWSGANYLDSIISTVQSGSSGTSSTGGDSTENQF
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Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate Organic acid metabolism; propanoate degradation. Repressed by glucose and induced by ethanol and threonine. Present with 1084 molecules/cell in log phase SD medium. Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
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MITMINNKTFNRKTTGTLKKLVLSSDKSLRRSFNGASSTKDFVFSESSKVEEWWESARFKNISRPYSATDVVKHRGSLPANTSIYPSSYQARKLFNLLEENFKNGTPLHTLGVIDPVQMSQLARCRNIKVAYISGWACSSTLVGSTNEVSPDFGDYPYDTVPNQVERIFKAQQLHDRKAFLEASIKGSTPVDYLKPIIADADMGHGGPTTVMKVAKLFAEKGAAGIHLEDQMVGGKRCGHLSGAVLVPTATHLMRLISTRFQWDIMGTENLVIARTDSCNGKLLSSSSDPRDHEFIRGIIRDNVVPWSEKLIEMEDKKIPNSAIADMEKEWYHENELFTFEEALEKQFTASEFESYKEKKEDLMVNKLGRAYLSLREMKLLAQEVTPLKKIIFDWDAPRTKEGYYMFNGCIEAAIRRSLVFAPYSDMIWLETKTPDLEQARSFSRKIHKQLPATKLVYNLSPSFNWSAHGFDDKALKSFVWDLAKEGFTLQLVSLAGLHSDGVSFWELANSFQSDGMKAYVEKVQKREKETNCDIMTHQLWSGAEYVDSLMKVVQNGASSQTLSTSGESFTETQF
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MPDTITNKLQNSTVQDVIATKLARAVFAGFEAMFATFLNITLGAQSRFEQRQYHEVQSAMRERLQVYERQVKSVSEAVKVIAYAELSCPQTWQLAKNIYGNMVKNHENEPIAHTFFNSTFGAIWDDKKIRTVHLFVLKAKYRTQPRPYDSLVKRISLQHGFNSAIKTLITNQVFRVPFSNLNQDVATLQATLTQGAKQQCRQVYELINLNDGYIEYAYSHFYRNKACYLIGRCIAKNGDNMPFAIAILNTPKGLKIDAVMMGADQLSLLFGFARTYFMVDTDQPARYVDYLSVLMPHKQRFELFNAIGFIKHAKTEFYRYKVDTTKNSPASFKYVAAPGTPGMVMLVFTIAGSDHVYKVIKDKFSAPKTATKAQVKEKYNFVKQADRVGRLVDTHEFRYLAFDLSRFSEQLLQQMKEHIGSSLIISGKALILKHVYVERKMTPLNLYINDCDSKALAQVMLDYGRAIKDLAGANIFPGDMLMKNFGVTRWGRVVFYDYDEICPLTDCNFREVPQTQNALEELSSDSYFDIEPNDIFPSQFKVFFSANELAFNAFNSHHSDLFNAQFWQTCQQQVQQGYLPDVYPYKQSWRFK
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MQPRHIAELILTGFKKHYLLFQKTTAKAPLAFAKRDWQAINDISRLRISHYDDRVNETTATLRQQQTEQLDEQLWLEVKKLYQHFLCFHPQAELAETFYNSVFCRLYHRRYFHNDFIFVEATLKDAPAVPVEAEYRSYFPVVDGLKPTIKQIINHFDFKAPFVNLERDIRLLVKAFYKQAPDTHHKAWQMRFDILHTPFYRNKAAYIVGRVVSQSGVQPFIIAVLHHEDKGLYLDALLTKSSQMRVIFGFARAYFMVETHAPCALVRFLNQLMPNKTIAELYNAIGFHKQGKTEFYREFLNHLTHSNDEFTIAPGTPGMVMMVFTLPSFGYVFKVIKDKFGESKPFGRDTVLKRYQLVKKHDRVGRMADTIEYSNVVFPLARFDSNLLQQLHQTIGSSMVIEGDWLIIKHLYIERRMTPLNLFLENADDASAADAIEEYGQALKEMIAVNIFPGDMLLKNFGVSKHKRIIFYDYDEVQYLTDMNFRALPKAKTYDDYLMDEQSYSVAPQDVFPEQLCTFVMPNPIYKQFLMSTHPELIDVNFWKQAQQNIKNGQVSHIYPYPTAQRFIHHW
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MFPRRLDSPAAYGIAQAMMDGFDRHYRLFRAESARAKHRFETSDWSGQQRAQRERIEFYDLRVKECVRRLEKEFSAGAQPMDVWHQVKLHYIGLLVGHRQPELAETFFNSVTTKILHRTHFHNDFIFVRPAISTEYLENDEPGARPTYRAYYPTPESLQETLVRVVDNFQLQGEFEDLARDAGRVAEVMRPRLGPAKWRANFQIQVLSSLFYRNKGAYLVGKVINGFQELAFALPILHGTDGRYVIDAALFGEDDLQMLFSFARAYFMVDMEIPSAYVQFLRSLMPRKPRAELYNALGLAKQGKTLFYRDFLHHLRYSSDRFRIAPGIKGMVMLVFDLPSFPFVFKVIKDYYPPQKDTTREQIKGKYLLVKQHDRVGRMADTLEYSEVAFPRERFEDDLIAEIEKFAPSQLEISDRDGDGNVEVILKHVYIERRMIPLNIYLQEAFDAGPHDARARQQMERSVVEYGNAIKDLVAANIFPGDMLWKNFGVTRNGKVVFYDYDEIEYLTDCHFRRVPAPRNEEDELSGEVWWAVGPRDVFPETFGPFLLGNDAVREVFMRHHADLLDPVFWQSHKERIQAGHMYDVFPYDPERRFGAGTGSPA
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MFPERLDAPQAYDIAKAMMDGFNRHYRLFRAESARAKHRFETADWHGQQRAQRERIEFYDLRVRECVRRLDKEFNAGALPMDVWHQIKLHYIGLMVNHLQPELAETFFNSVTTKILHRTHFHNDFIFVRPAVSTEYIESDDPGARPTYRAYYPSRDNLHETVVRIVEHCALQRDFENLPRDAGHVVQALQQRLGAVKLRTNFQVQVLSSLFFRNKGAYLVGKVINGYNELPFALPILHGEDGRLLIDAVLFGENDLQMLFSFARAYFMVDMEIPSAYVQFLRSLMPRKPRAELYTALGLAKQGKTLFYRDFLHHLRYSTDKFRIAPGIKGMVMLVFDLPSFPYVFKLIKDQFPAPKDTTREQVQGKYLLVKQHDRVGRMADTLEYSLVAFPRERFSDELIEEIRRHAPSQIEISDRDGDGRQEVIIAHLYIERRMIPLNIHLQECFDTGLDKPEARSALEHAVTEYGNAIKDMVAANIFPGDMLWKNFGITRNGKVVFYDYDEIEYLTDCNFRRVPPPRCEEDEVSGEVWWPVGPHDVFPETFGPFLLGNDSVREAFMRHHADLLDVEFWQSHKERIQAGHLYDVFPYDSARRFRCASPSSFQTQGDST
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MQQPLEQAVAETILQRFESFYSRFLEITQGSKSRFENSDWLGVQLAGRERIRLYDHHVGATTALIKQMMGATLPSQALLKQVKGAFSDLLPKCENFEVAESFFNSVYRRIFRHRNIRDENLYIHPFRSRGEHPDLSALLRIYRTDLAHLPQTLSQLLGDYSFTLPYEDKQRDIVDIQRHLAENGPAILHDEPFAIELLKEVFYRNKGAYLVGLIRVKGQVFPFILPLLSTGQSIYVDTVIFEPELASIVFGFARAYFMVYAPMPALFVLFLRQIMPHKPDYEIYNAIGCQKHGKTELYRHYQQHLAQSREQFVIAPGIKGMVMSVFTLPSYDVVFKVIKDEFTPPKDVSHEQVKAKYRLVKQHDRVGRMADTQEFTNFEFPLDRISPELLAELKTVAPSALTLTDDKLVIKHLYTERKMIPLNLYLDKADEQQTRLALEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTECNFRQIPPPRYPEDEWSAEPWYSVAPNDIFPEEFATFLLQKPQVRDIMMQLHKELFDANYWKMLQSNIKEGVFEDVYPYRRKKRFKFQRGG
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MQQPLEQAVAETILQRFESFYSRFLEITQGSKSRFENSDWLGVQLAGRERIRLYDHHVGATTALIKQMMGEHHATQELLKRVKGAFSDLLPRCDNFEVAESFFNSVYRRIFRHRNIRDENLYIHPFRSRGEHPDLSALLRVYRTDLTHLPQTLSQMLGDYSFTLPYEDKQRDIVDIHRHLAENGPQILHEEPFAIELLKEVFYRNKGAYLVGLIRVKGQVFPFILPLLSTGQSIYVDTVIFEPELASIVVGFARAYFMVYAPVPALFVVFLRQIMPHKPDYEIYNAIGCQKHGKTELYRHYQQHLAQSREQFVIAPGIKGMVMSVFTLPSYDVVFKVIKDEFTPPKDVSHEQVRAKYRLVKQHDRVGRMADTQEFTNFEFPLDRISPELLAELKTVAPSALTITSDKLVIKHLYTERKMIPLNLYLDKADEQQTRLALEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTECNFRQIPPPRYPEDEWSAEPWYSVAPNDIFPEEFATFLLQKPQVREIMMQLHKEMFDANYWKMLQSNIKVGVFEDVYPYRRKKRFKFQRGG
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MFPTRLDSSLAYDIAKAMMDGFNRHYRLFRTESARAKHRFETADWHGQQRAQRDRIEFYDLRVRECFMRLAREFKADEQPMEVWQQVKLHYIGLLVDHHQPELAETFFNSVTTKILHHSYFQNDFIFVRPAVSTEYIENDESETSPTYRSYYPTHDSLAEVLVQMVLDFDLRCPFADLDSDAARVQAAMVEQLGEVKLRANFQLQVLSGLFFRNKGCYIVGKLINGFNEFPFALPVLYGRAGQLVIDAVLFGEDDLLMLFSFARAYFMVDMEIPSAYVQYLRSMMPRKPRNEIYNALGLAKQGKTLFYRDFLHHQRHSTDKFRIAPGIKGMVMLVFDLPSFPYVFKVIKDFYPPPKDTTREQIKAKYLLVKQHDRVGRMADTLEYSEVGFPRARFDDELIAELEKFAPSQLEISDRDGDGRIEVIIKHVYIERRMIPLNIYLQEAFDAGGANPDDTSPAALRAREQIERGVIEYGNALKDLVAANIFPGDMLWKNFGITRHGKVVFYDYDEIEYITDCNFRKVPQARNEEDEMSGEVWYRVGPKDVFPETFAPFLLGNPFVREVFMKHHAELLDAAFWQSHKERIQAGHVYDVFPYDQGKRFHPEISDAQVPSSI
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MLDERGALARGAAEAIRAGYEAYQAERARITARARGRFEARDWAGAQRDARERLDLRDGVVHRTVGEVRAELGGAVQDREVWRRAKEAFEAVAAARPDAEIAGSFFNSVTRRVLTTVGVDPAIEFLAADAPPPREDPPQHRAFAREATTEALLARILRAAPISAPFEDLARDARLAALELDAHVRGLPDRQPIDAVELARPVFYRGKGAYLVGRIRRGRHLTPLVLALAHGDRGVALDAVLFTEEDVSIVFGFTRSYFHVALERPRAMVAFLSTLLPLKRRSELYTGLGYHKHGKAELYREVAQHLAEGDDRFVPARGDRGLVMCVFTLPGLDVIFKVIRDRFAPPKQTTRREVMDRYRHVFRHDRAGRLVDAQEYEHLAFPAARFSPALLEELRTECGDGVRVAGGEVAIRHLYAERRVTPLNLFVREADEWTARQAVLDFGCALRDLAATDTFPGDLLLKNFGVTRHGRVIFYDYDELTRVTDCNFRDLPGAGPGDGDDGWGGGPDAGYDGGDPPFYVGPADVFPEELLPFLGLTGRLREVFLRAHGELLTGRWWRDIQARLRAGEIVDIFPYREEQRLRHAHP
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MAEPNDVAAAGAAAIAASFEAYQEERARITRRARERFEKRDWAAGQADARERLDLRDRLVNACVGTVRAELGGAAHDHGLWRAMKELYEARVESRPDREIGQSFFNSVTRRVFVTVGVDPAIEFLAADGPAVREGPVPVYARYRREVSTEALLRTVLRACAFAAPYEDLERDARIAAIELDSHLRELDDGQPIEALELVKAVFYRGKGAYLVGRLRRGRYTTPLVLALVHGERGVVLDAILFTQEDVSIVFSFTRSYFHVEVERPRELVAFLSTLLPLKRVSELYIALGFNKHGKTELYREIARHIAETGEAFVPARGDKGLVMSVFTLPGLDVVFKVIKDEFKPPKQTTRREVMDKYRHVFRHDRAGRLVDAQEFEHLAFPADRFSPEVLRELSEECRGSIEIGRAEISVKHLYAERRVTPLNLFIREADEWTARQAVLDFGRALKDLAATNTFPGDLLLKNFGVTRHGRVIFYDYDELTRVTDCVFRDLPTPSGDDEETSGEPWFYVGQDDVFPEELLPFLGLAGRLREVFLQAHGDLLTARYWRAIQERIREGEIVDIYPYREEQRLVHGYE
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MDASVGENPVAQSIAQAMIEGFNKHYRIFRETSRRAKESFEAAEWQAQIDAVRERVQFYDERVDEAVRRLHEEFDADSLDDSTWQQLKLQYIGILMRHKQPELAETFFNSVCCKILHRTYFNNDYLFARPAVSTEYIESYPPVYSSYYPQDEGLRTTVRRIIEDFDWQRPFANLDRDIDNILRAVHEHIGAWPDMEVNCQIQVLYSAFYRNKTAYIIGKAINGYQEYPFALAVRHNPAGRLEADTILLDPWRISVLFSLSRAYFLVDMEVPSGYVHFLRSIMPNKHRSELYTMLGLGKQGKTMFFRDLIAHLRHSNDQFIIAPGIRGLVMLVFTLPSYPYVFKIIKDVFGASKNMDRATVKRKYLMVKQVDRVGRLADTLEFSYAALPLSRFHPELLDELRALAPSSFEIEGDSVIIKHLYIERRMTPLNIYLEHADDDQVEYAVREYGNAIRELATANIFPGDMLWKNFGVTRYGRVVFYDYDEIEFMTAMNFRRIPPAPYPEMEMAAEPWYSAGPMDVFPEEFATFLLGAPRVRKAFLKHHRDLLDAKFWQDVQASIRKGYLEDFFPYPTELRFCNMWSNERGRAHQAA
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MDAQVGDNPVAQAIAHALVEGFNKHYRIFRGTSRRAKEYFEAGDWRAQLDAVRDRVQFYDDRVDETVRRLLEEFDADSLDDATWQQVKLHFIGALINHKQPELAETFFNSVGCKILHRTYFNNDYIFARPAISTEYIESYPPVYSSYYPQDGGLRATIRRIIEDFDWQRPFEDLDRDIDCIMRAALAHLGEWPAMEVNCQLQVLYSAFYRNKTAYIIGKVINGWQDYPFTLAVRHGASGRLVIDTILLDPWRISVLFSLSRAYFMVDMEVPSGYVQFLRSIMPNKPRSELYTMLGLGKQGKTMFFRDLVAHLRHSNDQFIIAPGIRGLVMLVFTLPSYPYVFKIIKDVFGSSKNMDRATVKRKYLMVKQVDRVGRMADTLEFSYAALPLSRFHPELLEELRTLAPSAFEIDGDALVLKHFYIERRMTPLNIHLEKASDGEVEAAVHEYGNAIRELAIANIFPGDMLWKNFGVTRYGRVVFYDYDEIEYMTSMNFRRIPPAPHEDMELSGEPWYSAGPMDVFPEEFATFLLGSPRVRKAFMKYHRDLLEPAFWQAAQQGVRDGHVEDFFPYPAELRFSVMFPATPVAAQD
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MIYSGDVQRIEPAPVAGPAPLDVAHLILAGFDRHYALFRYSAQRAKSLFESGDWHGMQRLSRERIEYYDMRVRECATQLDSALRGSDARTADGSRANGSAALSEAQTAFWQAVKQEFVGLLADHRQPECAETFFNSVSCRILHRDYFHNDFLFVRPAIATDYLDSRIPSYRVYYPVAEGLHKSLIRMVADFGLAVPYADLPRDARLLARAAVRQLRGQLPRHAGPRLASDCQIQVLGSLFFRNTGAYIVGRLINQGTVYPFAVALRRNPAGQVCLDALLLGADDLSTLFSFTRAYFLVDMETPAAVVNFLASLLPRKPKAELYTMLGLQKQGKTLFYRDFLHHLTHSRDAFDIAPGIRGMVMCVFTLPSYPYVFKLIKDRIDKDGMDHATVRRKYQMVKLHDRVGRMADTWEYSQVALPRSRFAPRLLEELRRLVPSLIEENGDTVVIRHVYIERRMMPLNLYLRHASDPLLEVAVREYGDAIRQLATANIFPGDMLYKNFGVTRLGRVVFYDYDEIQRMTEMNFRAIPPAPNEEAELSSEPWYAVGPNDVFPEEFGRFLLGDPRVRQAFLRHHADLLAPQWWQACRARVAQGRIEEFFPYDTDRRLHPQAAPPPRTAA
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MIYSGDVQRIEPAPVAGPAPLDVAHLILAGFDRHYALFRYSAQRAKSLFESGDWHGMQRLSRERIEYYDMRVRECATQLDSALRGSDARTADGSRANGSAALSEAQTAFWQAVKQEFVGLLADHRQPECAETFFNSVSCRILHRDYFHNDFLFVRPAIATDYLDSRIPSYRVYYPVAEGLHKSLIRMVADFGLAVPYADLPRDAGPRLASDCQIQVLGSLFFRNTGAYIVGRLINQGTVYPFAVALRRNPAGQVCLDALLLGTDDLSTLFSFTRAYFLVDMETPAAVVNFLASLLPRKPKAELYTMLGLQKQGKTLFYRDFLHHLTHSRDAFDIAPGIRGMVMCVFTLPSYPYVFKLIKDRIDKDGMDHATVRRKYQMVKLHDRVGRMADTWEYSQVALPRSRFAPRLLEELRRLVPSLIEENGDTVVIRHVYIERRMMPLNLYLRHASDPLLEVAVREYGDAIRQLATANIFPGDMLYKNFGVTRLGRVVFYDYDEIQRMTEMNFRAIPPAPNEEAELSSEPWYAVGPNDVFPEEFGRFLLGDPRVRQAFLRHHADLLAPQWWQACRARVAQGRIEEFFPYDTDRRLHPQAAPPPRAAA
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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. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.
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MNHFPKLLSSQIGFDVAQTMLENFDRHYRIFREAAVDAKTLYERADWHGLQRLARERITSYDDRVQECVEVLQDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFNNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAATLERIVTNFQLEPPFEDLTRDIGCVMQAITDEFGEFDAAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGLLALDTVLLRRDLLQIIFSFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTREQIMEKYQLVKRHDRLGRMADTLEYSSVALPISRLDHALVRELEKEVPSLLEYEDGNLVIKHLYIERRMIPLNLYLQNGTDAEIEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRAVFMKHHADFFEASLWQASKDKLLQGELPDFYPYDVSLRFSVRYPDRFDSTPDAGDGDSAGDAQRAA
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Fibrinolytic activity; shows preferential cleavage of Arg-Gly bonds in all three fibrinogen chains. Contact with the caterpillars causes severe bleeding, due the anticoagulant effect of the protein. Sensitive to serine proteinase inhibitors and thiol proteinase inhibitors. Hemolymph and saliva of the larval form (caterpillar). Belongs to the peptidase S1 family.
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IVGGSTTTIASYPEITALLYFNRQACGGTILNNRSVLTAAHCPFGDAASSWSFRVGSTNANSGGTVHSLSTFIIHPSYNRWTLDNDIAIMRTASNINFINNAVRPGSIAGANYNLADNQVVWAAGWGTTSPGGSLARFPGVNARHVQIWTVNQATCRTRYASIGHTVTDNMLCSGWLDVGGRDQCQGDSGGPLYHNGVVVGVVSRYTAWIQSNA
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Subunit of the non-synaptic neuronal acetylcholine receptor, which may play a role in chemotaxis towards choline. After binding choline or acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane (PubMed:9860996, PubMed:11273652). The functional receptor is a heteromer of deg-3 and des-2. Interacts with ric-3; which is required for proper receptor folding. Enriched in the sensory endings of sensory neurons. This locus is redundant or nonessential as suppression of deg-3 function results in wild-type revertants. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MTLKIRTIIILFCVISVTTTSQSLNATLKTFDPRLLNSTADRDIAMKNVPLVRLTRHLLSPERYDVRVRPILDHKKSLKVHISISLYQIIEVDEPSQNIKLNVWMIQKWRDEYLDWNPNEYGMINSTIIPFHHLWIPDTYLYNSVKMSRDETERYMNIQATSNYWKGEKGAELSFLYPAIYTITCRLNIRFFPYDRQNCTLTISSWTNSKSALDYYADTEVSMQSFIPNEEWQVKSFKIHRHEYKYACCAEPWVILQASLVIQRKPLYYLVNLIIPTSIITLVAITGFFTPASTDDDRTEKINLGITTLLAMSILMLMVSDQMPTTSEFVPLIAWFYLSIIIIISIGTFLTSVVLSVQGRRQYGRNPPQFIRYIFFVLLPQVLLLNVPPPLQTLWGELDDDPLNVRRRKKSHYLSRNVNNGSTKMASPMSTLRVPQSAGSVSEKRQSFQMIDVTSPNSPNTARSRAPSLAPSTAKATMWEGTMSALAGTNTQLRRTSNVFNKEVDEMRRKRQCSLEWEFLATVLDRFLLIVFVGAVVIVTAGLILVGRMAQYSYDHPDDRFFNV
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CNS in embryos. Late embryonic and late pupal stages. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MESSCKSWLLCSILVLVAFSLVSASEDEERLVRDLFRGYNKLIRPVQNMTQKVGVRFGLAFVQLINVNEKNQVMKSNVWLRLVWYDYQLQWDEADYGGIGVLRLPPDKVWKPDIVLFNNADGNYEVRYKSNVLIYPTGEVLWVPPAIYQSSCTIDVTYFPFDQQTCIMKFGSWTFNGDQVSLALYNNKNFVDLSDYWKSGTWDIIEVPAYLNVYEGDSNHPTETDITFYIIIRRKTLFYTVNLILPTVLISFLCVLVFYLPAEAGEKVTLGISILLSLVVFLLLVSKILPPTSLVLPLIAKYLLFTFIMNTVSILVTVIIINWNFRGPRTHRMPMYIRSIFLHYLPAFLFMKRPRKTRLRWMMEMPGMSMPAHPHPSYGSPAELPKHISAIGGKQSKMEVMELSDLHHPNCKINRKVNSGGELGLGDGCRRESESSDSILLSPEASKATEAVEFIAEHLRNEDLYIQTREDWKYVAMVIDRLQLYIFFIVTTAGTVGILMDAPHIFEYVDQDRIIEIYRGK
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Subunit of the non-synaptic neuronal acetylcholine receptor (AChR), which may play a role in chemotaxis towards choline. After binding choline or acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The functional receptor is a heteromer of deg-3 and des-2. Interacts with ric-3; which is required for proper receptor folding. Enriched in the sensory endings of sensory neurons. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MLIIIQSLLLATTASLCIADTPVPTQIRLVHDLLDNYDKKAKPMWDNSKPINVSFSMDLYQILELNEPQQYILLNAWIIERWFDEFLYWNPDDYENITELRLPYDSIWLPDTTLYNSLVMKDDDTRRLLNSKLTTDTHRRAALIELLYPTIYKFSCLLDLRFFPFDVQVCTMTFSSWTYDQKGIDYFPYSDKIGTSNYLENEGWYILQTKIKRQEVKYACCPNNYTLLQLTLYLRRKPLFYLVNLIIPTSIITLIAIVGFFTTSSASGMREEKVSLGITTLLSMSILMLMVSDQMPTTSTFIPLIGWFILAMIIVISLGTVVSSVIIAIQKRGSLGERMSKRALKFAKVLAWFTCTSLPPHVEKEHMMEAFDAPTPLVEVRPLQLASVKESVRNKWVSGARRATQRGNSGLALISDKSTDPLIHLSPTAHQPDESISPSAPPVPSSSPLPPPLTPGPADDVVSVASELSSKFLTSRMRPKSQKDNTFAAMQSSIKANRQLAVAEFEWFATVVERTCFVIFVVAFLIITFGINFIGFIHWHQAGVEYGG
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CNS in embryos. Late embryonic and late pupal stages. Partially edited. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MWHWSLLCVFLLVPLANSTAPISFEANPDTKRLYDDLLSNYNRLIRPVVNNTETLTVWLGLKLSQLIEVNLKNQVMTTNLWVKQRWFDYKLRWDPEEYGGVEQLYVPSEHIWVPDIVLYNNWDGNYEVTLMTKATLKYTGEVFWEPPAIYKSSCEMNVEYFPYDEQICFMKFGSWTYNGAQVDLKHLDQIPGSNLVQVGIDLTEFYLSVEWDILEVPATKNEEYYPDTLEPFSDITFKLTMRRKTLFYTVNLIVPCVALTFLTVLVFYLPSDSGEKVTLCISILVSLTVFFLLLAEIIPPTSLAVPLLGKYLLFTMILVSLSVWTTVCVLNIHFRSPSTHNMSPLVRKLFLHFMPKLMMMRRTQYTLPDYDDSTPSNGYTNEIDVRDSISDFPSEFKDSQDGAYDNGMQNSVDSDNVIPRNLTPEVLQALRAVRFIAQHIKDADKDNEIVEDWKFVSMVLDRFFLWLFTLSCVFGTLAIICQSPSLYDTRSPIDRQLSEIPLRKNNFMLPPDIVRQVLT
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Alpha subunit of nicotinic acetylcholine receptor (nAChR) (PubMed:9221782, PubMed:15990870, PubMed:20027209). Probably acts in cholinergic motoneurons to regulate presynaptic neurotransmitter release, thereby ensuring normal level of excitation of cholinergic motoneurons during locomotion (PubMed:20027209). Involved in nAChR sensitivity to nicotine (PubMed:9221782, PubMed:15990870). Component of nicotinic acetylcholine receptor (PubMed:15990870, PubMed:20027209). In muscles, composed of 2 non-alpha subunits lev-1 and unc-29, and 3 alpha subunits unc-38, unc-63 and lev-8 (PubMed:15990870). In cholinergic motoneurons, composed of 2 non-alpha subunits acr-2 and acr-3, and 3 alpha subunits unc-38, unc-63 and acr-12 (PubMed:20027209). Co-localizes with unc-29 and lev-1 and partially with acr-12 and acr-8 at nerve cord synapses. RNAi-mediated knockdown causes a resistance to nicotine-mediated paralysis. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MRSFWLFLLLLLFCISFIKLTEGNEDAKRLYDDLMVNYNRHRRPSTSPNKPLTIKLKLRLSQIIDVHEIDQIMTCSVWLKQTWIDRKLSWDPVNYGGVNVLYVPYEMIWVPDIVLYNNADSNYNITISTKATLHYTGEVTWEPPAIFKSMCQIDVRWFPFDEQQCHLKFGSWTFSENLLSVELNEPSLRYEEEIDEKGIIDNVTVAEDGIDLSDYYPSVEWDIMSRVAKRRAKNYPSCCPQSAYIDVTYYLQLRRKPLFYTVNLVFPCVGISFLTILVFYLPSDSGEKVTLCISILVALTIFFLLLTEIIPATSITLPLIGKYLLFTMVMVTLSVVVTVISLNLHFRTPTTHLMPNWVKKVFLKWLPKLLFMRRPIDDYEEKFDDKKKPKDGKIALSVHAHRVSNVGNNIRNATIDDTIQKMYYSPPVVKAFENICFIAELLKKKDRDDKIDEDWKYVAMVLDRLFLLIFSIACFVGTVIILLRAPTLYDTRQPIDLQYRPANLSANPISF
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Alpha subunit of nicotinic acetylcholine receptor (nAChR) (PubMed:15280391, PubMed:15990870, PubMed:20027209). Probably acts in cholinergic motoneurons to regulate presynaptic neurotransmitter release, thereby ensuring normal level of excitation of cholinergic motoneurons during locomotion (PubMed:20027209). Involved in nAChR sensitivity to nicotine and levamisole (PubMed:15280391, PubMed:15990870). Component of nicotinic acetylcholine receptor (PubMed:15990870, PubMed:20027209). In muscles, composed of 2 non-alpha subunits lev-1 and unc-29, and 3 alpha subunits unc-38, unc-63 and lev-8 (PubMed:15990870). In cholinergic motoneurons, composed of 2 non-alpha subunits acr-2 and acr-3, and 3 alpha subunits unc-38, unc-63 and acr-12 (PubMed:20027209). Interacts with lev-10 (PubMed:21252855). Expressed in body wall muscles, in vulval muscles and in neurons. RNAi-mediated knockdown causes a resistance to nicotine-mediated paralysis. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MGPNDHGFAYILIFLLLSPPTHANRDANRLFEDLIADYNKLVRPVSENGETLVVTFKLKLSQLLDVHEKNQIMTTNVWLQHSWMDYKLRWDPVEYGGVEVLYVPSDTIWLPDVVLYNNADGNYQVTIMTKAKLTYNGTVEWAPPAIYKSMCQIDVEFFPFDRQQCEMKFGSWTYGGLEVDLQHRDKHLEKEIEEDVEGVDGPTKEIVWVVDRGIDLSDYYPSVEWDILNVPGKRHSKRYPCCESPFIDITYEIHLRRKTLFYTVNLIFPSVGISFLTALVFYLPSDGGEKISLCISILISLTVFFLLLVEIIPSTSLVIPLIGKYLLFTMVLVTLSVVVTVVTLNVHYRSPTTHTMPKWMKRLFVDFLPKYLLMTRPQPPGHHSKPNRKFDSRASTFSIGVNHVLGQNSELLSPGLNSNREESSFTLPRDNSPVRSAVESVAYIADHLKNEEDDKQVIEDWKYISVVMDRIFLITFTFACAFGTVVIIARAPSIYDNTPALA
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Non-alpha subunit of nicotinic acetylcholine receptor (nAChR). Involved in nAChR sensitivity to nicotine. Interacts with unc-29. Component of nicotinic acetylcholine receptor composed of 2 non-alpha subunits lev-1 and unc-29, and 3 alpha subunits unc-38, unc-63 and lev-8. Co-localizes with unc-29 and unc-38 at nerve cord synapses. RNAi-mediated knockdown causes a resistance to nicotine-mediated paralysis. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MMLGGGGGCGAGGTWLGFLVFLAVSLRNHSTCEDIDAEDRLMVDLFRGYNSLVQPVRNRSELPMIVKIGMQLVLLINVDEKEQVMHTNVWLTMKWDDFQLKWDPRDYANITQIRVAPEKVWLPDIVLFNNADGNYEVSFMCNVLILSTGTVLWVPPAIYKSSCIIDVEFFPFDDQLCSLTFGSWTYNRDEIKLDFLTSDRVDFSEYSTSSIWDMMDGPAVLTSDRSRIEFQIRIRRKTLFYTVVLILPTVLMAFLNVTVFYLPTASGEKMGLTMNVLLSIVVFLLLVSKILPPTSSSIPLVAKYLLLTFVLNIITIMVTTIICNIYFRSPITHRLPPWVRKVFLDILPLLMCMQRPHRKNVIQRSHRRLLETGPSVEENPMRSGEHHPLCRHTHNQDSCRRVRIQSDELDDELSPEAQRAIDAIEFITENRRDEEITKQFRDDWKFIASVVDRFLLYGFFGATVGGTIGIIFTAPSVFETFDENATLVKLKQLYDMGLANDTVLGIF
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Nicotinic acetylcholine receptor in the MC pharyngeal motor neuron involved in pharyngeal pumping. Has a role in the determination of life span possibly via calorific restriction which affects growth rate, although this is independent of metabolic activity (By similarity). Neuronal AChR seems to be composed of two different type of subunits: alpha and beta. MC motor neuron. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MFLLLQILYILLFLNLADTSDDEYRLLKDLREGYDPMERPVSDHMKPVNVKLRLILQQLVDVDEKNQVITLVVWTQYTWNDYKMKWSPEEYGNITSLQIPFGTLWKPDILLFNSANEHFDSSFPVNMVVSNDGNVLFAPPGIMQFSCSLSMTWFPYDEQVCYLKFGSWTYGKKLDLRIDDADLPEGHKMDLQYYVPNGEFDLISTPAFRKSTTFLDETYVELYFHMHLKRRTMYYGLNWIIPSILISLSNILGFTMPVECGEKVTLQITNFLSIMVFLAMVSEVAPPTSESIPIIAAFFSFAIVILGVSICVSLITVNIFYRHPKMHRMGDWTRYIFLEWLPWFLLMSRPDHVFRKPKREKKKEEEEDEESNAGGKEEESELISQKQQRPRLLVNSQIVMDSTIPYLEEVIGYLKVFKAKLDDDEEEEEEILNWRFMAMVIDRASLFLFTGLIFGTTFVIFAACPNLFSADQIIETEPVIT
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane (By similarity). Nicotinic acetylcholine receptor in the MC pharyngeal motor neuron involved in pharyngeal pumping (PubMed:15020415, PubMed:8601480). Has a role in the determination of life span possibly via calorific restriction which affects growth rate, although this is independent of metabolic activity (PubMed:8462849, PubMed:9789046, PubMed:15141086, PubMed:28853436, PubMed:30965033). Plays a role in the defense against the accumulation of ingested live pathogenic bacteria in the intestine (PubMed:30965033). Neuronal AChR seems to be composed of two different type of subunits: alpha and beta. MC motor neuron. Expressed in pharyngeal muscle. Worms exhibit a lack of MC neurotransmission possibly explaining the observed reduction in pharyngeal pumping rate (PubMed:15020415). Mutants show differences in their pharyngeal responses to nicotine (PubMed:15020415). A variety of mutants show an increase in lifespan ranging from 29-57% longer than wild-type (PubMed:15141086, PubMed:28853436). Extended self-fertile reproductive span, fast body movement, and a longer pharyngeal pumping span (PubMed:15141086). The strongest allele (ad1113) shows retarded growth (PubMed:15141086). Animals generally have smaller nucleoli (PubMed:28853436). Double knockout with ncl-1 reduces the increased longevity and suppresses the reduced nucleoli size phenotype of the eat-2 single mutant, and reduces the increased ribosomal protein synthesis in the ncl-1 single mutant (e1942) (PubMed:28853436). Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MTLKIAFFTLILLVSIERVYSSDEEYRLLKDLREGYDPVERPVADHRKPVNVKLRLILQQLVDVDERNQVITLVVWNQYTWNDYKLRWSPEEYGNITTLQIPHGTLWKPDILLFNSANEHFDASFPVHMVVSSNGDVLFAPPGIVSFSCSLSMTWFPYDQQVCYLKFGSWTYGKKLDLQIDDSDLPDGHKMDLQYYIPNGEFDLLATPAFRKSTTFLDETYVELYFHMHLKRRTMYYGLNWIVPSILISLSNILGFTMPPECGEKITLQITNFLSVMVFLAMVSEVAPPTSESIPIIAAFFSLSIVILGLSICASLIIVNIFFRHPKTHRMGDWTRYVFLEWLPWFLLMSRPEHTFCRPRREEEKNDEEAGGDGTKLLENQQHQPRPRLLVNSQLVMDSTVPYLEEIIGYLKVFKAKLDDDEEEEEEILNWRFMAMVIDRLSLFLFTGLIFGTTALIFAFCPNLFTDSPIVDIE
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Expressed in the liver, olfactory mucosa, pituitary gland, hair cells of the saccule and spleen. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MKTVVLLTWISCWIDVCTSAQGRYAQKLLNDLMENYSSALRPVEDTDKTLNVTLQITLSQIKDMDERNQVLTTYLWIRQTWFDAYLKWDKEEYDGLEVIRIPSNLVWRPDIVLYNKADEEASGPADTNVVLRYNGEITWDMPAITKSSCVVDVSYFPFDWQWCNLTFGSWTYNGNQVDIAMGMDSGDLSDFVENVEWECHGMPAVRNVIMYGCCSDPYPDITYTLHLKRRSLFYIFNLLLPCFLISFLAPLGFYLPADSGEKVSLGVTVLLALTVFQLMVAESMPPSESVPYIGKYYIATMTMITASTSLTIFIMNIHFCGAEAKPVPHWAKVLIIDYMSKILFVYEVGENCTTPESERTPLYSEEPMSGNSALARNHYHDDLYHDGGCYQDDCHRLRPYQYGNGHLQNHHSTHQNHLDNCRYANGGHRDDHYSNRSNQNHHSNRSQTSKGEGGEEKREPLRHYHHIGREELDYQAPPPGNLQNGGLNEPLPYPKEKHLNPASAPACSCPCPHHKQVVYNIQYIANCFREQRATCAKGAEWKKVAKVMDRFFMWIFFIMVFLMSILIIGKAT
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Expressed in the brain, liver, olfactory mucosa, pituitary gland and hair cells of the saccule. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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MRKMVPVVCFATMLLQVAHSAQGRYAQQLLTDLMENYSNALRPVEDTDKALNVTLQITLSQIKDMDERNQVLIAYLWIRQTWHDAYLRWNKEDYDGLEVIRIPSSLVWRPDLVLYNKADDDFSGPLDTNVVLRYNGEITWDAPAITKSSCVVDVSYFPFDSQECNLTFGSWTYNGNQVDIAMGMDSGDLSDFVENVEWECHGMPATKNVIMYGCCSDPYPDITYTVLLQRRSSFYIFNLLLPCFLISFLAPLGFYLPADSGEKVSLGVTVLLALTVFQLMVAESMPPSESVPLIGKYYIATMTMITASTALTIFIMNIHFCGAEAKPVPHWAKVLIIDYMSKIFFVYEVGENCATATSSSSSSSSSSHFGQDDVHQPNFSSHRQANGKPGGNSGRENQYRHKNPRPQTPGPQRHPKPRHQHHITRDEKNHLSSSKYEGFESNRNLPLGDCCKEAPPCCPEDEKTAVVAAAVASVTFGPCVFCSHGSSLPGVDSKLVRNVEYIANCFREQRATCAKGAEWKRVAKVMDRFFMWIFFIMVFLMSILIIGKAP
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Neuronal AChR seems to be composed of two different type of subunits: alpha and non-alpha (also called beta). A functional receptor seems to consist of two alpha-chains and three non-alpha chains. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-subfamily.
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MGWPCRSIIPLLVWCFVTLQAATREQKQPHGFAEDRLFKHLFTGYNRWSRPVPNTSDVVIVKFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPEDFDNVTSIRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSNGKVKWVPPAIYKSSCSIDVTYFPFDQQNCKMKFGSWTYDKAKIDLENMEHHVDLKDYWESGEWAIINAIGRYNSKKYDCCTEIYPDITFYFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIIITVFVLNVHHRSPSTHTMPHWVRSFFLGFIPRWLFMKRPPLLLPAEGTTGQYDPPGTRLSTSRCWLETDVDDKWEEEEEEEEEEEEEEEEEKAYPSRVPSGGSQGTQCHYSCERQAGKASGGPAPQVPLKGEEVGSDQGLTLSPSILRALEGVQYIADHLRAEDADFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPYLAGMI
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. The alpha-2:beta-2 nAChR complex is proposed to be a heteropentamer with two subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding. The disease is caused by variants affecting the gene represented in this entry. The disease may be caused by variants affecting the gene represented in this entry. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-subfamily. With the use of epibatidine as high affinity ligand, an alpha-2 homopentamer has been purified and crystallized. Its physiological relevance has not been proven.
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MGPSCPVFLSFTKLSLWWLLLTPAGGEEAKRPPPRAPGDPLSSPSPTALPQGGSHTETEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVDAEEREVVVEEEDRWACAGHVAPSVGTLCSHGHLHSGASGPKAEALLQEGELLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLPPFLAGMI
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. The alpha-2:beta-2 nAChR complex is proposed to be a heteropentamer with two subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding (By similarity). Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-subfamily.
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MAPSHPAFQFWIHLYLWCLLLMPAVLAQQGSHTHAEDRLFKHLFGGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWNDYKLRWDPAEFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFFTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMERTVDLKDYWESGEWAIINATGTYNSKKYDCCAEIYPDVTYYFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHNMPNWVRVALLGRVPRWLMMNRPLPPMELHGSPGLKLSPTYHWLETNMDAEEREETEEEEEEEEDENICMCAGLPDSSMGVLYGHGSLHLRAMGPEAKTPSQASEILLSPQIQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVVDRIFLWLFIIVCFLGTIGLFLPPFLAGMI
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. The alpha-2:beta-2 nAChR complex is proposed to be a heteropentamer with two subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding (By similarity). Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-subfamily.
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MGPSCPVFLSFTKLSLWWLLLTPAGGEEAKRPPPRAPGDPLSSPSPTALPQGGSHTETEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPADFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSNCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTMPHWVRGTLLGCVPRWLLMNRPPPPLELCHPLHLKLSPSYHWLESNVDAEEREVVVEEEDRWACAGHVAPSVGTLCSHGHLHSGASGPKAEALLQEGELLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLPPFLAGMI
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. The alpha-2:beta-2 nAChR complex is proposed to be a heteropentamer with two subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-subfamily.
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MTLSHSALQFWTHLYLWCLLLVPAVLTQQGSHTHAEDRLFKHLFGGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWNDYKLRWDPAEFGNVTSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFFTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMERTVDLKDYWESGEWAIINATGTYNSKKYDCCAEIYPDVTYYFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHNMPNWVRVALLGRVPRWLMMNRPLPPMELHGSPDLKLSPSYHWLETNMDAGEREETEEEEEEEDENICVCAGLPDSSMGVLYGHGGLHLRAMEPETKTPSQASEILLSPQIQKALEGVHYIADRLRSEDADSSVKEDWKYVAMVVDRIFLWLFIIVCFLGTIGLFLPPFLAGMI
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