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Information on EC 6.4.1.2 - acetyl-CoA carboxylase

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EC Tree
IUBMB Comments
This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
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UNIPROT: P0ABD8
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acetyl-coa carboxylase, accase, acetyl coa carboxylase, acetyl-coenzyme a carboxylase, acaca, acc-2, acetyl coenzyme a carboxylase, acetyl-coa carboxylase 1, acc-1, acacb, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyl-CoA carboxylase
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ACCase
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Acetyl CoA carboxylase
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Acetyl coenzyme A carboxylase
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Acetyl-coenzyme A carboxylase
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Carboxylase, acetyl coenzyme A
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:hydrogencarbonate ligase (ADP-forming)
This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-93-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BCCP_ECOLI
Escherichia coli (strain K12)
156
0
16687
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Escherichia coli biotinylated biotin carboxyl carrier protein (BCCP) complexed with biotin carboxylase (BC) to a resolution of 2.49 A. The protein-protein complex shows a unique quaternary structure and two distinct interfaces for each biotinylated biotin carboxyl carrier protein monomer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Broussard, T.C.; Kobe, M.J.; Pakhomova, S.; Neau, D.B.; Price, A.E.; Champion, T.S.; Waldrop, G.L.
The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase
Structure
21
650-657
2013
Escherichia coli (P0ABD8), Escherichia coli
Manually annotated by BRENDA team