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Acetyl-coenzyme A carboxylase (EC 6.4.1.2) (ACC), a member of the biotin-dependent enzyme family, catalyses the formation of malonyl-coenzyme A (CoA) and regulates fatty acid biosynthesis and oxidation. Biotin-dependent carboxylase enzymes perform a two step reaction: enzyme-bound biotin is first carboxylated by bicarbonate and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such as acetyl-CoA. The carboxyltransferase domain perform the second part of the reaction [1,2].

The N- and C-terminal regions of the carboxyltransferase domain share similar polypeptide backbone folds, with a central β-β-α superhelix (see <PDB:1OD2>) [3]. The CoA molecule is mostly associated with the N subdomain. In bacterial acetyl coenzyme A carboxylase the N and C subdomains are encoded by two different polypeptides.

The acetyl-coenzyme A carboxyltransferase domain is also found in the following enzymes:

• Methylcrotonyl-CoA carboxylase β chain, mitochondrial precursor (EC 6.4.1.4).
• Glutaconyl-CoA decarboxylase α subunit (EC 4.1.1.70).
• Propionyl-CoA carboxylase β chain (EC 6.4.1.3) (PCCase).

We developed two profiles for this domain, one that spans the N subdomain and also recognizes the bacterial ACC β-subunit, the other profile is directed against the C subdomain and recognizes also the α-subunit of bacterial ACC.

Herbicide that target the carboxyltransferase domain are powerful inhibitors of plastid ACC and can kill sensitive plants by shutting down fatty acid biosynthesis.

May 2004 / First entry.

PROSITE methods (with tools and information) covered by this documentation:

COA_CT_CTER, PS50989; Acetyl-coenzyme A carboxyltransferase domain C-terminal region profile  (MATRIX)

Sequences known to belong to this class detected by the second profile: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Domain architecture view of Swiss-Prot proteins matching PS50989 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50989 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50989 • Scan Swiss-Prot/TrEMBL entries against PS50989 • view ligand binding statistics

Matching PDB structures: 1OD2 1OD4 1ON3 1ON9 ... [ALL]

COA_CT_NTER, PS50980; Acetyl-coenzyme A carboxyltransferase domain N-terminal region profile  (MATRIX)

Sequences known to belong to this class detected by the first profile: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Domain architecture view of Swiss-Prot proteins matching PS50980 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50980 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50980 • Scan Swiss-Prot/TrEMBL entries against PS50980 • view ligand binding statistics

Matching PDB structures: 1OD2 1OD4 1ON3 1ON9 ... [ALL]

1	Authors	Knowles J.R.
	Title	The mechanism of biotin-dependent enzymes.
	Source	Annu. Rev. Biochem. 58:195-221(1989).
	PubMed ID	2673009
	DOI	10.1146/annurev.bi.58.070189.001211;

2	Authors	Attwood P.V., Wallace J.C.
	Title	Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes.
	Source	Acc. Chem. Res. 35:113-120(2002).
	PubMed ID	11851389

3	Authors	Zhang H., Yang Z., Shen Y., Tong L.
	Title	Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
	Source	Science 299:2064-2067(2003).
	PubMed ID	12663926
	DOI	10.1126/science.1081366

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