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InterPro: IPR011763 Acetyl-coenzyme A carboxyltransferase, C-terminal

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UniProtKB

Matches:

3881 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011763 COA_CT_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PROSITE profile	PS50989	COA_CT_CTER	3881
Signatures in BioMart

InterPro Relationships Help

Children

IPR001095 Acetyl-CoA carboxylase, alpha subunit

Found in

IPR000022 Carboxyl transferase
IPR005783 Methylmalonyl-CoA decarboxylase, alpha subunit

Contains

IPR020582 Acetyl-CoA carboxylase, alpha subunit, conserved region

GO Term annotation Help

Function

GO:0016874 ligase activity

InterPro annotation

Entry Details in BioMart

Abstract

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 performs 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 beta-beta-alpha superhelix [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.

Structural links Help

PDB - click here

SCOP: c.14.1.4

CATH: 3.90.226.10

Database links Help

Enzyme: EC:6.4.1.2

PROSITE doc: PDOC50980

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011763

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00763 Acetyl-CoA carboxylase 2

P34385 Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Q00955 Acetyl-CoA carboxylase

Q3ULD5 Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Q9V9A7 Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005481	Carbamoyl phosphate synthase, large subunit, N-terminal
IPR013816	ATP-grasp fold, subdomain 2
IPR013817	Pre-ATP-grasp fold
IPR001882	Biotin-binding site
IPR005482	Biotin carboxylase, C-terminal
IPR013537	Acetyl-CoA carboxylase, central region
IPR011764	Biotin carboxylation domain
IPR005479	Carbamoyl phosphate synthetase, large subunit, ATP-binding
IPR016185	PreATP-grasp-like fold
IPR000022	Carboxyl transferase
IPR011761	ATP-grasp fold
IPR011762	Acetyl-coenzyme A carboxyltransferase, N-terminal
IPR011763	Acetyl-coenzyme A carboxyltransferase, C-terminal
IPR011053	Single hybrid motif
IPR011054	Rudiment single hybrid motif
IPR000089	Biotin/lipoyl attachment
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Knowles JR. The mechanism of biotin-dependent enzymes. Annu. Rev. Biochem. 58 195-221 1989 [PubMed: 2673009] http://dx.doi.org/10.1146/annurev.bi.58.070189.001211
2.	Attwood PV, Wallace JC. Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes. Acc. Chem. Res. 35 113-20 2002 [PubMed: 11851389] http://dx.doi.org/10.1021/ar000049+
3.	Zhang H, Yang Z, Shen Y, Tong L. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Science 299 2064-7 2003 [PubMed: 12663926] http://dx.doi.org/10.1126/science.1081366

Additional Reading Open in usermanual
	Zhang H, Tweel B, Li J, Tong L. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in complex with CP-640186. Structure 12 2004 1683-91 [PubMed: 15341732] http://dx.doi.org/10.1016/j.str.2004.07.009
	Zhang H, Tweel B, Tong L. Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop. Proc. Natl. Acad. Sci. U.S.A. 101 2004 5910-5 [PubMed: 15079078] http://dx.doi.org/10.1073/pnas.0400891101
	Lin TW, Melgar MM, Kurth D, Swamidass SJ, Purdon J, Tseng T, Gago G, Baldi P, Gramajo H, Tsai SC. Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 103 2006 3072-7 [PubMed: 16492739] http://dx.doi.org/10.1073/pnas.0510580103
	Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL. The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry 45 2006 1712-22 [PubMed: 16460018] http://dx.doi.org/10.1021/bi0520479
	Holton SJ, King-Scott S, Nasser Eddine A, Kaufmann SH, Wilmanns M. Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis. FEBS Lett. 580 2006 6898-902 [PubMed: 17157300] http://dx.doi.org/10.1016/j.febslet.2006.11.054

InterPro 23.1