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InterPro: IPR005482 Biotin carboxylase, C-terminal

Protein matches Help

UniProtKB

Matches:

4359 proteins

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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

IPR005482 Biotin_COase_C

Secondary

IPR000901

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02785	Biotin_carb_C	4323
SMART	SM00878	Biotin_carb_C	4137
Signatures in BioMart

InterPro Relationships Help

Parent

IPR011054 Rudiment single hybrid motif

Found in

IPR004549 Acetyl-CoA carboxylase, biotin carboxylase
IPR005930 Pyruvate carboxylase
IPR011764 Biotin carboxylation domain
IPR013816 ATP-grasp fold, subdomain 2
IPR014084 Urea carboxylase

GO Term annotation Help

Function

GO:0016874 ligase activity

InterPro annotation

Entry Details in BioMart

Abstract

Acetyl-CoA carboxylase is found in all animals, plants, and bacteria and catalyzes the first committed step in fatty acid synthesis. It is a multicomponent enzyme containing a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase functionality. The "B-domain" extends from the main body of the subunit where it folds into two alpha-helical regions and three strands of beta-sheet. Following the excursion into the B-domain, the polypeptide chain folds back into the body of the protein where it forms an eight-stranded antiparallel beta-sheet. In addition to this major secondary structural element, the C-terminal domain also contains a smaller three-stranded antiparallel beta-sheet and seven alpha-helices [1].

Structural links Help

PDB - click here

SCOP: b.84.2.1

CATH: 3.30.470.20

Database links Help

Enzyme: EC:6.4.1

PANDIT: PF02785

Blocks: IPB005482

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005482

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00763 Acetyl-CoA carboxylase 2

O17732 Pyruvate carboxylase 1

Q00955 Acetyl-CoA carboxylase

Q05920 Pyruvate carboxylase, mitochondrial

Q42523 Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR005479	Carbamoyl phosphate synthetase, large subunit, ATP-binding
IPR011764	Biotin carboxylation domain
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
IPR000891	Pyruvate carboxyltransferase
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
IPR003379	Carboxylase, conserved domain
IPR016185	PreATP-grasp-like fold
IPR005930	Pyruvate carboxylase
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Waldrop GL, Rayment I, Holden HM. Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry 33 10249-56 1994 [PubMed: 7915138] http://dx.doi.org/10.1021/bi00200a004

Additional Reading Open in usermanual
	Shen Y, Volrath SL, Weatherly SC, Elich TD, Tong L. A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product. Mol. Cell 16 2004 881-91 [PubMed: 15610732] http://dx.doi.org/10.1016/j.molcel.2004.11.034
	Mochalkin I, Miller JR, Evdokimov A, Lightle S, Yan C, Stover CK, Waldrop GL. Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase. Protein Sci. 17 2008 1706-18 [PubMed: 18725455] http://dx.doi.org/10.1110/ps.035584.108
	Kondo S, Nakajima Y, Sugio S, Yong-Biao J, Sueda S, Kondo H. Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution. Acta Crystallogr. D Biol. Crystallogr. 60 2004 486-92 [PubMed: 14993673] http://dx.doi.org/10.1107/S0907444904000423
	Shen Y, Chou CY, Chang GG, Tong L. Is dimerization required for the catalytic activity of bacterial biotin carboxylase? Mol. Cell 22 2006 807-18 [PubMed: 16793549] http://dx.doi.org/10.1016/j.molcel.2006.04.026
	Kondo S, Nakajima Y, Sugio S, Sueda S, Islam MN, Kondo H. Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans. Acta Crystallogr. D Biol. Crystallogr. 63 2007 885-90 [PubMed: 17642515] http://dx.doi.org/10.1107/S0907444907029423

InterPro 23.1