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InterPro: IPR001249 Acetyl-CoA biotin carboxyl carrier

Protein matchesHelp
UniProtKB
Matches:
1480 proteins
AccessionHelp IPR001249 AcCoA_biotinCC
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR001882 Biotin-binding site
IPR011053 Single hybrid motif
GO Term annotationHelp
Process GO:0006633 fatty acid biosynthetic process
Function GO:0003989 acetyl-CoA carboxylase activity
Component GO:0009317 acetyl-CoA carboxylase complex
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The proteins in this family are a component of the acetyl coenzyme A carboxylase complex (EC:6.4.1.2) and are involved in the first step in long-chain fatty acid synthesis. In plants this is usually located in the chloroplast. In the first step, biotin carboxylase catalyses the carboxylation of the carrier protein to form an intermediate. Next, the transcarboxylase complex transfers the carboxyl group from the intermediate to acetyl-CoA forming malonyl-CoA. This protein functions in the transfer of CO2 from one site to another, the biotin binding site locates to the C-terminal of this protein. The biotin is specifically attached to a lysine residue in the sequence AMKM.

The structure of the C-terminal domain of the biotin carboxyl carrier (BCC) protein was shown to be a flattened beta-barrel structure comprising two four-stranded beta sheets interrupted by a structural loop forming a thumb structure. The biotinyl-lysine is located on a tight beta-turn on the opposite end of the molecule. The thumb structure has been shown to attached biotin, thus stabilising the structure.

Structural linksHelp
SCOP: b.84.1.1
CATH: 2.40.50.100
Database linksHelp
Blocks: IPB001249
COMe: PRX001098

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001249 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O19918 Biotin carboxyl carrier protein of acetyl-CoA carboxylase

P0ABD8 Biotin carboxyl carrier protein of acetyl-CoA carboxylase

Q06881 Biotin carboxyl carrier protein of acetyl-CoA carboxylase

Q42533 Biotin carboxyl carrier protein of acetyl-CoA carboxylase 1, chloroplastic

Q42783 Biotin carboxyl carrier protein of acetyl-CoA carboxylase, chloroplastic

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001882 Biotin-binding site
IPR011053 Single hybrid motif
IPR001249 Acetyl-CoA biotin carboxyl carrier
IPR000089 Biotin/lipoyl attachment
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp

Additional ReadingHelp
Li SJ, Cronan JE Jr.
The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase.
J. Biol. Chem. 267 1992 16841-7 [PubMed: 1355089]
http://intl.jbc.org/cgi/content/abstract/267/24/16841
Li SJ, Cronan JE Jr.
The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase.
J. Biol. Chem. 267 1992 855-63 [PubMed: 1370469]
http://intl.jbc.org/cgi/content/abstract/267/2/855
Yao X, Wei D, Soden C Jr, Summers MF, Beckett D.
Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase.
Biochemistry 36 1997 15089-100 [PubMed: 9398236]
http://dx.doi.org/10.1021/bi971485f
Athappilly FK, Hendrickson WA.
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.
Structure 3 1995 1407-19 [PubMed: 8747466]
http://dx.doi.org/10.1016/S0969-2126(01)00277-5
Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE Jr, Perham RN.
Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy.
Biochemistry 38 1999 5045-53 [PubMed: 10213607]
http://dx.doi.org/10.1021/bi982466o
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InterPro 23.1