Biotin_carb_C

Biotin carboxylase C-terminal domain

• SMART accession number: SM00878
• Description: Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
• Interpro abstract (IPR005482):

  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 [(PUBMED:7915138)].

• GO function: ligase activity (GO:0016874)

There are 4247 Biotin_carb_C domains in 4247 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: metabolism

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Waldrop GL, Rayment I, Holden HM
• Three-dimensional structure of the biotin carboxylase subunit ofacetyl-CoA carboxylase.
• Biochemistry. 1994; 33: 10249-56

Acetyl-CoA carboxylase is found in all animals, plants, and bacteria andcatalyzes the first committed step in fatty acid synthesis. It is amulticomponent enzyme containing a biotin carboxylase activity, a biotincarboxyl carrier protein, and a carboxyltransferase functionality. Here wereport the X-ray structure of the biotin carboxylase component fromEscherichia coli determined to 2.4-A resolution. The structure was solvedby a combination of multiple isomorphous replacement and electron densitymodification procedures. The overall fold of the molecule may be describedin terms of three structural domains. The N-terminal region, formed by Met1-Ile 103, adopts a dinucleotide binding motif with five strands ofparallel beta-sheet flanked on either side by alpha-helices. The"B-domain" extends from the main body of the subunit where it folds intotwo alpha-helical regions and three strands of beta-sheet. Following theexcursion into the B-domain, the polypeptide chain folds back into thebody of the protein where it forms an eight-stranded antiparallelbeta-sheet. In addition to this major secondary structural element, theC-terminal domain also contains a smaller three-stranded antiparallelbeta-sheet and seven alpha-helices. The active site of the enzyme has beenidentified tentatively by a difference Fourier map calculated betweenX-ray data from the native crystals and from crystals soaked in aAg+/biotin complex. Those amino acid residues believed to form part of theactive site pocket include His 209-Glu 211, His 236-Glu 241, Glu 276, Ile287-Glu 296, and Arg 338.2+ represents the first X-ray model of abiotin-dependent carboxylase.

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
31.80	map00061	Fatty acid biosynthesis
15.75	map00620	Pyruvate metabolism
12.20	map00252	Alanine and aspartate metabolism
12.20	map00020	Citrate cycle (TCA cycle)
9.84	map00280	Valine, leucine and isoleucine degradation
8.43	map00640	Propanoate metabolism
3.55	map00253	Tetracycline biosynthesis
3.48	map04910	Insulin signaling pathway
1.26	map00220	Urea cycle and metabolism of amino groups
0.67	map00791	Atrazine degradation
0.30	map00632	Benzoate degradation via CoA ligation
0.07	map00260	Glycine, serine and threonine metabolism
0.07	map00970	Aminoacyl-tRNA biosynthesis
0.07	map00251	Glutamate metabolism
0.07	map00910	Nitrogen metabolism
0.07	map00071	Fatty acid metabolism
0.07	map00330	Arginine and proline metabolism
0.07	map00780	Biotin metabolism

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with Biotin_carb_C domain which could be assigned to a KEGG orthologous group, and not all proteins containing Biotin_carb_C domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of Biotin_carb_C domains in PDB

PDB code	Title
1bnc	Three-dimensional structure of the biotin carboxylase subunit of acetyl-coa carboxylase
1dv1	Structure of biotin carboxylase (apo)
1dv2	The structure of biotin carboxylase, mutant e288k, complexed with atp
1ulz	Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase
1w93	Crystal structure of biotin carboxylase domain of acetyl- coenzyme a carboxylase from saccharomyces cerevisiae
1w96	Crystal structure of biotin carboxylase domain of acetyl- coenzyme a carboxylase from saccharomyces cerevisiae in complex with soraphen a
2c00	Crystal structure of biotin carboxylase from pseudomonas aeruginosa in apo form
2dzd	Crystal structure of the biotin carboxylase domain of pyruvate carboxylase
2gps	Crystal structure of the biotin carboxylase subunit, e23r mutant, of acetyl-coa carboxylase from escherichia coli.
2gpw	Crystal structure of the biotin carboxylase subunit, f363a mutant, of acetyl-coa carboxylase from escherichia coli.
2hjw	Crystal structure of the bc domain of acc2
2j9g	Crystal structure of biotin carboxylase from e. coli in complex with amppnp and adp
2qf7	Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli
2v58	Crystal structure of biotin carboxylase from e.coli in complex with potent inhibitor 1
2v59	Crystal structure of biotin carboxylase from e.coli in complex with potent inhibitor 2
2v5a	Crystal structure of biotin carboxylase from e.coli in complex with potent inhibitor 3
2vpq	Crystal structure of biotin carboxylase from s. aureus complexed with amppnp
2vqd	Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp
2vr1	Crystal structure of biotin carboxylase from e. coli in complex with atp analog, adpcf2p.
2w6m	Crystal structure of biotin carboxylase from e. coli in complex with amino-oxazole fragment series
2w6n	Crystal structure of biotin carboxylase from e. coli in complex with amino-oxazole fragment series
2w6o	Crystal structure of biotin carboxylase from e. coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro- quinazolinone fragment
2w6p	Crystal structure of biotin carboxylase from e. coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine
2w6q	Crystal structure of biotin carboxylase from e. coli in complex with the triazine-2,4-diamine fragment
2w6z	Crystal structure of biotin carboxylase from e. coli in complex with the 3-(3-methyl-but-2-enyl)-3h-purin-6- ylamine fragment
2w70	Crystal structure of biotin carboxylase from e. coli in complex with the amino-thiazole-pyrimidine fragment
2w71	Crystal structure of biotin carboxylase from e. coli in complex with the imidazole-pyrimidine inhibitor
3bg5	Crystal structure of staphylococcus aureus pyruvate carboxylase
3g8c	Crystal stucture of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion
3g8d	Crystal structure of the biotin carboxylase subunit, e296a mutant, of acetyl-coa carboxylase from escherichia coli
3gid	The biotin carboxylase (bc) domain of human acetyl-coa carboxylase 2 (acc2) in complex with soraphen a
3glk	The biotin carboxylase (bc) domain of human acetyl-coa carboxylase 2 (acc2)
3hb9	Crystal structure of s. aureus pyruvate carboxylase a610t mutant
3hbl	Crystal structure of s. aureus pyruvate carboxylase t908a mutant
3ho8	Crystal structure of s. aureus pyruvate carboxylase in complex with coenzyme a
3jzf	Crystal structure of biotin carboxylase from e. coli in complex with benzimidazoles series
3jzi	Crystal structure of biotin carboxylase from e. coli in complex with benzimidazole series

Links (links to other resources describing this domain)

• PFAM: Biotin_carb_C
• INTERPRO: IPR005482