Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2008) Nucleic Acids Res , doi:10.1093/nar/gkn808

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Biotin_carb_C Biotin carboxylase C-terminal domain

There are 2023 Biotin_carb_C domains in 2023 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a Biotin_carb_C domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Biotin_carb_C domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• 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
  • Display abstract

  • 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)

• Click the image to view the interactive version of the map in iPath

  % 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	Main view	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
  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
  2qf7		Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli
  2v58
  2v59
  2v5a
  2vpq
  2vqd
  2vr1
  2w6m
  2w6n
  2w6o
  2w6p
  2w6q
  2w6z
  2w70
  2w71
  3bg5		Crystal structure of staphylococcus aureus pyruvate carboxylase
  3g8c
  3g8d
  3gid
  3glk
  3hb9
  3hbl
  3ho8
  3jzf
  3jzi

• Links (links to other resources describing this domain)

• PFAM	Biotin_carb_C