Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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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) ].
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 58280 Biotin_carb_C domains in 58272 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing Biotin_carb_C domain.

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

  Click on the protein counts, or double click on taxonomic names to display all proteins containing Biotin_carb_C domain in the selected taxonomic class.

• 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		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
  2yl2		Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain
  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
  3jrw		Phosphorylated BC domain of ACC2
  3jrx		Crystal structure of the BC domain of ACC2 in complex with soraphen 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
  3n6r		CRYSTAL STRUCTURE OF the holoenzyme of PROPIONYL-COA CARBOXYLASE (PCC)
  3ouu		Crystal Structure of Biotin Carboxylase-beta-gamma-ATP Complex from Campylobacter jejuni
  3ouz		Crystal Structure of Biotin Carboxylase-ADP complex from Campylobacter jejuni
  3rup		Crystal structure of E.coli biotin carboxylase in complex with two ADP and two Ca ions
  3rv3		Crystal structure of E.coli biotin carboxylase in complex with two ADP and one Mg ion
  3rv4		Crystal structure of E.coli biotin carboxylase R16E mutant in complex with Mg-ADP and bicarbonate
  3tw6		Structure of Rhizobium etli pyruvate carboxylase T882A with the allosteric activator, acetyl coenzyme-A
  3tw7		Structure of Rhizobium etli pyruvate carboxylase T882A crystallized without acetyl coenzyme-A
  3u9s		Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, CoA complex
  3u9t		Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, free enzyme
  3va7		Crystal structure of the Kluyveromyces lactis Urea Carboxylase
  4hnt		crystal structure of F403A mutant of S. aureus Pyruvate carboxylase
  4hnu		crystal structure of K442E mutant of S. aureus Pyruvate carboxylase
  4hnv		Crystal structure of R54E mutant of S. aureus Pyruvate carboxylase
  4hq6		BC domain in the presence of citrate
  4hr7		Crystal Structure of Biotin Carboxyl Carrier Protein-Biotin Carboxylase Complex from E.coli
  4mv1		4MV1
  4mv3		4MV3
  4mv4		4MV4
  4mv6		4MV6
  4mv7		4MV7
  4mv8		4MV8
  4mv9		4MV9
  4qsh		4QSH
  4qsk		4QSK
  4qsl		4QSL
  4rcn		4RCN
  4rzq		4RZQ
  5csk		5CSK
  5csl		5CSL
  5h80		5H80
  5i6i		5I6I
  5kkn		5KKN
  5ks8		5KS8

• Links (links to other resources describing this domain)

• PFAM	Biotin_carb_C
  INTERPRO	IPR005482

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