I6YFP0 · BIRA_MYCTU

Function

function

Catalyzes the transfer of biotin onto a conserved lysine residue of the biotin carboxyl carrier protein (BCCP) domain of acetyl-CoA carboxylase and converts it to active holo-BCCP (PubMed:18509457, PubMed:24723382).
Forms an acyl-adenylate intermediate (PubMed:18509457, PubMed:24723382).
Cannot use GTP or desthiobiotin (PubMed:18509457).

Miscellaneous

Identified as a drug target (PubMed:22118677, PubMed:26299766, PubMed:28942842).
Inhibited by Bio-AMS, an acylsulfamide bisubstrate inhibitor, and analogs (PubMed:22118677, PubMed:26299766).
Bio-AMS displays potent subnanomolar enzyme inhibition and antitubercular activity against multidrug resistant and extensively drug resistant Mtb strains (PubMed:22118677).

Catalytic activity

Activity regulation

Binding of biotin and ATP significantly increases the thermal stability of BirA and leads to the formation of a high affinity holoenzyme complex.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.42 μMbiotin
21.08 μMMg/ATP
0.2 mMATP
5.2 μMapo-BCCP
kcat is 0.034 sec-1 with biotin as substrate. kcat is 0.0282 sec-1 with Mg/ATP as substrate. kcat is 0.030 sec-1 with apo-BCCP as substrate (PubMed:18509457).
kcat is 0.017 sec-1 with ATP as substrate (PubMed:24723382).

pH Dependence

Optimum pH is 7.5-8.0.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site38-39biotin (UniProtKB | ChEBI)
Binding site63biotin (UniProtKB | ChEBI)
Binding site67biotin (UniProtKB | ChEBI)
Binding site138biotin (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentprotein-containing complex
Molecular FunctionATP binding
Molecular Functionbiotin binding
Molecular Functionbiotin-[acetyl-CoA-carboxylase] ligase activity
Molecular Functionprotein homodimerization activity
Biological Processpositive regulation of cell population proliferation
Biological Processprotein modification process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Biotin--[acetyl-CoA-carboxylase] ligase
  • EC number
  • Alternative names
    • Biotin--[biotin carboxyl-carrier protein] ligase
    • Biotin--protein ligase
      (BPL
      )
    • Biotin-[acetyl-CoA carboxylase] synthetase

Gene names

    • Name
      birA
    • Ordered locus names
      Rv3279c

Organism names

Accessions

  • Primary accession
    I6YFP0

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis138Loss of activity.

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004525011-266Biotin--[acetyl-CoA-carboxylase] ligase

Proteomic databases

Interaction

Subunit

Monomer in solution (PubMed:18509457, PubMed:20169168, PubMed:24723382).
Forms dimers under specific crystallization conditions (PubMed:18540066, PubMed:20169168).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain14-202BPL/LPL catalytic

Domain

Belongs to monofunctional group I BPL as it lacks the N-terminal helix-turn-helix (HTH) DNA-binding domain.

Sequence similarities

Belongs to the biotin--protein ligase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    266
  • Mass (Da)
    28,121
  • Last updated
    2012-10-03 v1
  • Checksum
    3DE5CE48830F070F
MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP46098.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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