I6YFP0 · BIRA_MYCTU
- ProteinBiotin--[acetyl-CoA-carboxylase] ligase
- GenebirA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids266 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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
- ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H+ + N6-biotinyl-L-lysyl-[protein]This reaction proceeds in the forward direction.
- ATP + biotin + H+ = biotinyl-5'-AMP + diphosphateThis reaction proceeds in the forward direction.
- biotinyl-5'-AMP + L-lysyl-[protein] = AMP + 2 H+ + N6-biotinyl-L-lysyl-[protein]This reaction proceeds in the forward direction.
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 μM | biotin | |||||
21.08 μM | Mg/ATP | |||||
0.2 mM | ATP | |||||
5.2 μM | apo-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).
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | protein-containing complex | |
Molecular Function | ATP binding | |
Molecular Function | biotin binding | |
Molecular Function | biotin-[acetyl-CoA-carboxylase] ligase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | protein modification process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBiotin--[acetyl-CoA-carboxylase] ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionI6YFP0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 138 | Loss of activity. | ||||
Sequence: K → S |
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452501 | 1-266 | Biotin--[acetyl-CoA-carboxylase] ligase | |||
Sequence: MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-202 | BPL/LPL catalytic | ||||
Sequence: RSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWR |
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 statusComplete
- Length266
- Mass (Da)28,121
- Last updated2012-10-03 v1
- Checksum3DE5CE48830F070F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP46098.1 EMBL· GenBank· DDBJ | Genomic DNA |