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UniProt functional annotation for I6YFP0 | ||
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| UniProt code: I6YFP0. |
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| Organism: | |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. |
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| 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). {ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}. |
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| Catalytic activity: | |
Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA- COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.15; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11757; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; |
| Catalytic activity: | |
Reaction=ATP + biotin + H(+) = biotinyl-5'-AMP + diphosphate; Xref=Rhea:RHEA:31115, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:62414; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31116; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; |
| Catalytic activity: | |
Reaction=biotinyl-5'-AMP + L-lysyl-[protein] = AMP + 2 H(+) + N(6)- biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:59732, Rhea:RHEA- COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:62414, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59733; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; |
| 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. {ECO:0000269|PubMed:28942842}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.420 uM for biotin {ECO:0000269|PubMed:18509457}; KM=21.08 uM for Mg/ATP {ECO:0000269|PubMed:18509457}; KM=0.20 mM for ATP {ECO:0000269|PubMed:24723382}; KM=5.2 uM for apo-BCCP {ECO:0000269|PubMed:18509457}; Note=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). {ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:18509457}; |
| Subunit: | |
Monomer in solution (PubMed:18509457, PubMed:20169168, PubMed:24723382). Forms dimers under specific crystallization conditions (PubMed:18540066, PubMed:20169168). {ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:18540066, ECO:0000269|PubMed:20169168, ECO:0000269|PubMed:24723382}. |
| Domain: | |
Belongs to monofunctional group I BPL as it lacks the N- terminal helix-turn-helix (HTH) DNA-binding domain. {ECO:0000305|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). {ECO:0000269|PubMed:22118677, ECO:0000269|PubMed:26299766, ECO:0000269|PubMed:28942842}. |
| Similarity: | |
Belongs to the biotin--protein ligase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.