A0R066 · ILVE_MYCS2
- ProteinBranched-chain-amino-acid aminotransferase
- GeneilvE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids368 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val.
Catalytic activity
- 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Cofactor
Activity regulation
Inhibited by ammonium sulfate at millimolar concentrations and by O-benzylhydroxylamine (Obe).
Pathway
Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 101 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 209 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 271-272 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: IT | ||||||
Binding site | 314 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | branched-chain-amino-acid transaminase activity | |
Molecular Function | L-isoleucine transaminase activity | |
Molecular Function | L-leucine transaminase activity | |
Molecular Function | L-leucine:2-oxoglutarate aminotransferase activity | |
Molecular Function | L-valine transaminase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | branched-chain amino acid metabolic process | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | L-leucine biosynthetic process | |
Biological Process | protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine | |
Biological Process | valine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBranched-chain-amino-acid aminotransferase
- EC number
- Short namesBCAT
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0R066
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000396109 | 1-368 | Branched-chain-amino-acid aminotransferase | |||
Sequence: MNSGPLEFTVSANTNPATDAVRESILANPGFGKYYTDHMVSIDYTVDEGWHNAQVIPYGPIQLDPSAIVLHYGQEIFEGLKAYRWADGSIVSFRPEANAARLQSSARRLAIPELPEEVFIESLRQLIAVDEKWVPPAGGEESLYLRPFVIATEPGLGVRPSNEYRYLLIASPAGAYFKGGIKPVSVWLSHEYVRASPGGTGAAKFGGNYAASLLAQAQAAEMGCDQVVWLDAIERRYVEEMGGMNLFFVFGSGGSARLVTPELSGSLLPGITRDSLLQLATDAGFAVEERKIDVDEWQKKAGAGEITEVFACGTAAVITPVSHVKHHDGEFTIADGQPGEITMALRDTLTGIQRGTFADTHGWMARLN | ||||||
Modified residue | 204 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K | ||||||
Cross-link | 299 | Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length368
- Mass (Da)39,837
- Last updated2007-01-09 v1
- Checksum19C86C028296591D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000480 EMBL· GenBank· DDBJ | ABK74679.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001663 EMBL· GenBank· DDBJ | AFP40633.1 EMBL· GenBank· DDBJ | Genomic DNA |