A0R066 · ILVE_MYCS2

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

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

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.

TypeIDPosition(s)Description
Binding site101pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site209pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site271-272pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site314pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionbranched-chain-amino-acid transaminase activity
Molecular FunctionL-isoleucine transaminase activity
Molecular FunctionL-leucine transaminase activity
Molecular FunctionL-leucine:2-oxoglutarate aminotransferase activity
Molecular FunctionL-valine transaminase activity
Molecular Functionpyridoxal phosphate binding
Biological Processbranched-chain amino acid metabolic process
Biological Processisoleucine biosynthetic process
Biological ProcessL-leucine biosynthetic process
Biological Processprotein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
Biological Processvaline biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Branched-chain-amino-acid aminotransferase
  • EC number
  • Short names
    BCAT

Gene names

    • Name
      ilvE
    • Ordered locus names
      MSMEG_4276, MSMEI_4176

Organism names

Accessions

  • Primary accession
    A0R066
  • Secondary accessions
    • I7FPI5

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00003961091-368Branched-chain-amino-acid aminotransferase
Modified residue204N6-(pyridoxal phosphate)lysine
Cross-link299Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Keywords

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    368
  • Mass (Da)
    39,837
  • Last updated
    2007-01-09 v1
  • Checksum
    19C86C028296591D
MNSGPLEFTVSANTNPATDAVRESILANPGFGKYYTDHMVSIDYTVDEGWHNAQVIPYGPIQLDPSAIVLHYGQEIFEGLKAYRWADGSIVSFRPEANAARLQSSARRLAIPELPEEVFIESLRQLIAVDEKWVPPAGGEESLYLRPFVIATEPGLGVRPSNEYRYLLIASPAGAYFKGGIKPVSVWLSHEYVRASPGGTGAAKFGGNYAASLLAQAQAAEMGCDQVVWLDAIERRYVEEMGGMNLFFVFGSGGSARLVTPELSGSLLPGITRDSLLQLATDAGFAVEERKIDVDEWQKKAGAGEITEVFACGTAAVITPVSHVKHHDGEFTIADGQPGEITMALRDTLTGIQRGTFADTHGWMARLN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000480
EMBL· GenBank· DDBJ
ABK74679.1
EMBL· GenBank· DDBJ
Genomic DNA
CP001663
EMBL· GenBank· DDBJ
AFP40633.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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