Q1RGV0 · AAPAT_RICBR

Function

function

Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate. Can also transaminate prephenate in the presence of glutamate.

Catalytic activity

Cofactor

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

Features

Showing features for site, binding site.

TypeIDPosition(s)Description
Site12Important for prephenate aminotransferase activity
Binding site39L-aspartate (UniProtKB | ChEBI)
Binding site125L-aspartate (UniProtKB | ChEBI)
Binding site175L-aspartate (UniProtKB | ChEBI)
Binding site375L-aspartate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglutamate-prephenate aminotransferase activity
Molecular FunctionL-aspartate:2-oxoglutarate aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Biological Processamino acid metabolic process
Biological Processbiosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable aspartate/prephenate aminotransferase
  • EC number
  • Short names
    AspAT / PAT
  • Alternative names
    • Transaminase A

Gene names

    • Name
      aatA
    • Ordered locus names
      RBE_1333

Organism names

Accessions

  • Primary accession
    Q1RGV0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002731241-399Probable aspartate/prephenate aminotransferase
Modified residue239N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    399
  • Mass (Da)
    43,981
  • Last updated
    2006-05-16 v1
  • Checksum
    09F007EFF3ABCE9A
MSIISTQLNAIKPSPTLAVVRKTLELKRAGIDIIALGAGEPDFDTPDNIKEAAIKAIKDGFTKYTNVEGIPALKEAIQAKFKRENNIDYDLEEIIVSTGGKQVIYNLFMASLNKGDEVIIPAPYWVSYPDMVLLAEGTPVFANCGIESNFKLSGEALEQLITPKTKWLIINSPSNPTGASYSHSELKNIAEVLRKHPYVNVMSDDIYEHITFDGFKFYTLAEIAPDLKDRIFTVNGVSKAYSMTGWRIGYGAGSKALIKAMTIIQSQSTSNPCSISQVAAVEALNGVQGYIAQNALNFEKKRDLALSILQRVKYFECYKPEGAFYLFIKCDKIFGAKTKSGKVINNSNDFGEYLLEEAKVAVVPGIAFGLEGYFRISYATSMEELEEACLRMERACGSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000087
EMBL· GenBank· DDBJ
ABE05414.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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