Q9ZJ10 · ARGD_BACAM

Function

Miscellaneous

May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the fourth step in lysine biosynthesis.

Catalytic activity

Cofactor

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

Note: Binds 1 pyridoxal phosphate per subunit.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 4/4.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site95-96pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site122pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site125N2-acetyl-L-ornithine (UniProtKB | ChEBI)
Binding site208-211pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionidentical protein binding
Molecular FunctionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Biological Processarginine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acetylornithine aminotransferase
  • EC number
  • Short names
    ACOAT

Gene names

    • Name
      argD

Organism names

Accessions

  • Primary accession
    Q9ZJ10

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001127181-229Acetylornithine aminotransferase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    229
  • Mass (Da)
    24,779
  • Last updated
    1999-05-01 v1
  • Checksum
    8E109AE708229176
MSSLFQTYGRWDIDIKKAKGTYVEDQNGKTYLDFIQGIAVSNLGHCHEAVTEAVKKQLDSVWHVSNLFQNSLQEQAAQKLAAHSAGDLVFFCNSGAEANEGAIKLARKATGKTKIITFLQSFHGRTYAGMAATGQDKIKTGFGPMLGGFHYLPYNDPSAFKALGEEGDIAAVMLETVQGEGGVNPASAEFLSAVQSFCKEKQALLIIDEIQTGIGRTGTRFAYQHFGLS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue229

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF001833
EMBL· GenBank· DDBJ
AAD00908.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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