H1W484 · H1W484_COLHI

Function

function

Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.

Catalytic activity

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N2-acetyl-L-ornithine (cyclic): step 1/1.
Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 1/4.

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site150Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Site151Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Binding site189substrate
Binding site218substrate
Site228-229Cleavage; by autolysis
Active site229Nucleophile
Binding site229substrate
Binding site316substrate
Binding site455substrate
Binding site460substrate

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Molecular Functionacetyl-CoA:L-glutamate N-acetyltransferase activity
Molecular Functionglutamate N-acetyltransferase activity
Molecular Functionmethione N-acyltransferase activity
Biological Processarginine biosynthetic process
Biological Processornithine biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Including 2 domains:

  • Recommended name
    Glutamate N-acetyltransferase
  • EC number
  • Short names
    GAT
  • Alternative names
    • Ornithine acetyltransferase
      (OATase
      )
    • Ornithine transacetylase
  • Recommended name
    Amino-acid acetyltransferase
  • EC number
  • Alternative names
    • N-acetylglutamate synthase
      (AGS
      )

Gene names

    • ORF names
      CH063_00668
      , CH63R_04276

Organism names

Accessions

  • Primary accession
    H1W484

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_50423004191-228Arginine biosynthesis bifunctional protein ArgJ alpha chain
ChainPRO_5042300418229-460Arginine biosynthesis bifunctional protein ArgJ beta chain

Post-translational modification

The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.

Keywords

Interaction

Subunit

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the ArgJ family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    460
  • Mass (Da)
    48,580
  • Last updated
    2012-03-21 v1
  • Checksum
    0380A43167B3EF15
MAQPVRRFPGHLAQFVRCYSVSAESIPAAKKKYVPTEGTYPQGFQASGILVGVKPGNKTKPDLALLSSDRPCAAAAVFTKNKFQAAPVTFSRDLLKKKSNRGIRSVLINSGCANAVTGKGGLEDASLMAHAADKAVGGEGDASSTIVMSTGVIGQRLPIAKIVDNVPAAQGALGSSHKHWLSFATAICTTDTFPKLKSKTFTLPSSPGVEYRIAGTTKGAGMIHPNMATLLGVVATDAPISPAVMPSVLKHAVDRSFNSITIDGDTSTNDTLALLANGAAGGKEIVSEDSADYAAFKEVLTDFSIDLAKLIVRDGEGATKFVTIRVVESASEEAARKIASTIARSPLVKTALYGRDANWGRILCATGYSLVSEPGQAVSDVPEVVPEKTNVSFVPTDGTPELKLLVNGEPEMVDEARASEILELEDLEIIVRLGTGDKEATYWTCDYSHEYITINGDYRT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CACQ02009568
EMBL· GenBank· DDBJ
CCF47297.1
EMBL· GenBank· DDBJ
Genomic DNA
LTAN01000003
EMBL· GenBank· DDBJ
OBR11980.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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