Q2U7R8 · ARGJ_ASPOR

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.

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.

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
Site145Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Site146Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Binding site184substrate
Binding site213substrate
Site223-224Cleavage; by autolysis
Active site224Nucleophile
Binding site224substrate
Binding site311substrate
Binding site451substrate
Binding site456substrate

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Molecular Functionglutamate N-acetyltransferase activity
Molecular FunctionL-glutamate N-acetyltransferase 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
      AO090701000729

Organism names

Accessions

  • Primary accession
    Q2U7R8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003980221-223Arginine biosynthesis bifunctional protein ArgJ alpha chain
ChainPRO_0000398023224-456Arginine 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

Structure

Family & Domains

Sequence similarities

Belongs to the ArgJ family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    456
  • Mass (Da)
    47,996
  • Last updated
    2006-01-24 v1
  • Checksum
    15F1B26AEC6077F4
MAAFARMVKGQVRSYSAPVDMAIPASKRKFIPSSGSYPKGFVVSGTHVGVKASNTKFPDLALISSETPCSAAAVFTTNKFQAAPVQVSRDIIKTRQGQGIRSVVINSGCANAVTGKGGLEDAVSMGKKVDECDGLNEPSTLVMSTGVIGQRLPISKILKKVPVAHANLSSTHDAWLTTARAICTTDTFPKLLSRTFTLPSSPGRTYSLAGMTKGAGMIHPNMATLLGVLCTDAPIEPSALQSLLKHSVNRSFNSISVDGDTSTNDTIAILANGAAGGAPISSSSSDDYAAMQDILTSFAQSLSQLVVRDGEGATKFVTVRVQNSPDYESGRLIASTIARSPLVKTALYGKDANWGRILCAIGYTQGVAPGTVVPEHTSVSFKPVDGSPVLNLLVNGEPEQVDEERASVILQEEDLEIVVDLGGGEKGEQGLGGEEAVYWFCDFSHEYVTINGDYRT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000053
EMBL· GenBank· DDBJ
BAE62397.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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