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A0A534W059 · A0A534W059_UNCDE

Function

function

Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N2-acetylornithine and glutamate.

Miscellaneous

Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.
Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 2/4.

Features

Showing features for site, binding site, active site.

Type
IDPosition(s)Description
Site105Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Site106Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Binding site141substrate
Binding site167substrate
Site177-178Cleavage; by autolysis
Active site178Nucleophile
Binding site178substrate
Binding site264substrate
Binding site389substrate
Binding site394substrate
Site440Transition state stabilizer
Binding site475-476substrate
Binding site497substrate
Binding site594substrate
Site653Transition state stabilizer

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionacetylglutamate kinase activity
Molecular FunctionATP binding
Molecular Functionglutamate N-acetyltransferase activity
Molecular FunctionL-glutamate N-acetyltransferase activity
Biological Processarginine biosynthetic process via ornithine
Biological Processornithine biosynthetic process
Biological Processphosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Including 2 domains:

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

Gene names

    • Name
      argJ
    • Synonyms
      argB
    • ORF names
      E6J64_11865

Organism names

Accessions

  • Primary accession
    A0A534W059

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_50232335581-177Arginine biosynthesis bifunctional protein ArgJ alpha chain
ChainPRO_5023233559178-695Arginine biosynthesis bifunctional protein ArgJ beta chain

Keywords

Interaction

Subunit

Heterotetramer of two alpha and two beta chains.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain436-672Aspartate/glutamate/uridylate kinase

Sequence similarities

Belongs to the ArgJ family.
Belongs to the acetylglutamate kinase family. ArgB subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    695
  • Mass (Da)
    72,008
  • Last updated
    2019-10-16 v1
  • MD5 Checksum
    C971E248E72213A03B62FC91B75A2936
MKIPSGFQFAGIQAGIKPNRKDLALVYSQAPCSAAGCFTRNTARAAPVLDAEARLPSAGVHAVVVNSGNANALTGPEGLQDVKAVCEAVAHALGVPASAVLSASTGVIGHRLPAAKIVAAAPLLAQSLRPEPERAAEAILTTDTRIKMAARAVRIGGKDATISAICKGSGMIAPSLATMIAVVTTDAAVGPTALAGALQKAMERSFNALTVDNDMSTNDVVFALANGLAGNKPLVDPGPELDRFAAALTEVCKELAKDIAADGEGATKLLEVEVNGAPSDEIAMELAKSVAGSSLVKAAIFGADPNWGRVLASIGARAGTAGYDVAPAEARVSVQGVDVYDRAPTGHDGAVLKARMREPEVRVEVDLRRGAGSAVAWGCDLSYDYVKINADYTSLIVPRPDGGVAKDDRLANYSPGFKQQLLVEALGYIRRFTGTRCVVKYGGAAMVKESLKKSFCDDIGLLRSVGLRPIVVHGGGPEITRTLEKLGGKAEFVDGQRVTNTSDLKVVEMVLTGSINADLVTLLNQEGGHAVGVSGKDGALLRARKLQPESGGRDLGQVGEVTRVNKDFLDLLLQQGYVPVISPIGIGEDGQSYNINADQVAAEVAIAVGAQKLIYLSDVPGIMKAGELVEELNGAGLAAQLEDGTVQGGMRVKVRSILKALQNGVQRVHLIDGRVPHSIIGELFTDKGVGTLVTP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VBKO01000212
EMBL· GenBank· DDBJ
TMB04868.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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