A0A351IT24 · A0A351IT24_9ACTN

  • Protein
    Arginine biosynthesis bifunctional protein ArgJ
  • Gene
    argJ
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

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

Lacks conserved residue(s) required for the propagation of feature annotation.
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.

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site112Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Site113Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Binding site149substrate
Binding site176substrate
Site186-187Cleavage; by autolysis
Active site187Nucleophile
Binding site187substrate
Binding site266substrate
Binding site388substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglutamate N-acetyltransferase activity
Molecular FunctionL-glutamate N-acetyltransferase activity
Biological Processarginine biosynthetic process
Biological Processornithine biosynthetic process

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
    • ORF names
      DCY69_02090
      , DCY87_00285
      , DCZ35_03700

Organism names

  • Taxonomic identifier
  • Strains
    • UBA11102
    • UBA11106
    • UBA9410
  • Taxonomic lineage
    Bacteria > Actinomycetota > Acidimicrobiia > Acidimicrobiales > Acidimicrobiaceae

Accessions

  • Primary accession
    A0A351IT24

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_50346237571-186Arginine biosynthesis bifunctional protein ArgJ alpha chain
ChainPRO_5034623756187-392Arginine biosynthesis bifunctional protein ArgJ beta chain

Keywords

Interaction

Subunit

Heterotetramer of two alpha and two beta chains.

Family & Domains

Sequence similarities

Belongs to the ArgJ family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    392
  • Mass (Da)
    39,335
  • Last updated
    2018-11-07 v1
  • Checksum
    0A231D917E3D10E5
MSVTAVPGFLAAGAACGVKASGADDLAMVATADGSPVTAAGVFTSNKMTAPPVLVTREHLAATGGRAAAVVLNSGNANAATGAAGMADAELMCTLTAEALGCSPDEVLVCSTGLIGFPLPMDRIIPAIPLLAGALTVDGGPAAARAIMTTDTVPRTTITTGTTLDGDTFTIGGVAKGAAMLEPNMATMLAVLTTDALLDTVTATDLLRAAVGVSFNCLTVDGAESTNDTVLLLASGAAGPVDTGEFGGLLADACRDLAIQMADDAEGSTKTVFLTVTGAADDAEAAKGARDTANCQLVKCSWYGEDPYWGRIAAEMGAAGIAFDPATITISYGGQVVYAAEQVQPVDEIALTAHMAGRRIHLEVDLGQGSGSAWIVTTDLSHAYIDENMRTS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DNIH01000011
EMBL· GenBank· DDBJ
HAZ17194.1
EMBL· GenBank· DDBJ
Genomic DNA
DNID01000084
EMBL· GenBank· DDBJ
HAZ35504.1
EMBL· GenBank· DDBJ
Genomic DNA
DNJP01000160
EMBL· GenBank· DDBJ
HBA94924.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp