A0A4U0ZWG8 · A0A4U0ZWG8_9BACT

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

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
Site106Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Site107Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Binding site143substrate
Binding site169substrate
Site179-180Cleavage; by autolysis
Active site180Nucleophile
Binding site180substrate
Binding site267substrate
Binding site390substrate
Binding site395substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
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

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
      FCL48_11250

Organism names

  • Taxonomic identifier
  • Strain
    • IMCC35007
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfobulbia > Desulfobulbales > Desulfocapsaceae > Desulforhopalus

Accessions

  • Primary accession
    A0A4U0ZWG8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_50234842901-179Arginine biosynthesis bifunctional protein ArgJ alpha chain
ChainPRO_5023484292180-395Arginine 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    395
  • Mass (Da)
    41,818
  • Last updated
    2019-07-31 v1
  • Checksum
    6E695D216B7AEFBB
MNIRGFSFSAVQAGIRYKNRLDLGLIFSDTPCVTAGVFTTSQVKAAPVVIDAERLRRTGEAQAILVNSGCANACTGKEGMKAALTTGRLLAQKLDIAEELIQLSSTGVIGEQLNMAAFEASMDALVAGLAPDNFDKVAQAIMTTDLVQKTAATRVVIGGKEVTIIGMAKGSGMIMPNMATMLSFVLTDANISQAELNEVLRQAVDTTFNRITVDGDTSTNDMVLIMANGSAKNPELNGQSPSDTGTFQQGLTVVLKDLALQIVTDGEGATKTITIRVNGAANDEDAHQVARTVANSNLVKTAFFGEDANWGRILGAMGRAGVVFDPENVTLSFGEVVMFENGLGKGKEIEAKATAVLKEKCFTVTIDLHCGQGAAEMYTCDFSLDYVKINADYRS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SWCN01000009
EMBL· GenBank· DDBJ
TKB09043.1
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