A0AA35SMB1 · A0AA35SMB1_GEOBA

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.

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.

Type
IDPosition(s)Description
Site21Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Site22Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Binding site56substrate
Binding site82substrate
Site92-93Cleavage; by autolysis
Active site93Nucleophile
Binding site93substrate
Binding site179substrate
Binding site302substrate
Binding site307substrate

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Molecular Functionglutamate N-acetyltransferase activity
Molecular FunctionL-glutamate N-acetyltransferase activity
Biological ProcessL-arginine biosynthetic process
Biological Processornithine biosynthetic process

Keywords

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
      GBAR_LOCUS17736

Organism names

Accessions

  • Primary accession
    A0AA35SMB1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_50414957031-92Arginine biosynthesis bifunctional protein ArgJ alpha chain
ChainPRO_504149570493-307Arginine 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.

Family & Domains

Sequence similarities

Belongs to the ArgJ family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    307
  • Mass (Da)
    32,265
  • Last updated
    2024-01-24 v1
  • MD5 Checksum
    89E2DFE2CCFF7887C09D66B1B65BA8CB
MTELAAAHTGVSADDMLVCSTGMIGVELPMALLRQHVGNVSLSGDGGHDFARSIMTTDTRRKDLAVSIDLGGRKVVLGGAAKGVGMIHPNMATMLAFVATDAPVEQSFLQSALSRAVDDSFNMCSVDGDQSTNDTVLVFANGQAGGDEVVAGTPEAEAFEEALTFVCTSLAKEMVRDGEGAKKLIEVTVGEAGTMADARKAAREISTSSLVKAMVHGNDPNWGRIMMALGKSGADMDESKIDIFIDDIQIVHEGKAIPFHMDSVVSSMASSPDVRFRVSLNLGGESATAWGCDLTEEYVTFNSAYST

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0AA35SLD4A0AA35SLD4_GEOBAGBAR_LOCUS17736397
A0AA35SKQ5A0AA35SKQ5_GEOBAGBAR_LOCUS17736368
A0AA35SJH3A0AA35SJH3_GEOBAGBAR_LOCUS17736375

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CASHTH010002526
EMBL· GenBank· DDBJ
CAI8031236.1
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.
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