Q54DY1 · ARGJ_DICDI
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- GeneargJ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids442 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- N2-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 137 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 138 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 173 | substrate | |||
Binding site | 199 | substrate | |||
Site | 209-210 | Cleavage; by autolysis | |||
Active site | 210 | Nucleophile | |||
Binding site | 210 | substrate | |||
Binding site | 297 | substrate | |||
Binding site | 437 | substrate | |||
Binding site | 442 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | glutamate N-acetyltransferase activity | |
Molecular Function | L-glutamate N-acetyltransferase activity | |
Biological Process | arginine biosynthetic process | |
Biological Process | ornithine biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- Cleaved into 2 chains
Including 2 domains:
- Recommended nameGlutamate N-acetyltransferase
- EC number
- Short namesGAT
- Alternative names
- Recommended nameAmino-acid acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Dictyostelium
Accessions
- Primary accessionQ54DY1
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-23 | Mitochondrion | |||
Chain | PRO_0000327743 | 24-209 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_0000327744 | 210-442 | Arginine 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
- PTM
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length442
- Mass (Da)47,724
- Last updated2005-05-24 v1
- MD5 Checksum15120924DD5B023B0FAB8DAB2CCEAF48
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAFI02000186 EMBL· GenBank· DDBJ | EAL61488.1 EMBL· GenBank· DDBJ | Genomic DNA |