A0A238FCM3 · A0A238FCM3_9BASI
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids450 (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 | 149 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 150 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 188 | substrate | |||
Binding site | 214 | substrate | |||
Site | 228-229 | Cleavage; by autolysis | |||
Active site | 229 | Nucleophile | |||
Binding site | 229 | substrate | |||
Binding site | 317 | substrate | |||
Binding site | 447 | 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
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
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Microbotryomycetes > Microbotryales > Microbotryaceae > Microbotryum
Accessions
- Primary accessionA0A238FCM3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5023537306 | 1-228 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_5023537305 | 229-450 | 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
Interaction
Structure
Sequence
- Sequence statusComplete
- Length450
- Mass (Da)47,257
- Last updated2017-11-22 v1
- Checksum7DCDDB15C8385666
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FMSP01000005 EMBL· GenBank· DDBJ | SCV70519.1 EMBL· GenBank· DDBJ | Genomic DNA |