A0A0D3BR77 · A0A0D3BR77_BRAOL
- ProteinArginine biosynthesis bifunctional protein ArgJ, chloroplastic
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids662 (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
- L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H+
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 | 367 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 368 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 406 | substrate | |||
Binding site | 432 | substrate | |||
Site | 442-443 | Cleavage; by autolysis | |||
Active site | 443 | Nucleophile | |||
Binding site | 443 | substrate | |||
Binding site | 530 | substrate | |||
Binding site | 657 | substrate | |||
Binding site | 662 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | glutamate N-acetyltransferase activity | |
Molecular Function | L-glutamate N-acetyltransferase activity | |
Molecular Function | RNA binding | |
Biological Process | L-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, chloroplastic
- 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
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica
Accessions
- Primary accessionA0A0D3BR77
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5023505351 | 1-442 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_5023505352 | 443-662 | Arginine biosynthesis bifunctional protein ArgJ beta chain | ||
Keywords
- PTM
Interaction
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length662
- Mass (Da)70,135
- Last updated2015-04-29 v1
- MD5 ChecksumC41BB92FABF865E236A78BE1E1743CD4
Keywords
- Technical term