A0A8H6B1W0 · A0A8H6B1W0_9HELO
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids479 (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 | 163 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 164 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 200 | substrate | |||
Binding site | 229 | substrate | |||
Site | 239-240 | Cleavage; by autolysis | |||
Active site | 240 | Nucleophile | |||
Binding site | 240 | substrate | |||
Binding site | 334 | substrate | |||
Binding site | 474 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Sclerotiniaceae > Botrytis
Accessions
- Primary accessionA0A8H6B1W0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5035023926 | 1-239 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_5035023925 | 240-479 | 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
Subunit
Heterodimer of an alpha and a beta chain.
Structure
Sequence
- Sequence statusComplete
- Length479
- Mass (Da)52,002
- Last updated2022-01-19 v1
- MD5 Checksum0E2F4D19758BFC43299AE6B1B8E606F7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JABFCT010000003 EMBL· GenBank· DDBJ | KAF5877580.1 EMBL· GenBank· DDBJ | Genomic DNA |