A0A559IPF9 · A0A559IPF9_9BACL
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids428 (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 N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N2-acetylornithine and glutamate.
Miscellaneous
Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
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 | 139 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 140 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 178 | substrate | |||
Binding site | 204 | substrate | |||
Site | 214-215 | Cleavage; by autolysis | |||
Active site | 215 | Nucleophile | |||
Binding site | 215 | substrate | |||
Binding site | 301 | substrate | |||
Binding site | 423 | substrate | |||
Binding site | 428 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- Cleaved into 2 chains
Including 2 domains:
- Recommended nameGlutamate N-acetyltransferase
- EC number
- Alternative names
- Recommended nameAmino-acid acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus
Accessions
- Primary accessionA0A559IPF9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5023468860 | 1-214 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_5023468859 | 215-428 | Arginine biosynthesis bifunctional protein ArgJ beta chain | ||
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains.
Structure
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)44,288
- Last updated2019-10-16 v1
- MD5 ChecksumDC25D2C5E067CB51111A6700886F9A91
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VNJK01000002 EMBL· GenBank· DDBJ | TVX89433.1 EMBL· GenBank· DDBJ | Genomic DNA |