A0A534W059 · A0A534W059_UNCDE
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids695 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
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
- N-acetyl-L-glutamate + ATP = N-acetyl-L-glutamyl 5-phosphate + ADP
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.
Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 2/4.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 105 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 106 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 141 | substrate | |||
Binding site | 167 | substrate | |||
Site | 177-178 | Cleavage; by autolysis | |||
Active site | 178 | Nucleophile | |||
Binding site | 178 | substrate | |||
Binding site | 264 | substrate | |||
Binding site | 389 | substrate | |||
Binding site | 394 | substrate | |||
Site | 440 | Transition state stabilizer | |||
Binding site | 475-476 | substrate | |||
Binding site | 497 | substrate | |||
Binding site | 594 | substrate | |||
Site | 653 | Transition state stabilizer | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acetylglutamate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | glutamate N-acetyltransferase activity | |
Molecular Function | L-glutamate N-acetyltransferase activity | |
Biological Process | arginine biosynthetic process via ornithine | |
Biological Process | ornithine biosynthetic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
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 > Myxococcota > Myxococcia
Accessions
- Primary accessionA0A534W059
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5023233558 | 1-177 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_5023233559 | 178-695 | Arginine biosynthesis bifunctional protein ArgJ beta chain | ||
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 436-672 | Aspartate/glutamate/uridylate kinase | |||
Sequence similarities
Belongs to the ArgJ family.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length695
- Mass (Da)72,008
- Last updated2019-10-16 v1
- MD5 ChecksumC971E248E72213A03B62FC91B75A2936
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VBKO01000212 EMBL· GenBank· DDBJ | TMB04868.1 EMBL· GenBank· DDBJ | Genomic DNA |