A0A941PM80 · A0A941PM80_UNCPS
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids426 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- L-glutamate + N2-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
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 | ||||
Sequence: T | ||||||
Site | 140 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 174 | substrate | ||||
Sequence: T | ||||||
Binding site | 200 | substrate | ||||
Sequence: K | ||||||
Site | 210-211 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 211 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 211 | substrate | ||||
Sequence: T | ||||||
Binding site | 298 | substrate | ||||
Sequence: E | ||||||
Binding site | 421 | substrate | ||||
Sequence: N | ||||||
Binding site | 426 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acetyl-CoA:L-glutamate N-acetyltransferase activity | |
Molecular Function | glutamate N-acetyltransferase activity | |
Biological Process | arginine biosynthetic process |
Keywords
- Molecular function
- Biological process
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 > Pseudomonadota
Accessions
- Primary accessionA0A941PM80
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5038193419 | 1-210 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MDGDNNQCGSIAVSGPAARVSPLAPKRFPDLPAIAGVEAGIGRAGLYKHERPDLLLMRFAAGARAAGVFTTNAVGSAPTDWCKQALSAGRGSVRGILVNAGCANSFTGPAGDAACKRALEAAAAQIGVGGAREMLAASTGVIGVVLDADKIEGALAGIELGPVRWPEAASAIMTTDTFAKGAGATCEIDGVKVSLAGIAKGSGMIAPNMA | ||||||
Chain | PRO_5038193418 | 211-426 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLAFVFTDAALSTPVLKSLLRAETEASFNSITVDGDRSTNDCVLLFATGQAKIPPIADAKDARLDSFRAALGQVLRDLAIQIVRDGEGATKLVAVNVDGAASDASAKAIARTICESPLVKTAIAGGDANWGRIVMAIGRADQPIRREMISVRFGDLFAARDGMIATEYDEGAMSAYMKRDELEISVTVGGGSGRARMYTCDLTKRYVEINGDYRS |
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains.
Structure
Sequence
- Sequence statusComplete
- Length426
- Mass (Da)43,834
- Last updated2023-02-22 v1
- ChecksumE9376834F846DFF7