A0A524GJV0 · A0A524GJV0_UNCDU
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids398 (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
- 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 | 109 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 110 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 146 | substrate | ||||
Sequence: T | ||||||
Binding site | 172 | substrate | ||||
Sequence: K | ||||||
Site | 182-183 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 183 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 183 | substrate | ||||
Sequence: T | ||||||
Binding site | 270 | substrate | ||||
Sequence: E | ||||||
Binding site | 393 | substrate | ||||
Sequence: N | ||||||
Binding site | 398 | 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 | |
Molecular Function | methione N-acyltransferase 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 > Thermodesulfobacteriota > Desulfobacteria > Desulfobacterales
Accessions
- Primary accessionA0A524GJV0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023488968 | 1-182 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MKEKLQVAGFKAGAVKAGIRGKDRLDVALIYSVVPAAAAGVFTTSKVKAAPVLLDMEYLQDGKAQAIIVNSGIANACTGKAGMELARGTSRLVAGQLGIADGLVLVSSTGVMGQQLDPAIFSNCMKPLAESLREDGFADVARAMMTTDTVPKTARREVGLSGKKITMLGLAKGAGMIMPNMA | ||||||
Chain | PRO_5023488969 | 183-398 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLSFIVTDAAVNAGVLKKMLQQSVALSFNAVTVDGDTSTNDTVLVLANGQAGNLEIDSLDSEDGRSFRQCLDDLCLDLALQIVKDGEGATKLITVHVKGAASVQEADQAARTVANSSLVKTAFFGEDANWGRIIAALGRCGVAFDPDKVDISFDDVMMVRDGLGLGPEQEKKATLVLKQAAFPVVIDLKNGQAEAKVYTCDLSVDYIRINADYRS |
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains.
Structure
Sequence
- Sequence statusComplete
- Length398
- Mass (Da)41,758
- Last updated2019-10-16 v1
- Checksum97F331382A36DABB