A0A355M5N1 · A0A355M5N1_9BACT
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids410 (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
- 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 | 118 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 119 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 155 | substrate | ||||
Sequence: T | ||||||
Binding site | 181 | substrate | ||||
Sequence: K | ||||||
Site | 196-197 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 197 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 197 | substrate | ||||
Sequence: T | ||||||
Binding site | 283 | substrate | ||||
Sequence: E | ||||||
Binding site | 405 | substrate | ||||
Sequence: N | ||||||
Binding site | 410 | substrate | ||||
Sequence: T |
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 > Lentisphaerota > Lentisphaeria
Accessions
- Primary accessionA0A355M5N1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023554014 | 1-196 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MSKISHIQSGSITSPKGFKASGIKCGLKASGSLDMALIFSEKDAVCAGAFTSNLFAAAPVQWCRNKLSTSPFAQAVIINSGNANACTGEQGYKNALEMAKHTAKFLNISHDHVFVASTGRIGVQMPMDKIRDGIESASKNLSAKGGHDSALAIMTTDTKPKETAVSFQIDGNTVTLAGMVKGAGMIAPSMNTHPHA | ||||||
Chain | PRO_5023554013 | 197-410 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLCFITTDANVSPEFLSSALNDAVENSFNKISVDGDMSTNDTVIVLANGMSGTAMLKGNCEDSKMFADALKAVTSDLARKIVMDGEGATKFVTVEVNGASTLQDAKKCAMAIANSLLCKTAWFGGDPNWGRVIAAAGYSGASFDPDKVNLFYDREQVVRDGGDAGAKEQDLADIIRKKEFTVRLDLNSGAHGFTAWTSDISYEYVKINADYHT |
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains.
Structure
Sequence
- Sequence statusComplete
- Length410
- Mass (Da)43,350
- Last updated2018-11-07 v1
- ChecksumD0CFCAA0166CED4E