A0A9X7UII6 · A0A9X7UII6_SPHYA
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids408 (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 | 120 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 121 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 156 | substrate | ||||
Sequence: T | ||||||
Binding site | 182 | substrate | ||||
Sequence: K | ||||||
Site | 192-193 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 193 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 193 | substrate | ||||
Sequence: T | ||||||
Binding site | 280 | substrate | ||||
Sequence: E | ||||||
Binding site | 403 | substrate | ||||
Sequence: N | ||||||
Binding site | 408 | substrate | ||||
Sequence: S |
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
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium
Accessions
- Primary accessionA0A9X7UII6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5041027703 | 1-192 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MTDRSPLAPAAFPALPAIAGVTLRVAKARYKNWDRCDLTYVELDAGTAVAGVTTQSKCPSPEVEWCRDAIPMGQARAVVVNAGNANAFTGHRGRAAVEAIAAKVANHLSCQPSDIFVSSTGVIGVPLPIDKAEAGLEAAFVAAPCGWEDAANTIGTTDTYAKGAHVSAMIGDTRVDLVGIIKGSGMIAPDMA | ||||||
Chain | PRO_5041027704 | 193-408 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLGYIFTDAAIDPALLQQILSAANKRTFSCITVDSDTSTSDTVLAFATGKAGNAPLVSMDDAGADAFAAALSDLCRQLAHLVVRDGEGASKFIEITVEGAESDASAHRIALSIANSPLVKTAIAGEDANWGRVVMAVGKAGEPAERDKLAIRFGATQVAAGGLALDGYDEAPVAAHLKGQDIVIGVDIGLGEGRATVWTCDLTHGYISINADYRS |
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains.
Structure
Sequence
- Sequence statusComplete
- Length408
- Mass (Da)41,998
- Last updated2023-11-08 v1
- ChecksumD74B84152CF523ED