A0A2V3J7U3 · A0A2V3J7U3_UNCME
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids403 (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 | 107 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 108 | 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 | 168 | 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 | 261 | substrate | ||||
Sequence: E | ||||||
Binding site | 399 | substrate | ||||
Sequence: N |
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 |
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
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanophagales
Accessions
- Primary accessionA0A2V3J7U3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023430046 | 1-182 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MEELRGGICAVPGVRAYGLRENNKGLALIEGKGKAVGMFTKNKMKAAPLIFTQRLLLETGRIGAIIANSGCANSFTGEEGMRNANRMAELASAALGIDKSEVAVASTGPIGKQLDIGMIERQVQEVAKRLTSDPEGSTAAAKAIMTTDTFPKELAIKVGDVTIGGIAKGSGMIYPHLHLATA | ||||||
Chain | PRO_5023430045 | 183-403 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLAFIYTDAELDVGTMRTCLKDACDNSFNMIVVDGDMSTNDMVLLVSRGGEAISEEDFKAGLNYLCKALAKMIARDGEGATKFIEVNVSLRGAPVEDAKLIAREILRSPLVKSAIFGERIDLACGRIIAAIGSCIGTNTSSNSIEVVSMKFRGKEREVEVVRNGRILSTWNREVMKGKEIAIDIVLDVGEEEGKVEEEATATAWGCDLSCDYVMLNASML |
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains.
Structure
Sequence
- Sequence statusComplete
- Length403
- Mass (Da)42,985
- Last updated2018-09-12 v1
- Checksum4F8C52ED75953B7E