A0A1F2P2U1 · A0A1F2P2U1_9EURY
- ProteinArginine biosynthesis bifunctional protein ArgJ
- GeneargJ
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids249 (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
- 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 binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 2 | substrate | ||||
Sequence: T | ||||||
Binding site | 27 | substrate | ||||
Sequence: K | ||||||
Site | 37-38 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 38 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 38 | substrate | ||||
Sequence: T | ||||||
Binding site | 117 | substrate | ||||
Sequence: E | ||||||
Binding site | 244 | substrate | ||||
Sequence: N | ||||||
Binding site | 249 | 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
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
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinales incertae sedis > ANME-2 cluster > Candidatus Syntrophoarchaeum
Accessions
- Primary accessionA0A1F2P2U1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023464213 | 1-37 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MTTDTYPKEVAVEIKGSRRFVIGGVAKGAGMIAPDMA | ||||||
Chain | PRO_5023464214 | 38-249 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLAFIYTDASFDSETLQDALRMAVDRSFNMTIVDGDMSTNDMVILTSTGKRSGLRMEEFQEGLNCVCEHLARMIASDGEGATRLIEVLVKGAETKDDAVKAVKTILRSPLVKTAIFGGDPNWGRIACAIGYSGASVSEKKLSISISDGRNEADLLSCGRALDEAVTDLASEILKGETIRIIVDLGLGGEEAKGWGCDLSYEYVRINAEYTS |
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Length249
- Mass (Da)26,714
- Last updated2017-01-18 v1
- ChecksumC3E0567ED9C48C01
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LYOR01000016 EMBL· GenBank· DDBJ | OFV65478.1 EMBL· GenBank· DDBJ | Genomic DNA |