A4S1K1 · ARGJ_OSTLU
- ProteinArginine biosynthesis bifunctional protein ArgJ, chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids461 (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 acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Miscellaneous
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
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 | 163 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 164 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 202 | substrate | ||||
Sequence: T | ||||||
Binding site | 228 | substrate | ||||
Sequence: K | ||||||
Site | 238-239 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 239 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 239 | substrate | ||||
Sequence: T | ||||||
Binding site | 326 | substrate | ||||
Sequence: E | ||||||
Binding site | 456 | substrate | ||||
Sequence: N | ||||||
Binding site | 461 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameArginine biosynthesis bifunctional protein ArgJ, chloroplastic
- Cleaved into 2 chains
Including 2 domains:
- Recommended nameGlutamate N-acetyltransferase
- EC number
- Short namesGAT
- Alternative names
- Recommended nameAmino-acid acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > Mamiellophyceae > Mamiellales > Bathycoccaceae > Ostreococcus
Accessions
- Primary accessionA4S1K1
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000397982 | 1-238 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MTSRGRARASDRRARGAVVASGKIDFTDAGCFELPYAPVAEALLPEGPWKVVEGGVCAAKGFKVAGYKAGLRAKGTRADCALIVADEDATCAGIFTTNIMCAAPVTYCKKQLAGKPTARALLINAAQANAATGDQGAADAQATAEELSKSLGVAEEDILLMSTGVIGKRIKLDKLMPAIPILSANVESSTAAANAAATAICTTDLVRKTVAIEVQIGGKTVCMGGMAKGSGMIHPNMA | ||||||
Chain | PRO_0000397983 | 239-461 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLGVVTCDADVTPEVWRNITSRAGAASFNQISVDGDTSTNDSLVCFASGKAGNAKITSVDSAEGKLLEQALTAVCRGLAKAIAWDGEGATCLIECNVSGAADDEDARVIARSVVCSSLAKAAIFGHDPNWGRLACAAGYAAPVKNRFDQNDLKLSLGPHQLMDKGQPLDFDAVAASRYLKEVTGVHGTCVVDISVGNGSGRGQAWGCDLSYDYVKINAEYTT |
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length461
- Mass (Da)47,495
- Last updated2007-05-15 v1
- Checksum8D45526E26E951CB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000588 EMBL· GenBank· DDBJ | ABO97456.1 EMBL· GenBank· DDBJ | Genomic DNA |