H1W484 · H1W484_COLHI
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids460 (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 acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
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 | 150 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 151 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 189 | substrate | ||||
Sequence: T | ||||||
Binding site | 218 | substrate | ||||
Sequence: K | ||||||
Site | 228-229 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 229 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 229 | substrate | ||||
Sequence: T | ||||||
Binding site | 316 | substrate | ||||
Sequence: E | ||||||
Binding site | 455 | substrate | ||||
Sequence: N | ||||||
Binding site | 460 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
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 | |
Biological Process | ornithine 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, mitochondrial
- 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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum destructivum species complex
Accessions
- Primary accessionH1W484
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5042300419 | 1-228 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MAQPVRRFPGHLAQFVRCYSVSAESIPAAKKKYVPTEGTYPQGFQASGILVGVKPGNKTKPDLALLSSDRPCAAAAVFTKNKFQAAPVTFSRDLLKKKSNRGIRSVLINSGCANAVTGKGGLEDASLMAHAADKAVGGEGDASSTIVMSTGVIGQRLPIAKIVDNVPAAQGALGSSHKHWLSFATAICTTDTFPKLKSKTFTLPSSPGVEYRIAGTTKGAGMIHPNMA | ||||||
Chain | PRO_5042300418 | 229-460 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TLLGVVATDAPISPAVMPSVLKHAVDRSFNSITIDGDTSTNDTLALLANGAAGGKEIVSEDSADYAAFKEVLTDFSIDLAKLIVRDGEGATKFVTIRVVESASEEAARKIASTIARSPLVKTALYGRDANWGRILCATGYSLVSEPGQAVSDVPEVVPEKTNVSFVPTDGTPELKLLVNGEPEMVDEARASEILELEDLEIIVRLGTGDKEATYWTCDYSHEYITINGDYRT |
Post-translational modification
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Length460
- Mass (Da)48,580
- Last updated2012-03-21 v1
- Checksum0380A43167B3EF15
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CACQ02009568 EMBL· GenBank· DDBJ | CCF47297.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LTAN01000003 EMBL· GenBank· DDBJ | OBR11980.1 EMBL· GenBank· DDBJ | Genomic DNA |