A0A7J7C9J6 · A0A7J7C9J6_TRIWF
- ProteinImidazole glycerol phosphate synthase hisHF
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids584 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
Catalytic activity
- 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamate + H+
Pathway
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 133 | For GATase activity | |||
Active site | 133 | Nucleophile | |||
Binding site | 133 | L-glutamine (UniProtKB | ChEBI); covalent | |||
Active site | 238 | ||||
Active site | 238 | For GATase activity | |||
Active site | 240 | ||||
Active site | 240 | For GATase activity | |||
Active site | 281 | ||||
Binding site | 368 | substrate | |||
Active site | 439 | ||||
Binding site | 504 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | glutaminase activity | |
Molecular Function | imidazoleglycerol-phosphate synthase activity | |
Molecular Function | oxo-acid-lyase activity | |
Biological Process | glutamine metabolic process | |
Biological Process | L-histidine biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameImidazole glycerol phosphate synthase hisHF
Including 2 domains:
- Recommended nameGlutaminase
- EC number
- Recommended nameCyclase
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Celastrales > Celastraceae > Tripterygium
Accessions
- Primary accessionA0A7J7C9J6
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 58-254 | Glutamine amidotransferase | |||
Region | 400-401 | PRFAR binding | |||
Region | 437-439 | PRFAR binding | |||
Region | 509-510 | PRFAR binding | |||
Region | 535-536 | PRFAR binding | |||
Region | 558-559 | PRFAR binding | |||
Sequence similarities
Belongs to the HisA/HisF family.
In the C-terminal section; belongs to the HisA/HisF family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length584
- Mass (Da)63,678
- Last updated2021-04-07 v1
- MD5 ChecksumFA4AE03128AD4DAC33201AA1D776336B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAAARO010000019 EMBL· GenBank· DDBJ | KAF5730537.1 EMBL· GenBank· DDBJ | Genomic DNA |