Q9HNI6 · HIS5_HALSA
- ProteinImidazole glycerol phosphate synthase subunit HisH
- GenehisH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids218 (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 HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 88 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 196 | |||||
Sequence: H | ||||||
Active site | 198 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | glutaminase activity | |
Molecular Function | imidazoleglycerol-phosphate synthase activity | |
Molecular Function | 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 subunit HisH
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Halobacteriaceae > Halobacterium > Halobacterium salinarum NRC-34001
Accessions
- Primary accessionQ9HNI6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000152456 | 1-218 | Imidazole glycerol phosphate synthase subunit HisH | |||
Sequence: MDTTGTGQRGASIVVVDYGLGNLRSVTRGLERASADVSIVGDPGALDDADGIVLPGVGAFGDGMENAGPFRDALTDAADEGRPLFGICLGMQMLLSSSEEADHEGQGDARGLDLIPGRNVRFTGTVKVPHMGWNELAVTRDHPLVGGVDGEYAYFVHSYYAAPDDPGHVVAETDYGERFPAVVANDAGNVFGTQFHPEKSGATGLRILRNFVDYCADQ |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-218 | Glutamine amidotransferase type-1 | ||||
Sequence: SIVVVDYGLGNLRSVTRGLERASADVSIVGDPGALDDADGIVLPGVGAFGDGMENAGPFRDALTDAADEGRPLFGICLGMQMLLSSSEEADHEGQGDARGLDLIPGRNVRFTGTVKVPHMGWNELAVTRDHPLVGGVDGEYAYFVHSYYAAPDDPGHVVAETDYGERFPAVVANDAGNVFGTQFHPEKSGATGLRILRNFVDYCADQ |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length218
- Mass (Da)22,959
- Last updated2002-04-16 v2
- Checksum362AE49D90C7881E
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004437 EMBL· GenBank· DDBJ | AAG20234.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |