A0A172YA69 · A0A172YA69_9GAMM
- ProteinImidazole glycerol phosphate synthase subunit HisH
- GenehisH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids212 (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 | 82 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 192 | |||||
Sequence: H | ||||||
Active site | 194 | |||||
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Halotalea
Accessions
- Primary accessionA0A172YA69
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-208 | Glutamine amidotransferase | ||||
Sequence: VIDYGMGNLHSVAKALEHVTEERIAITRDPRAIKGATRVVLPGQGAIRDCIGELERTELTGLVKTLLADGDKPLLGICVGQQMLMEKSEENGGVRCLGYLEGEVKRFPADMVEHGERLKVPHMGWNQVEQHHMHPLWEGIPTGDRFYFVHSYYVAASHDAEVFGTVRYGDVVAHVATGRDATFAVQFHPEKSAAMGLRLLANFV |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length212
- Mass (Da)23,387
- Last updated2016-09-07 v1
- ChecksumB138E995D01F8508
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP015243 EMBL· GenBank· DDBJ | ANF56119.1 EMBL· GenBank· DDBJ | Genomic DNA |