Q9X0C6 · HIS6_THEMA
- ProteinImidazole glycerol phosphate synthase subunit HisF
- GenehisF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids253 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Catalytic activity
- 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H+ + L-glutamate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.5 μM | PRFAR | |||||
2.2 mM | NH3 |
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 | 11 | |||||
Sequence: D | ||||||
Active site | 130 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | imidazoleglycerol-phosphate synthase activity | |
Molecular Function | lyase activity | |
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 HisF
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermotogota > Thermotogae > Thermotogales > Thermotogaceae > Thermotoga
Accessions
- Primary accessionQ9X0C6
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 9 | No change in activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 11 | Loss of activity. | ||||
Sequence: D → X | ||||||
Mutagenesis | 19 | Decrease in activity. | ||||
Sequence: K → S | ||||||
Mutagenesis | 51 | No change in activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 103 | No change in activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 130 | Complete loss of activity. | ||||
Sequence: D → A, C, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, or Y | ||||||
Mutagenesis | 130 | Weak activity. | ||||
Sequence: D → E | ||||||
Mutagenesis | 176 | Decrease in activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 183 | No change in activity. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000142253 | 1-253 | Imidazole glycerol phosphate synthase subunit HisF | |||
Sequence: MLAKRIIACLDVKDGRVVKGTNFENLRDSGDPVELGKFYSEIGIDELVFLDITASVEKRKTMLELVEKVAEQIDIPFTVGGGIHDFETASELILRGADKVSINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTGILLRDWVVEVEKRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIASGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYLKKHGVNVRLEGL |
Proteomic databases
Interaction
Subunit
Heterodimer of HisH and HisF.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9X0C6 | hisH Q9X0C8 | 2 | EBI-9026911, EBI-9026913 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length253
- Mass (Da)27,719
- Last updated1999-11-01 v1
- ChecksumFE0F97F0C57E9025
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000512 EMBL· GenBank· DDBJ | AAD36113.1 EMBL· GenBank· DDBJ | Genomic DNA |