| Standard Name | HIS7 1, 2 |
|---|---|
| Systematic Name | YBR248C |
| Feature Type | ORF, Verified |
| Description | Imidazole glycerol phosphate synthase (glutamine amidotransferase:cyclase), catalyzes the fifth step of histidine biosynthesis and also produces 5-aminoimidazole-4-carboxamide ribotide (AICAR), a purine precursor (1, 3, 4 and see Summary Paragraph) |
| Name Description | HIStidine requiring 1 |
| Chromosomal Location | |
|---|---|
| Note: this feature is encoded on the Crick strand. | |
| Genetic position: 146 cM |
Gene Ontology Annotations All HIS7 GO evidence and references
| View Computational GO annotations for HIS7 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Pathways |
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Mutant phenotypes All HIS7 Phenotype evidence and references
| Classical genetics | |
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| null | |
| unspecified | |
| Large-scale survey | |
| null |
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| Resources |
interactions All HIS7 Interaction evidence and references
| 13 total interaction(s) for 10 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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Expression Summary
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| Resources |
Protein Information All HIS7 Protein evidence and references
| Localization | |
|---|---|
| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Genetic position: 146 cM | |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1997-01-28 | ||||||||||||
| Subfeature details |
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| Retrieve sequences | |||||||||||||
Analyze Sequence
| S288C only | |
|---|---|
| S288C vs. other species | |
| S288C vs. other strains |
Resources
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000452 |
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SUMMARY PARAGRAPH for HIS7
HIS7 encodes imidazoleglycerol-phosphate synthase, also called glutamine amidotransferase:cyclase, which catalyzes the fifth step in histidine biosynthesis (5, 4). The biosynthesis of histidine has been most extensively studied in Salmonella typhimurium and E. coli. The reactions and enzymes involved in histidine biosynthesis have been identified in many organisms, and are thoroughly reviewed in Alifano et al. (4). Mutations in HIS7, as well as in genes encoding other histidine biosynthetic enzymes, cause histidine auxotrophy and sensitivity to copper, cobalt, and nickel salts (6). The transcription factors Bas1p and Pho2p activate HIS7 transcription (7).
References cited on this page View Complete Literature Guide for HIS7
| 1) | Kuenzler M, et al. (1993) Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: cyclase from Saccharomyces cerevisiae. J Bacteriol 175(17):5548-58 |
| 2) | Plotkin, D.J. (1978) Commitment to meiotic recombination: a temporal analysis. Ph.D Thesis |
| 3) | Chittur SV, et al. (2000) Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae. Protein Expr Purif 18(3):366-77 |
| 4) | Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 |
| 5) | Fani R, et al. (1997) Paralogous histidine biosynthetic genes: evolutionary analysis of the Saccharomyces cerevisiae HIS6 and HIS7 genes. Gene 197(1-2):9-17 |
| 6) | Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9 |
| 7) | Springer C, et al. (1996) Amino acid and adenine cross-pathway regulation act through the same 5'-TGACTC-3' motif in the yeast HIS7 promoter. J Biol Chem 271(47):29637-43 |





