HIS6/YIL020C Summary 
| Standard Name | HIS6 1 |
|---|---|
| Systematic Name | YIL020C |
| Feature Type | ORF, Verified |
| Description | Phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxiamide isomerase, catalyzes the fourth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts (1, 2, 3 and see Summary Paragraph) |
| Name Description | HIStidine requiring 1 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
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| Genetic position: -17 cM |
Gene Ontology Annotations All HIS6 GO evidence and references
| View Computational GO annotations for HIS6 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| High-throughput |
| Pathways |
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Mutant phenotypes All HIS6 Phenotype evidence and references
| Classical genetics | |
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| unspecified | |
| Large-scale survey | |
| null |
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| Resources |
interactions All HIS6 Interaction evidence and references
| 15 total interaction(s) for 15 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 HIS6 Protein evidence and references
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Genetic position: -17 cM | |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1994-12-10 | ||||||||||||
| Subfeature details |
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| Retrieve sequences | |||||||||||||
Analyze Sequence
| S288C only | |
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| 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 | S000001282 |
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SUMMARY PARAGRAPH for HIS6
HIS6 encodes N-(5'-phospho-D-ribosylformimino)-5-amino-1-(5''-phosphoribosyl)-4-imidazole carboxamide isomerase, which catalyzes the fourth step in histidine biosynthesis (1, 3). 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. (3). Mutations in HIS6, as well as in genes encoding other histidine biosynthetic enzymes, cause histidine auxotrophy and sensitivity to copper, cobalt, and nickel salts (2).
Last updated: 1999-11-12 
References cited on this page View Complete Literature Guide for HIS6
| 1) | 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 |
| 2) | 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 |
| 3) | Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 |
