HIS7/YBR248C Summary Help

Standard Name HIS7 1, 2
Systematic Name YBR248C
Feature Type ORF, Verified
Description Imidazole glycerol phosphate synthase; glutamine amidotransferase:cyclase that 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
ChrII:716465 to 714807 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
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
Regulators 3 genes
Resources
Pathways
Classical genetics
null
unspecified
Large-scale survey
null
Resources
15 total interaction(s) for 10 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Affinity Capture-RNA: 1

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 2
  • Synthetic Growth Defect: 4
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 552
Molecular Weight (Da) 61,068
Isoelectric Point (pI) 5.24
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrII:716465 to 714807 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: 146 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1659 716465..714807 2011-02-03 1997-01-28
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
Primary SGDIDS000000452
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).

Last updated: 1999-11-12 Contact SGD

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