Difference between revisions of "YBR248C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000452 YBR248C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000452 YBR248C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HIS7 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HIS7 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr II:716460..714802
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|nowrap| Chr II:716465..714807
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000452
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000452
 
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'''Description of YBR248C:''' Imidazole glycerol phosphate synthase (glutamine amidotransferase:cyclase), catalyzes the fifth and sixth steps of histidine biosynthesis and also produces 5-aminoimidazole-4-carboxamide ribotide (AICAR), a purine precursor<ref name='S000044976'>Chittur SV, et al. (2000) Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae. Protein Expr Purif 18(3):366-77 {{SGDpaper|S000044976}} PMID 10733892</ref><ref name='S000055916'>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 {{SGDpaper|S000055916}} PMID 8366040</ref><ref name='S000057959'>Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69
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'''Description of YBR248C:''' 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<ref name='S000057959'>Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 {{SGDpaper|S000057959}} PMID 8852895</ref><ref name='S000044976'>Chittur SV, et al. (2000) Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae. Protein Expr Purif 18(3):366-77 {{SGDpaper|S000044976}} PMID 10733892</ref><ref name='S000055916'>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
{{SGDpaper|S000057959}} PMID 8852895</ref>
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{{SGDpaper|S000055916}} PMID 8366040</ref>
 
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Latest revision as of 14:05, 26 June 2012

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Systematic name YBR248C
Gene name HIS7
Aliases
Feature type ORF, Verified
Coordinates Chr II:716465..714807
Primary SGDID S000000452


Description of YBR248C: 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][2][3]




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References

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  1. Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 SGD PMID 8852895
  2. Chittur SV, et al. (2000) Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae. Protein Expr Purif 18(3):366-77 SGD PMID 10733892
  3. 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 SGD PMID 8366040

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