E. coli Genetic Resources at Yale
CGSC, The Coli Genetic Stock Center

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Site hemC

• Name: hemC
• Type: Gene
  Synonyms

  b3805	MG1655 locus tag
  popE

  
  
• Mnemonic: Hemin
• Left End Point: 85.95
• Right End Point: 85.97
  Products:

  porphobilinogen deaminase

  pre-uroporphyrinogen I synthase

  hydroxymethylbilane synthase

  
  
• Direction: <
• Priority: 1
• External Database Links:

  Host Site	Page Links
  NCBI/GenBank	X04242
  EcoGene.org	EG10429
  EcoliWiki	hemC

  
  
• Comment:
  • Selectable phenotype. Loss: plate method. Loss: neomycin resistance. Dir.of transcr. changed from '90 map. encodes N-glycosylase with apurinic/apyrimidinic lyase activity also.
• References:
  • McConville, M.L., H.P. Charles 1979. Mutants of Escherichia coli K12 accumulating porphobilinogen: a new locus, hemC. J.Gen.Microbiol. 111:193-200
  
  
  • Sasaki, M., T. Fujiyoshi, K. Shimada, Y. Takagi 1982. Fine structure of the recB and recC gene region of Escherichia coli. Biochem.Biophys.Res.Commun. 109:414-422
  
  
  • Thomas, S.D., P.M. Jordan 1986. Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12. Nucleic Acids Res. 14:6215-6226
  
  
  • Jordan, P.M., B.I.A. Mgbeje, A.F. Alwan, S.D. Thomas 1987. Nucleotide sequence of hemD, the second gene in the hem operon of Escherichia coli K-12. Nucleic Acids Res. 15:10583
  
  
  • Sasarman, A., A. Nepveu, Y. Echelard, J. Dymetryszyn, M. Drolet, C. Goyer 1987. Molecular cloning and sequencing of the hemD gene of Escherichia coli K-12 and preliminary data on the Uro operon. J.Bacteriol. 169:4257-4262
  
  
  • Jordan, P.M., S.D. Thomas, M.J. Warren 1988. Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12. Biochem.J. 254:427-435
  
  
  • Alefounder, P.R., C. Abell, A.R. Battersby 1988. The sequence of hemC, hemD and two additional E. coli genes. Nucleic Acids Res. 16:9871
  
  
  • Hadener, A., P.R. Alefounder, G.J. Hart, C. Abell, A.R. Battersby 1990. Investigation of putative active-site lysine residues in hydroxymethylbilane synthase. Biochem.J. 271:487-491
  
  
  • Jordan, P.M., S.C. Woodcock 1991. Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation. Biochem.J. 280:445-4
  
  
  • Daniels, D.L., G. Plunkett, V.D. Burland, F.R. Blattner 1992. Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science 257:771-778
  
  
  • Shoolingin-Jordan, P.M. 1995. Porphobilinogen deaminase and uroporphyrinogen III synthase: structure, molecular biology, and mechanism. J.Bioenerg.Biomembr. 27:181-195
  
  
  • Lu, A.L., D.S. Yuen, J. Cillo 1996. Catalytic mechanism and DNA substrate recognition of Escherichia coli MutY protein. J.Biol.Chem. 271:24138-24143