Porphobilinogen deaminase

Details

Name
Porphobilinogen deaminase
Synonyms
  • 2.5.1.61
  • HMBS
  • Hydroxymethylbilane synthase
  • PBG
  • popE
  • Pre-uroporphyrinogen synthase
Gene Name
hemC
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0003486|Porphobilinogen deaminase
MLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDTPLAKVGGKG
LFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALP
AGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLE
SRIRAALPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERAMNTRLEG
GCQVPIGSYAELIDGEIWLRALVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAR
EILAEVYNGDAPA
Number of residues
313
Molecular Weight
33851.43
Theoretical pI
5.12
GO Classification
Functions
hydroxymethylbilane synthase activity
Processes
heme biosynthetic process / peptidyl-pyrromethane cofactor linkage / protoporphyrinogen IX biosynthetic process / tetrapyrrole biosynthetic process
Components
cytoplasm / cytosol
General Function
Hydroxymethylbilane synthase activity
Specific Function
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0020562|Porphobilinogen deaminase (hemC)
ATGTTAGACAATGTTTTAAGAATTGCCACACGCCAAAGCCCACTTGCACTCTGGCAGGCA
CACTATGTCAAAGACAAGTTGATGGCGAGCCATCCGGGCCTGGTCGTTGAACTGGTACCG
ATGGTGACGCGCGGCGATGTGATTCTTGATACGCCGCTGGCGAAAGTAGGCGGAAAAGGC
TTATTTGTAAAAGAGCTGGAAGTCGCGCTCCTCGAAAATCGCGCCGATATCGCCGTACAC
TCAATGAAAGATGTGCCGGTTGAATTCCCGCAAGGTCTGGGACTGGTCACTATTTGTGAG
CGTGAAGATCCTCGCGATGCCTTTGTGTCCAATAACTATGACAGTCTGGATGCGTTACCG
GCAGGCAGTATCGTCGGGACGTCCAGTTTACGTCGCCAGTGCCAACTGGCTGAACGCCGT
CCGGATCTGATTATCCGCTCCCTGCGCGGCAACGTCGGCACTCGCCTGAGCAAACTGGAT
AACGGCGAATACGATGCCATCATTCTTGCCGTAGCCGGACTAAAACGTTTAGGTCTGGAG
TCACGTATTCGCGCCGCGTTGCCACCCGAGATTTCTCTTCCGGCGGTAGGACAAGGTGCG
GTGGGTATTGAATGCCGCCTTGATGATTCACGCACTCGCGAGCTGCTTGCCGCGCTGAAT
CACCACGAAACTGCACTGCGCGTTACCGCAGAACGCGCCATGAATACCCGTCTCGAAGGC
GGATGTCAGGTGCCAATTGGTAGCTACGCCGAGCTTATTGATGGCGAAATCTGGCTGCGT
GCGCTGGTCGGCGCGCCGGACGGTTCGCAGATTATTCGCGGTGAACGCCGCGGTGCGCCG
CAAGATGCCGAACAAATGGGGATTTCGCTGGCAGAAGAGCTACTGAATAACGGCGCGCGC
GAGATCCTCGCTGAAGTCTATAACGGAGACGCCCCGGCATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP06983
UniProtKB Entry NameHEM3_ECOLI
GenBank Protein ID41664
GenBank Gene IDX04242
General References
  1. Thomas SD, Jordan PM: Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12. Nucleic Acids Res. 1986 Aug 11;14(15):6215-26. [Article]
  2. Alefounder PR, Abell C, Battersby AR: The sequence of hemC, hemD and two additional E. coli genes. Nucleic Acids Res. 1988 Oct 25;16(20):9871. [Article]
  3. Daniels DL, Plunkett G 3rd, Burland V, Blattner FR: Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science. 1992 Aug 7;257(5071):771-8. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G 3rd, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL: Escherichia coli K-12: a cooperatively developed annotation snapshot--2005. Nucleic Acids Res. 2006 Jan 5;34(1):1-9. Print 2006. [Article]
  6. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  7. Trotot P, Sismeiro O, Vivares C, Glaser P, Bresson-Roy A, Danchin A: Comparative analysis of the cya locus in enterobacteria and related gram-negative facultative anaerobes. Biochimie. 1996;78(4):277-87. [Article]
  8. Jordan PM, Thomas SD, Warren MJ: Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12. Biochem J. 1988 Sep 1;254(2):427-35. [Article]
  9. Miller AD, Hart GJ, Packman LC, Battersby AR: Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242. Biochem J. 1988 Sep 15;254(3):915-8. [Article]
  10. Miller AD, Packman LC, Hart GJ, Alefounder PR, Abell C, Battersby AR: Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase). Biochem J. 1989 Aug 15;262(1):119-24. [Article]
  11. Hadener A, Alefounder PR, Hart GJ, Abell C, Battersby AR: Investigation of putative active-site lysine residues in hydroxymethylbilane synthase. Preparation and characterization of mutants in which (a) Lys-55, (b) Lys-59 and (c) both Lys-55 and Lys-59 have been replaced by glutamine. Biochem J. 1990 Oct 15;271(2):487-91. [Article]
  12. Lander M, Pitt AR, Alefounder PR, Bardy D, Abell C, Battersby AR: Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding. Biochem J. 1991 Apr 15;275 ( Pt 2):447-52. [Article]
  13. Jordan PM, Woodcock SC: 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. 1991 Dec 1;280 ( Pt 2):445-9. [Article]
  14. Louie GV, Brownlie PD, Lambert R, Cooper JB, Blundell TL, Wood SP, Warren MJ, Woodcock SC, Jordan PM: Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site. Nature. 1992 Sep 3;359(6390):33-9. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04517Dipyrromethane CofactorexperimentalunknownDetails