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
- Functionshydroxymethylbilane synthase activityProcessesheme biosynthetic process / peptidyl-pyrromethane cofactor linkage / protoporphyrinogen IX biosynthetic process / tetrapyrrole biosynthetic processComponentscytoplasm / 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
Resource Link UniProtKB ID P06983 UniProtKB Entry Name HEM3_ECOLI GenBank Protein ID 41664 GenBank Gene ID X04242 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]