Delta-aminolevulinic acid dehydratase
Details
- Name
- Delta-aminolevulinic acid dehydratase
- Synonyms
- 4.2.1.24
- ALAD
- ncf
- Porphobilinogen synthase
- Gene Name
- hemB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0003964|Delta-aminolevulinic acid dehydratase MTDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMPGVMRIPEKH LAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVARMSRICKQTVPEMIVMSDTC FCEYTSHGHCGVLCEHGVDNDATLENLGKQAVVAAAAGADFIAPSAAMDGQVQAIRQALD AAGFKDTAIMSYSTKFASSFYGPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQG ADCLMVKPAGAYLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGS IKRAGADLIFSYFALDLAEKKILR
- Number of residues
- 324
- Molecular Weight
- 35624.365
- Theoretical pI
- 5.04
- GO Classification
- Functionsmetal ion binding / porphobilinogen synthase activity / zinc ion bindingProcessesheme biosynthetic process / protoporphyrinogen IX biosynthetic processComponentscytosol
- General Function
- Zinc ion binding
- Specific Function
- Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
- Pfam Domain Function
- ALAD (PF00490)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011442|Delta-aminolevulinic acid dehydratase (hemB) ATGACAGACTTAATCCAACGCCCTCGTCGCCTGCGCAAATCTCCTGCGCTGCGCGCTATG TTTGAAGAGACAACACTTAGCCTTAACGACCTGGTGTTGCCGATCTTTGTTGAAGAAGAA ATTGACGACTACAAAGCCGTTGAAGCCATGCCAGGCGTGATGCGCATTCCAGAGAAACAT CTGGCACGCGAAATTGAACGCATCGCCAACGCCGGTATTCGTTCCGTGATGACTTTTGGC ATCTCTCACCATACCGATGAAACCGGCAGCGATGCCTGGCGGGAAGATGGACTGGTGGCG CGTATGTCGCGCATCTGCAAGCAGACCGTGCCAGAAATGATCGTTATGTCAGACACCTGC TTCTGTGAATACACTTCTCACGGTCACTGCGGTGTGCTGTGCGAGCATGGCGTCGACAAC GACGCGACTCTGGAAAATTTAGGCAAGCAAGCCGTGGTTGCAGCTGCTGCAGGTGCAGAC TTCATCGCCCCTTCCGCCGCGATGGACGGCCAGGTACAGGCGATTCGTCAGGCGCTGGAC GCTGCGGGATTTAAAGATACGGCGATTATGTCGTATTCGACCAAGTTCGCCTCCTCCTTT TATGGCCCGTTCCGTGAAGCTGCCGGAAGCGCATTAAAAGGCGACCGCAAAAGCTATCAG ATGAACCCAATGAACCGTCGTGAGGCGATTCGTGAATCACTGCTGGATGAAGCCCAGGGC GCAGACTGCCTGATGGTTAAACCTGCTGGAGCGTACCTCGACATCGTGCGTGAGCTGCGT GAACGTACTGAATTGCCGATTGGCGCGTATCAGGTGAGCGGTGAGTATGCGATGATTAAG TTCGCCGCGCTGGCGGGTGCTATAGATGAAGAGAAAGTCGTGCTCGAAAGCTTAGGTTCG ATTAAGCGTGCGGGTGCGGATCTGATTTTCAGCTACTTTGCGCTGGATTTGGCTGAGAAG AAGATTCTGCGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0ACB2 UniProtKB Entry Name HEM2_ECOLI GenBank Protein ID 450371 GenBank Gene ID M24488 - General References
- Li JM, Russell CS, Cosloy SD: The structure of the Escherichia coli hemB gene. Gene. 1989 Jan 30;75(1):177-84. [Article]
- Echelard Y, Dymetryszyn J, Drolet M, Sasarman A: Nucleotide sequence of the hemB gene of Escherichia coli K12. Mol Gen Genet. 1988 Nov;214(3):503-8. [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]
- 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]
- Spencer P, Jordan PM: Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain. Biochem J. 1993 Feb 15;290 ( Pt 1):279-87. [Article]
- Mitchell LW, Volin M, Jaffe EK: The phylogenetically conserved histidines of Escherichia coli porphobilinogen synthase are not required for catalysis. J Biol Chem. 1995 Oct 13;270(41):24054-9. [Article]
- Erskine PT, Norton E, Cooper JB, Lambert R, Coker A, Lewis G, Spencer P, Sarwar M, Wood SP, Warren MJ, Shoolingin-Jordan PM: X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution. Biochemistry. 1999 Apr 6;38(14):4266-76. [Article]
- Kervinen J, Jaffe EK, Stauffer F, Neier R, Wlodawer A, Zdanov A: Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity. Biochemistry. 2001 Jul 27;40(28):8227-36. [Article]
- Jaffe EK, Kervinen J, Martins J, Stauffer F, Neier R, Wlodawer A, Zdanov A: Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid. J Biol Chem. 2002 May 31;277(22):19792-9. Epub 2002 Mar 21. [Article]