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
Functions
metal ion binding / porphobilinogen synthase activity / zinc ion binding
Processes
heme biosynthetic process / protoporphyrinogen IX biosynthetic process
Components
cytosol
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
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
ResourceLink
UniProtKB IDP0ACB2
UniProtKB Entry NameHEM2_ECOLI
GenBank Protein ID450371
GenBank Gene IDM24488
General References
  1. Li JM, Russell CS, Cosloy SD: The structure of the Escherichia coli hemB gene. Gene. 1989 Jan 30;75(1):177-84. [PubMed:2656410]
  2. 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. [PubMed:2464127]
  3. 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. [PubMed:9278503]
  4. 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. [PubMed:16738553]
  5. 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. [PubMed:8439296]
  6. 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. [PubMed:7592604]
  7. 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. [PubMed:10194344]
  8. 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. [PubMed:11444968]
  9. 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. [PubMed:11909869]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB022604-Oxosebacic AcidexperimentalunknownDetails
DB04530S,S-(2-Hydroxyethyl)ThiocysteineexperimentalunknownDetails
DB045604,7-Dioxosebacic AcidexperimentalunknownDetails