Delta-aminolevulinic acid dehydratase (P0ACB2)

Identification
Name:Delta-aminolevulinic acid dehydratase
Synonyms:
  • ALAD
  • ALADH
  • Porphobilinogen synthase
Gene Name:hemB
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
2.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
2.05-Aminolevulinic acid ↔ 1.0Hydrogen ion + 2.0Water + 1.0Porphobilinogen
ReactionCard
2.0Thumb ↔ 1.0Thumb+2.0Thumb
2.05-Aminolevulinic acid ↔ 1.0Porphobilinogen + 2.0Water
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.05-Aminolevulinic acid ↔ 1.0Hydrogen ion + 1.0Water + 1.0Porphobilinogen
ReactionCard
SMPDB Reactions:
8.0Thumb → 4.0Thumb+8.0Thumb+4.0Thumb
8.05-Aminolevulinic acid → 4.0Hydrogen ion + 8.0Water + 4.0Porphobilinogen
ReactionCard
EcoCyc Reactions:
2.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
2.05-Aminolevulinic acid ↔ 1.0Hydrogen ion + 2.0Water + 1.0Porphobilinogen
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.05-Aminolevulinic acid ↔ 1.0Hydrogen ion + 1.0Water + 1.0Porphobilinogen
ReactionCard
Complex Reactions:
2.0Thumb → 1.0Thumb+2.0Thumb
2.05-Aminolevulinic acid → 1.0Porphobilinogen + 2.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB011495-Aminolevulinic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00245PorphobilinogenMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbon-oxygen lyase activity
catalytic activity
cation binding
hydro-lyase activity
ion binding
lyase activity
metal ion binding
porphobilinogen synthase activity
Process
biosynthetic process
cellular biosynthetic process
heterocycle biosynthetic process
metabolic process
tetrapyrrole biosynthetic process
Gene Properties
Blattner:b0369
Gene OrientationCounterclockwise
Centisome Percentage:8.36
Left Sequence End387977
Right Sequence End388951
Gene Sequence:
>975 bp
ATGACAGACTTAATCCAACGCCCTCGTCGCCTGCGCAAATCTCCTGCGCTGCGCGCTATG
TTTGAAGAGACAACACTTAGCCTTAACGACCTGGTGTTGCCGATCTTTGTTGAAGAAGAA
ATTGACGACTACAAAGCCGTTGAAGCCATGCCAGGCGTGATGCGCATTCCAGAGAAACAT
CTGGCACGCGAAATTGAACGCATCGCCAACGCCGGTATTCGTTCCGTGATGACTTTTGGC
ATCTCTCACCATACCGATGAAACCGGCAGCGATGCCTGGCGGGAAGATGGACTGGTGGCG
CGTATGTCGCGCATCTGCAAGCAGACCGTGCCAGAAATGATCGTTATGTCAGACACCTGC
TTCTGTGAATACACTTCTCACGGTCACTGCGGTGTGCTGTGCGAGCATGGCGTCGACAAC
GACGCGACTCTGGAAAATTTAGGCAAGCAAGCCGTGGTTGCAGCTGCTGCAGGTGCAGAC
TTCATCGCCCCTTCCGCCGCGATGGACGGCCAGGTACAGGCGATTCGTCAGGCGCTGGAC
GCTGCGGGATTTAAAGATACGGCGATTATGTCGTATTCGACCAAGTTCGCCTCCTCCTTT
TATGGCCCGTTCCGTGAAGCTGCCGGAAGCGCATTAAAAGGCGACCGCAAAAGCTATCAG
ATGAACCCAATGAACCGTCGTGAGGCGATTCGTGAATCACTGCTGGATGAAGCCCAGGGC
GCAGACTGCCTGATGGTTAAACCTGCTGGAGCGTACCTCGACATCGTGCGTGAGCTGCGT
GAACGTACTGAATTGCCGATTGGCGCGTATCAGGTGAGCGGTGAGTATGCGATGATTAAG
TTCGCCGCGCTGGCGGGTGCTATAGATGAAGAGAAAGTCGTGCTCGAAAGCTTAGGTTCG
ATTAAGCGTGCGGGTGCGGATCTGATTTTCAGCTACTTTGCGCTGGATTTGGCTGAGAAG
AAGATTCTGCGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:324
Protein Molecular Weight:35624
Protein Theoretical pI:5
PDB File:1I8J
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Delta-aminolevulinic acid dehydratase
MTDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMPGVMRIPEKH
LAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVARMSRICKQTVPEMIVMSDTC
FCEYTSHGHCGVLCEHGVDNDATLENLGKQAVVAAAAGADFIAPSAAMDGQVQAIRQALD
AAGFKDTAIMSYSTKFASSFYGPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQG
ADCLMVKPAGAYLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGS
IKRAGADLIFSYFALDLAEKKILR
References
External Links:
ResourceLink
Uniprot ID:P0ACB2
Uniprot Name:HEM2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674510
PDB ID:1I8J
Ecogene ID:EG10428
Ecocyc:EG10428
ColiBase:b0369
Kegg Gene:b0369
EchoBASE ID:EB0423
CCDB:HEM2_ECOLI
BacMap:90111123
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Echelard, Y., Dymetryszyn, J., Drolet, M., Sasarman, A. (1988). "Nucleotide sequence of the hemB gene of Escherichia coli K12." Mol Gen Genet 214:503-508. Pubmed: 2464127
  • Erskine, P. T., Norton, E., Cooper, J. B., Lambert, R., Coker, A., Lewis, G., Spencer, P., Sarwar, M., Wood, S. P., Warren, M. J., Shoolingin-Jordan, P. M. (1999). "X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution." Biochemistry 38:4266-4276. Pubmed: 10194344
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jaffe, E. K., Kervinen, J., Martins, J., Stauffer, F., Neier, R., Wlodawer, A., Zdanov, A. (2002). "Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid." J Biol Chem 277:19792-19799. Pubmed: 11909869
  • Kervinen, J., Jaffe, E. K., Stauffer, F., Neier, R., Wlodawer, A., Zdanov, A. (2001). "Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity." Biochemistry 40:8227-8236. Pubmed: 11444968
  • Li, J. M., Russell, C. S., Cosloy, S. D. (1989). "The structure of the Escherichia coli hemB gene." Gene 75:177-184. Pubmed: 2656410
  • Mitchell, L. W., Volin, M., Jaffe, E. K. (1995). "The phylogenetically conserved histidines of Escherichia coli porphobilinogen synthase are not required for catalysis." J Biol Chem 270:24054-24059. Pubmed: 7592604
  • Spencer, P., Jordan, P. M. (1993). "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 290 ( Pt 1):279-287. Pubmed: 8439296