Identification
Name:2-keto-4-pentenoate hydratase
Synonyms:
  • 2-hydroxypentadienoic acid hydratase
Gene Name:mhpD
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb
1.0Thumb1.04-Carboxy-2-oxo-3-hexenedioate+1.0Thumb
1.04-Carboxy-4-hydroxy-2-oxoadipate ↔ 1.04-Carboxy-2-oxo-3-hexenedioate + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb1.0Thumb
SMPDB Reactions:
1.02-oxopent-4-enoate+1.0Thumb1.0Thumb+1.04-hydroxy-2-oxopentanoate+1.0Thumb
1.02-oxopent-4-enoate + 1.02-Hydroxy-2,4-pentadienoate → 1.0Water + 1.04-hydroxy-2-oxopentanoate + 1.04-Hydroxy-2-oxopentanoate
ReactionCard
Complex Reactions:
1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB200412-Hydroxy-2,4-pentadienoateMetaboCard
ECMDB200442-Hydroxy-cis-hex-2,4-dienoateMetaboCard
ECMDB200874-Carboxy-4-hydroxy-2-oxoadipateMetaboCard
ECMDB200894-Hydroxy-2-oxohexanoic acidMetaboCard
ECMDB200904-Hydroxy-2-oxopentanoateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
Process
metabolic process
Gene Properties
Blattner:b0350
Gene OrientationClockwise
Centisome Percentage:8.00
Left Sequence End371339
Right Sequence End372148
Gene Sequence:
>810 bp
ATGACGAAGCATACTCTTGAGCAACTGGCGGCGGATTTACGCCGCGCCGCAGAGCAGGGC
GAAGCGATTGCACCGCTGCGCGATCTGATTGGTATCGATAACGCTGAAGCGGCTTACGCC
ATTCAGCACATAAATGTGCAACATGACGTTGCGCAGGGGCGTCGCGTGGTAGGGCGTAAA
GTGGGCCTGACACATCCGAAAGTGCAACAACAACTGGGCGTTGATCAACCGGATTTTGGG
ACGTTATTTGCCGACATGTGTTATGGCGATAACGAAATCATTCCTTTTTCCCGTGTTCTG
CAACCCCGCATTGAAGCGGAGATCGCACTGGTGTTGAACCGCGATTTGCCCGCAACCGAT
ATCACCTTCGACGAATTGTATAACGCCATTGAATGGGTACTTCCGGCGCTGGAAGTGGTG
GGGAGCCGCATTCGCGACTGGTCGATTCAGTTTGTCGATACCGTGGCAGATAACGCCTCC
TGTGGGGTGTATGTCATCGGCGGTCCGGCGCAACGTCCGGCGGGGTTAGACCTGAAAAAC
TGCGCCATGAAGATGACGCGTAATAACGAAGAGGTTTCTAGCGGGCGCGGCAGCGAATGC
CTGGGACATCCGCTTAATGCGGCCGTCTGGCTGGCACGCAAAATGGCCAGTCTGGGTGAA
CCGCTGCGCACCGGAGATATCATTCTTACCGGGGCATTAGGTCCGATGGTGGCGGTGAAT
GCGGGCGATCGTTTTGAAGCCCATATTGAAGGCATAGGTTCAGTTGCTGCGACATTTTCA
AGCGCAGCCCCAAAAGGAAGTCTGTCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:269
Protein Molecular Weight:28890
Protein Theoretical pI:5
PDB File:1SV6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-keto-4-pentenoate hydratase
MTKHTLEQLAADLRRAAEQGEAIAPLRDLIGIDNAEAAYAIQHINVQHDVAQGRRVVGRK
VGLTHPKVQQQLGVDQPDFGTLFADMCYGDNEIIPFSRVLQPRIEAEIALVLNRDLPATD
ITFDELYNAIEWVLPALEVVGSRIRDWSIQFVDTVADNASCGVYVIGGPAQRPAGLDLKN
CAMKMTRNNEEVSSGRGSECLGHPLNAAVWLARKMASLGEPLRTGDIILTGALGPMVAVN
AGDRFEAHIEGIGSVAATFSSAAPKGSLS
References
External Links:
ResourceLink
Uniprot ID:P77608
Uniprot Name:MHPD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674492
PDB ID:1SV6
Ecogene ID:EG14274
Ecocyc:EG14274
ColiBase:b0350
Kegg Gene:b0350
EchoBASE ID:EB4022
CCDB:MHPD_ECOLI
BacMap:90111116
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
  • Ferrandez, A., Garcia, J. L., Diaz, E. (1997). "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12." J Bacteriol 179:2573-2581. Pubmed: 9098055
  • 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
  • Pollard, J. R., Bugg, T. D. (1998). "Purification, characterisation and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli." Eur J Biochem 251:98-106. Pubmed: 9492273