Identification |
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Name: | 2-keto-4-pentenoate hydratase |
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Synonyms: | - 2-hydroxypentadienoic acid hydratase
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Gene Name: | mhpD |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in catalytic activity |
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Specific Function: | Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid |
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Cellular Location: | Not Available |
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SMPDB Pathways: | - 2-Oxopent-4-enoate metabolism PW001890
- 2-Oxopent-4-enoate metabolism 2 PW002035
- Collection of Reactions without pathways PW001891
- Phenylalanine metabolism PW000921
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KEGG Pathways: | |
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KEGG Reactions: | | | |
1.0 | ↔ | 1.04-Carboxy-2-oxo-3-hexenedioate | + | 1.0 |
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SMPDB Reactions: | |
1.02-oxopent-4-enoate | + | 1.0 | → | 1.0 | + | 1.04-hydroxy-2-oxopentanoate | + | 1.0 |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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catalytic activity | Process |
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metabolic process |
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Gene Properties |
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Blattner: | b0350 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 8.00 |
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Left Sequence End | 371339 |
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Right Sequence End | 372148 |
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Gene Sequence: | >810 bp
ATGACGAAGCATACTCTTGAGCAACTGGCGGCGGATTTACGCCGCGCCGCAGAGCAGGGC
GAAGCGATTGCACCGCTGCGCGATCTGATTGGTATCGATAACGCTGAAGCGGCTTACGCC
ATTCAGCACATAAATGTGCAACATGACGTTGCGCAGGGGCGTCGCGTGGTAGGGCGTAAA
GTGGGCCTGACACATCCGAAAGTGCAACAACAACTGGGCGTTGATCAACCGGATTTTGGG
ACGTTATTTGCCGACATGTGTTATGGCGATAACGAAATCATTCCTTTTTCCCGTGTTCTG
CAACCCCGCATTGAAGCGGAGATCGCACTGGTGTTGAACCGCGATTTGCCCGCAACCGAT
ATCACCTTCGACGAATTGTATAACGCCATTGAATGGGTACTTCCGGCGCTGGAAGTGGTG
GGGAGCCGCATTCGCGACTGGTCGATTCAGTTTGTCGATACCGTGGCAGATAACGCCTCC
TGTGGGGTGTATGTCATCGGCGGTCCGGCGCAACGTCCGGCGGGGTTAGACCTGAAAAAC
TGCGCCATGAAGATGACGCGTAATAACGAAGAGGTTTCTAGCGGGCGCGGCAGCGAATGC
CTGGGACATCCGCTTAATGCGGCCGTCTGGCTGGCACGCAAAATGGCCAGTCTGGGTGAA
CCGCTGCGCACCGGAGATATCATTCTTACCGGGGCATTAGGTCCGATGGTGGCGGTGAAT
GCGGGCGATCGTTTTGAAGCCCATATTGAAGGCATAGGTTCAGTTGCTGCGACATTTTCA
AGCGCAGCCCCAAAAGGAAGTCTGTCATGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 269 |
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Protein Molecular Weight: | 28890 |
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Protein Theoretical pI: | 5 |
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PDB File: | 1SV6 |
Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >2-keto-4-pentenoate hydratase
MTKHTLEQLAADLRRAAEQGEAIAPLRDLIGIDNAEAAYAIQHINVQHDVAQGRRVVGRK
VGLTHPKVQQQLGVDQPDFGTLFADMCYGDNEIIPFSRVLQPRIEAEIALVLNRDLPATD
ITFDELYNAIEWVLPALEVVGSRIRDWSIQFVDTVADNASCGVYVIGGPAQRPAGLDLKN
CAMKMTRNNEEVSSGRGSECLGHPLNAAVWLARKMASLGEPLRTGDIILTGALGPMVAVN
AGDRFEAHIEGIGSVAATFSSAAPKGSLS |
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References |
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External Links: | |
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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
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