| Identification |
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| Name: | 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase |
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| Synonyms: | Not Available |
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| Gene Name: | mhpB |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in iron ion binding |
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| Specific Function: | Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3- dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2- hydroxy-6-ketononatrienedioate, respectively |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | |
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| KEGG Pathways: | - Microbial metabolism in diverse environments ec01120
- Phenylalanine metabolism ec00360
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| KEGG Reactions: | |
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| SMPDB Reactions: | |
1.02-Hydroxy-3-(4-hydroxyphenyl)propenoic acid | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | → | 1.0(2E,4Z)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | |
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| Metabolites: | | ECMDB ID | Name | View |
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| ECMDB24915 | 2-Hydroxy-3-(4-hydroxyphenyl)propenoic acid | MetaboCard | | ECMDB04081 | 2-Hydroxy-6-ketononadienedicarboxylate | MetaboCard | | ECMDB20042 | 2-Hydroxy-6-ketononatrienedioate | MetaboCard | | ECMDB20064 | 3-(2,3-Dihydroxyphenyl)propanoate | MetaboCard | | ECMDB04061 | 3-(2,3-Dihydroxyphenyl)propionic acid | MetaboCard | | ECMDB21225 | Hydrogen ion | MetaboCard | | ECMDB04124 | Oxygen | MetaboCard | | ECMDB20197 | Trans-2,3-Dihydroxycinnamate | MetaboCard |
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| GO Classification: | | Function |
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| binding | | catalytic activity | | cation binding | | ferrous iron binding | | ion binding | | iron ion binding | | metal ion binding | | oxidoreductase activity | | transition metal ion binding | | Process |
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| cellular aromatic compound metabolic process | | cellular metabolic process | | metabolic process |
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| Gene Properties |
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| Blattner: | b0348 |
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| Gene Orientation | Clockwise |
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| Centisome Percentage: | 7.96 |
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| Left Sequence End | 369501 |
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| Right Sequence End | 370445 |
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| Gene Sequence: | >945 bp
ATGCCAGAGGTACAAACAGATCATCCAGAGACGGCGGAGTTAAGCAAACCACAGCTACGC
ATGGTCGATCTCAACTTATTAACCGTTTTCGATGCCGTGATGCAGGAGCAAAACATTACT
CGTGCCGCTCATGTTCTGGGAATGTCGCAACCTGCGGTCAGTAACGCTGTTGCACGCCTG
AAGGTGATGTTTAATGACGAGCTTTTTGTTCGTTATGGCCGTGGTATTCAACCGACTGCT
CGCGCATTTCAACTTTTTGGTTCAGTTCGTCAGGCATTGCAACTAGTACAAAATGAATTG
CCTGGTTCAGGTTTTGAACCCGCGAGCAGTGAACGTGTATTTCATCTTTGTGTTTGCAGC
CCGTTAGACAGCATTCTGACCTCGCAGATTTATAATCACATTGAGCAGATTGCGCCAAAT
ATACATGTTATGTTCAAGTCTTCATTAAATCAGAACACTGAACATCAGCTGCGTTATCAG
GAAACGGAGTTTGTGATTAGTTATGAAGACTTCCATCGTCCTGAATTTACCAGCGTACCA
TTATTTAAAGATGAAATGGTGCTGGTAGCCAGCAAAAATCATCCAACAATTAAGGGCCCG
TTACTGAAACATGATGTTTATAACGAACAACATGCGGCGGTTTCGCTCGATCGTTTCGCG
TCATTTAGTCAACCTTGGTATGACACGGTAGATAAGCAAGCCAGTATCGCGTATCAGGGC
ATGGCAATGATGAGCGTACTTAGCGTGGTGTCGCAAACGCATTTGGTCGCTATTGCGCCG
CGTTGGCTGGCTGAAGAGTTCGCTGAATCCTTAGAATTACAGGTATTACCGCTGCCGTTA
AAACAAAACAGCAGAACCTGTTATCTCTCCTGGCATGAAGCTGCCGGGCGCGATAAAGGC
CATCAGTGGATGGAAGAGCAATTAGTCTCAATTTGCAAACGCTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 314 |
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| Protein Molecular Weight: | 34196 |
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| Protein Theoretical pI: | 5 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
MHAYLHCLSHSPLVGYVDPAQEVLDEVNGVIASARERIAAFSPELVVLFAPDHYNGFFYD
VMPPFCLGVGATAIGDFGSAAGELPVPVELAEACAHAVMKSGIDLAVSYCMQVDHGFAQP
LEFLLGGLDKVPVLPVFINGVATPLPGFQRTRMLGEAIGRFTSTLNKRVLFLGSGGLSHQ
PPVPELAKADAHMRDRLLGSGKDLPASERELRQQRVISAAEKFVEDQRTLHPLNPIWDNQ
FMTLLEQGRIQELDAVSNEELSAIAGKSTHEIKTWVAAFAAISAFGNWRSEGRYYRPIPE
WIAGFGSLSARTEN |
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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
- Bugg, T. D. (1993). "Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli." Biochim Biophys Acta 1202:258-264. Pubmed: 8399388
- 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
- Mendel, S., Arndt, A., Bugg, T. D. (2004). "Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)." Biochemistry 43:13390-13396. Pubmed: 15491145
- Spence, E. L., Kawamukai, M., Sanvoisin, J., Braven, H., Bugg, T. D. (1996). "Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases." J Bacteriol 178:5249-5256. Pubmed: 8752345
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