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http://purl.uniprot.org/citations/9603882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9603882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9603882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9603882http://www.w3.org/2000/01/rdf-schema#comment"We have identified, cloned, and sequenced the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid (PP) in Escherichia coli K-12. This cluster maps at min 57.5 of the chromosome and is composed of five catabolic genes arranged as a putative operon (hcaA1A2CBD) and two additional genes transcribed in the opposite direction that encode a potential permease (hcaT) and a regulator (hcaR). Sequence comparisons revealed that while hcaA1A2CD genes encode the four subunits of the 3-phenylpropionate dioxygenase, the hcaB gene codes for the corresponding cis-dihydrodiol dehydrogenase. This type of catabolic module is homologous to those encoding class IIB dioxygenases and becomes the first example of such a catabolic cluster in E. coli. The inducible expression of the hca genes requires the presence of the hcaR gene product, which acts as a transcriptional activator and shows significant sequence similarity to members of the LysR family of regulators. Interestingly, the HcaA1A2CD and HcaB enzymes are able to oxidize not only PP to 3-(2,3-dihydroxyphenyl)propionate (DHPP) but also cinnamic acid (CI) to its corresponding 2, 3-dihydroxy derivative. Further catabolism of DHPP requires the mhp-encoded meta fission pathway for the mineralization of 3-hydroxyphenylpropionate (3HPP) (A. Ferrández, J. L. García, and E. Díaz, J. Bacteriol. 179:2573-2581, 1997). Expression in Salmonella typhimurium of the mhp genes alone or in combination with the hca cluster allowed the growth of the recombinant bacteria in 3-hydroxycinnamic acid (3HCI) and CI, respectively. Thus, the convergent mhp- and hca-encoded pathways are also functional in S. typhimurium, and they are responsible for the catabolism of different phenylpropanoid compounds (3HPP, 3HCI, PP, and CI) widely available in nature."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.org/dc/terms/identifier"doi:10.1128/jb.180.11.2915-2923.1998"xsd:string
http://purl.uniprot.org/citations/9603882http://purl.org/dc/terms/identifier"doi:10.1128/jb.180.11.2915-2923.1998"xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/author"Diaz E."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/author"Diaz E."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/author"Garcia J.L."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/author"Garcia J.L."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/author"Ferrandez A."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/author"Ferrandez A."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/pages"2915-2923"xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/pages"2915-2923"xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/title"Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/title"Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12."xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/volume"180"xsd:string
http://purl.uniprot.org/citations/9603882http://purl.uniprot.org/core/volume"180"xsd:string
http://purl.uniprot.org/citations/9603882http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9603882
http://purl.uniprot.org/citations/9603882http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9603882
http://purl.uniprot.org/citations/9603882http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9603882