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http://purl.uniprot.org/citations/19321747http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19321747http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19321747http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/19321747http://www.w3.org/2000/01/rdf-schema#comment"Phylloquinone (vitamin K(1)) is a bipartite molecule that consists of a naphthoquinone ring attached to a phytyl side chain. The coupling of these 2 moieties depends on the hydrolysis of the CoA thioester of 1,4-dihydroxy-2-naphthoate (DHNA), which forms the naphthalenoid backbone. It is not known whether such a hydrolysis is enzymatic or chemical. In this study, comparative genomic analyses identified orthologous genes of unknown function that in most species of cyanobacteria cluster with predicted phylloquinone biosynthetic genes. The encoded approximately 16-kDa proteins display homology with some Hotdog domain-containing CoA thioesterases that are involved in the catabolism of 4-hydroxybenzoyl-CoA and gentisyl-CoA (2,5-dihydroxybenzoyl-CoA) in certain soil-dwelling bacteria. The Synechocystis ortholog, encoded by gene slr0204, was expressed as a recombinant protein and was found to form DHNA as reaction product. Unlike its homologs in the Hotdog domain family, Slr0204 showed strict substrate specificity. The Synechocystis slr0204 knockout was devoid of DHNA-CoA thioesterease activity and accumulated DHNA-CoA. As a result, knockout cells contained 13-fold less phylloquinone than their wild-type counterparts and displayed the typical photosensitivity to high light associated to phylloquinone deficiency in cyanobacteria."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0900738106"xsd:string
http://purl.uniprot.org/citations/19321747http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0900738106"xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"Widhalm J.R."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"Widhalm J.R."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"Basset G.J.C."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"Basset G.J.C."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"van Oostende C."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"van Oostende C."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"Furt F."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/author"Furt F."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/pages"5599-5603"xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/pages"5599-5603"xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/title"A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/title"A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1."xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/volume"106"xsd:string
http://purl.uniprot.org/citations/19321747http://purl.uniprot.org/core/volume"106"xsd:string
http://purl.uniprot.org/citations/19321747http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19321747