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http://purl.uniprot.org/citations/8563148http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8563148http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8563148http://www.w3.org/2000/01/rdf-schema#comment"The gene encoding a beta-galactosidase from Xanthomonas manihotis was cloned into Escherichia coli. The gene resides on a 2.4 kb DNA fragment which was isolated from a partial Sau3A library in the cloning vector pUC19 using 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal) as the selection. The enzyme produced by the clone has a specificity for beta 1-3-> beta 1-4-linked galactose. The nucleotide sequence of the gene was determined. The deduced protein sequence contained 597 amino acids yielding a monomeric molecular mass of 66 kDa. The cloned beta-galactosidase showed no similarity to any known prokaryotic beta-galactosidase. However, extensive similarity was observed with eukaryotic beta-galactosidases from animals, plants and fungi. The strongest similarity was with the beta-galactosidases found in the human and mouse lysosomes (42 and 41% identity, respectively). Alignment of the X.manihotis and eukaryotic beta-galactosidase sequences revealed seven highly conserved domains common to each protein. Additionally, Domain 1 in X.manihotis showed similarity to regions within catalytic domains from seven xylanases and cellulases belonging to family 10 of glucosyl hydrolases. A region spanning Domain 2 showed similarity to the catalytic domain of endo beta 1-3 glucanases from tobacco and barley."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.org/dc/terms/identifier"doi:10.1093/glycob/5.6.603"xsd:string
http://purl.uniprot.org/citations/8563148http://purl.org/dc/terms/identifier"doi:10.1093/glycob/5.6.603"xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Benner J.S."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Benner J.S."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Hornstra L.J."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Hornstra L.J."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Guthrie E.P."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Guthrie E.P."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Taron C.H."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/author"Taron C.H."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/pages"603-610"xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/pages"603-610"xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/title"A novel beta-galactosidase gene isolated from the bacterium Xanthomonas manihotis exhibits strong homology to several eukaryotic beta-galactosidases."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/title"A novel beta-galactosidase gene isolated from the bacterium Xanthomonas manihotis exhibits strong homology to several eukaryotic beta-galactosidases."xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/8563148http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/8563148http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8563148
http://purl.uniprot.org/citations/8563148http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8563148