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LOCUS WP_002892001 685 aa linear BCT 31-DEC-2024 ACCESSION WP_002892001 VERSION WP_002892001.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 685) AUTHORS Coines,J., Raich,L. and Rovira,C. TITLE Modeling catalytic reaction mechanisms in glycoside hydrolases JOURNAL Curr Opin Chem Biol 53, 183-191 (2019) PUBMED 31731209 REFERENCE 2 (residues 1 to 685) AUTHORS Naumoff,D.G. TITLE Hierarchical classification of glycoside hydrolases JOURNAL Biochemistry (Mosc) 76 (6), 622-635 (2011) PUBMED 21639842 REFERENCE 3 (residues 1 to 685) AUTHORS Vuong,T.V. and Wilson,D.B. TITLE Glycoside hydrolases: catalytic base/nucleophile diversity JOURNAL Biotechnol Bioeng 107 (2), 195-205 (2010) PUBMED 20552664 REFERENCE 4 (residues 1 to 685) AUTHORS Davies,G. and Henrissat,B. TITLE Structures and mechanisms of glycosyl hydrolases JOURNAL Structure 3 (9), 853-859 (1995) PUBMED 8535779 REFERENCE 5 (residues 1 to 685) AUTHORS Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and Davies,G. TITLE Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases JOURNAL Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995) PUBMED 7624375 REMARK Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi: 10.1073/pnas.93.11.5674. PMID: 8643635] COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 11449001 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..685 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..685 /product="beta-galactosidase" /EC_number="3.2.1.23" /GO_component="GO:0009341 - beta-galactosidase complex [Evidence IEA]" /GO_function="GO:0004565 - beta-galactosidase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_process="GO:0006012 - galactose metabolic process [Evidence IEA]" /calculated_mol_wt=77426 Region 4..634 /region_name="GanA" /note="Beta-galactosidase GanA [Carbohydrate transport and metabolism]; COG1874" /db_xref="CDD:441478" Region 626..683 /region_name="Glyco_hydro_42C" /note="Beta-galactosidase C-terminal domain; pfam08533" /db_xref="CDD:400716" ORIGIN 1 mnkfaplhpk vstllhgady npeqwendpd iidkdiammq qakcnvmsvg ifswaklepr 61 egvfnfawld iildklyaag ihvflatpsg arpawmsqry pqvlrvgrdr vpalhggrhn 121 hcmsspvyre ktlqintlla erysshpavl gwhisneygg echcdlcqnr frdwlkaryq 181 tlenlnqaww stfwshtytd wsqiespapq gemsihglnl dwhrfntaqv tdfcrheiap 241 lkaanaslpv ttnfmeyfyd ydywqlaeal dfiswdsypm whrdkdetal acytamyhdm 301 mrslkggkpf vlmestpgat nwqptsklkk pgmhilsslq avahgadsvq yfqwrksrgs 361 vekfhgavvd hvghidtrig revcqlgeil sklpevrgcr teakvaiifd qqnrwaldda 421 qgprnlgmey ektvnehyrp fweqgiavdv idadvdltpy qlviapmlym vrdgfagrae 481 afvangghlv ttywtgivne sdlcylggfp gplrnllgiw aeeidclndg efnlvqglag 541 nqcglqgpyq vrhlcelihi esaqalatyr ddfyagrpav tvnafgkgka whvasrndla 601 fqrdfftals kelalpraia telppgvvat artdgdnafi flqnysaqnh tltlpqgyrd 661 cltdaavsap ltlsawdcri lrrha