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LOCUS WP_002904416 388 aa linear BCT 23-DEC-2024 ACCESSION WP_002904416 VERSION WP_002904416.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 388) 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 388) 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 388) 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 388) AUTHORS Taylor,G. TITLE Sialidases: structures, biological significance and therapeutic potential JOURNAL Curr Opin Struct Biol 6 (6), 830-837 (1996) PUBMED 8994884 REFERENCE 5 (residues 1 to 388) AUTHORS Davies,G. and Henrissat,B. TITLE Structures and mechanisms of glycosyl hydrolases JOURNAL Structure 3 (9), 853-859 (1995) PUBMED 8535779 REFERENCE 6 (residues 1 to 388) 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] REFERENCE 7 (residues 1 to 388) AUTHORS Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R. TITLE The sialidase superfamily and its spread by horizontal gene transfer JOURNAL Mol Microbiol 9 (5), 915-921 (1993) PUBMED 7934919 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 10008717 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..388 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..388 /product="sialidase family protein" /EC_number="3.2.1.-" /GO_function="GO:0004308 - exo-alpha-sialidase activity [Evidence IEA]" /GO_function="GO:0016997 - alpha-sialidase activity [Evidence IEA]" /GO_process="GO:0005975 - carbohydrate metabolic process [Evidence IEA]" /calculated_mol_wt=42818 Region 29..386 /region_name="COG4692" /note="Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]" /db_xref="CDD:443727" ORIGIN 1 mtvippfdgv irqhqqdehi awamlpcacp qnhaanllpl ddgslmcvwf ggsqegkadi 61 siwgsrlapg sdrwseavkl cddpdrseqn pvlfqapdnv lwllwtaqfa gnqdtaivry 121 rlshdggrsw gaidtlldqp gtfirqpisv msdgnwllpv fycrtepgek wvgnndvsav 181 kissdcgksw rdvavpeslg cvhmsitplp dgrlaaffrs rwadhiwfsq ssdqgeswsa 241 pvpttlpnnn ssiqatpldn gelalvfnnm saagaterra slydeiaddd grrepeatgk 301 safwgaprap mtvaisadgg eswpwlrnld egdgycmtnn seqklnrefs ypsikqgadg 361 nlhiaytwyr qaikyvrvsp qwvkgesa