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LOCUS WP_010989000 412 aa linear BCT 07-JAN-2025 ACCESSION WP_010989000 VERSION WP_010989000.1 KEYWORDS RefSeq. SOURCE Salmonella enterica ORGANISM Salmonella enterica Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Salmonella. REFERENCE 1 (residues 1 to 412) 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 412) 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 412) 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 412) 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 412) 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 412) 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 412) 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 10202570 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..412 /organism="Salmonella enterica" /db_xref="taxon:28901" Protein 1..412 /product="sialidase family protein" /EC_number="3.2.1.-" /GO_function="GO:0004308 - exo-alpha-sialidase activity [Evidence IEA]" /GO_process="GO:0005975 - carbohydrate metabolic process [Evidence IEA]" /calculated_mol_wt=45541 Region 53..402 /region_name="Sialidase_non-viral" /note="Non-viral sialidases; cd15482" /db_xref="CDD:271234" Region 66..117 /region_name="Sialidase propeller 1" /note="Sialidase propeller 1 [structural motif]" /db_xref="CDD:271234" Site order(67,92,261,276,339,372,391) /site_type="active" /note="catalytic site [active]" /db_xref="CDD:271234" Region 128..191 /region_name="Sialidase propeller 2" /note="Sialidase propeller 2 [structural motif]" /db_xref="CDD:271234" Region 203..253 /region_name="Sialidase propeller 3" /note="Sialidase propeller 3 [structural motif]" /db_xref="CDD:271234" Region 260..296 /region_name="Sialidase propeller 4" /note="Sialidase propeller 4 [structural motif]" /db_xref="CDD:271234" Region 309..360 /region_name="Sialidase propeller 5" /note="Sialidase propeller 5 [structural motif]" /db_xref="CDD:271234" ORIGIN 1 mtrhllncri lymhppldmh thpfikegks mtveksvvfk aegehftdqk gntivgsgsg 61 gttkyfripa mcttskgtiv vfadarhnta sdqsfidtaa arstdggktw nkkiaiyndr 121 vnsklsrvmd ptcivaniqg retilvmvgk wnnndktwga yrdkapdtdw dlvlykstdd 181 gvtfskvetn ihdivtkngt isamlggvgs glqlndgklv fpvqmvrtkn ittvlntsfi 241 ystdgitwsl psgycegfgs enniiefnas lvnnirnsgl rrsfetkdfg ktwtefppmd 301 kkvdnrnhgv qgstitipsg nklvaahssa qnknndytrs dislyahnly sgevkliddf 361 ypkvgnasga gysclsyrkn vdketlyvvy eangsiefqd lsrhlpviks yn