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MULTISPECIES: sialidase family protein [Salmonella].


LOCUS       WP_000761746             347 aa            linear   BCT 24-DEC-2024
ACCESSION   WP_000761746
VERSION     WP_000761746.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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 347)
  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 347)
  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 347)
  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 347)
  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..347
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..347
                     /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=38855
     Region          4..344
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 mklalvnrqv ilpesgtesf qchastlvrl pcgtlvaawf aglregsedt aiwlsryehn
       61 iwttpqrvaa regeahwnpv lfypsdklwl fykvgsdvhv wktwfitssd rgftwstpap
      121 lvnddilprg pvknklllas ngawiapgsi esperwrafv drssdegkhw sisfvplepd
      181 naisgtnval wdgikkgrlw ecclenllrw dgviqptlwe sspghihmll rstrgaifrs
      241 dsidygatws varatslpnn nsgidlvsmq dgtlilalnp vngnwgkryp lsliasqdng
      301 eswlplldle sdhgeysypa iiseggivhi tytwnrkniv ycrlqtv