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MULTISPECIES: glycoside hydrolase family 32 protein [Klebsiella].


LOCUS       WP_002915999             477 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_002915999
VERSION     WP_002915999.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  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 477)
  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 477)
  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 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..477
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54368
     Region          22..477
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mtytisraeq vlqtqrqaln lrwyphyhla aragwindpn glvwfdgwyh afyqhhpyst
       61 qwgpmhwgha rskdlvhweh lpvalapegp edkdgcfsgs avvdgdtlal iytghkfhgd
      121 pgdeanlyqv qclatsrdgi hferqgmvvd tppgmhhfrd pkvwregdcw ymivgaregd
      181 tgqvrlyrsa dlrqwqdagv ldeaestmgy mwecpdfftl ngkrvlmfsp qgmqaagfsn
      241 rnlfqsgyli gewqpgqrfi rhgefremdn ghdfyapqsf stpdgrrivi gwldmwespl
      301 peqqdgwagm lslprelsls addrlqmrpa keveslrgaw fpwpvstlnn qqttmvdnce
      361 amevnlrwdc arssaeqygl rfgdglriym daqqqrlvle rhypqyglcg trsvpltaga
      421 dlnlriffds ssvevfvndg eaclssriyp qaprrelalf awsgaaalte agawqle