MULTISPECIES: 6-phospho-beta-glucosidase [Klebsiella].

LOCUS       WP_004148093             448 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_004148093
VERSION     WP_004148093.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Varrot,A., Yip,V.L., Li,Y., Rajan,S.S., Yang,X., Anderson,W.F.,
            Thompson,J., Withers,S.G. and Davies,G.J.
  TITLE     NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases:
            structural insight into specificity for phospho-beta-D-glucosides
  JOURNAL   J Mol Biol 346 (2), 423-435 (2005)
   PUBMED   15670594
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 10143090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..448
                     /product="6-phospho-beta-glucosidase"
                     /EC_number="3.2.1.86"
                     /GO_function="GO:0008706 - 6-phospho-beta-glucosidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50118
     Region          5..436
                     /region_name="GH4_P_beta_glucosidase"
                     /note="Glycoside Hydrolases Family 4;
                     Phospho-beta-glucosidase; cd05296"
                     /db_xref="CDD:133432"
     Site            order(13..14,16,40..41,47,87..89,112,132,148,150,290,312,
                     317)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(96,112,150,173,203,258,282,312..313,317)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(172,203)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(192,195,211,214,331,343,362..363,365,367..370)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(244,246,249..251,263,265..266,376..377,384,388,395,
                     403,406..407,417..418,420,422)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 msqklkvvti gggssytpel legflkryhe lpvselwlvd veegqekldi ihalcqrmve
       61 kagvpmkvyk tldrraalqg adfvttqlrv gqlkarekde riplshgylg qetngagglf
      121 kglrtipvif divkdvqeic pdawiinftn pagmvteavy rhtnfkrfig vcnipigmkm
      181 fitdvlqlsp sdelnidlfg lnhlvfvrdv lvngvsrfde lldgvasgrl tansvknifd
      241 lpfseglirs lrlipcsyll yyfkpkemla iemgeyykgg araqvvqkve kqlfelyknp
      301 dlnvkpkele qrggayysda acevinaiyn dkqtehyvni phhghvdnip adwavemsct
      361 lgrdgakptp rithfdekvl gliytikgfe vaasqaaisg elndvllaln lsplihsdrd
      421 aeqlaremil ahekwlpnfa atieklks