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

LOCUS       WP_002901977             437 aa            linear   BCT 21-MAR-2023
ACCESSION   WP_002901977
VERSION     WP_002901977.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 437)
  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..437
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..437
                     /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=48300
     Region          4..432
                     /region_name="GH4_P_beta_glucosidase"
                     /note="Glycoside Hydrolases Family 4;
                     Phospho-beta-glucosidase; cd05296"
                     /db_xref="CDD:133432"
     Site            order(12..13,15,39..40,46,86..88,111,131,147,149,287,309,
                     314)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(95,111,149,171,201,255,279,309..310,314)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(170,201)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(190,193,209,212,328,340,359..360,362,364..367)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(241,243,246..248,260,262..263,372..373,380,384,391,
                     399,402..403,413..414,416,418)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 msglkivvig ggssytpeli egllnryhem pvaslwlvdi eegkekveii aglarrmiak
       61 agltievvat ldresalrda dfvcsqfrag cldarisder islkygligq etnglggfan
      121 acrtipiale iaadmerlcp dawllnftnp sgmvteailr hsrikavglc nvpvimqkgi
      181 ttllqcadek evvmqvagln hfifvrqilh kgkewlpevi aeinagrdpl vprnippfrw
      241 pshllqglgm ipcaylryyy mkddllrqel aeaggegtrg evvkqlekil fdqyrdphla
      301 vkpkalegrg gqyyseaace lmnaiyndkr iimhvntrnn gainglpddc avevsslita
      361 sgplplnvap fpedtlrllq lmksferlti eaaltgnrht awralmlnpl ivsgeklela
      421 ldeviaenrq wlpafha