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

LOCUS       WP_002886908             435 aa            linear   BCT 21-MAR-2023
ACCESSION   WP_002886908
VERSION     WP_002886908.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 435)
  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..435
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..435
                     /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=47463
     Region          4..431
                     /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..40,46,87..89,112,132,148,150,286,308,
                     313)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(96,112,150,172,201,254,278,308..309,313)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(171,201)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(190,193,209,212,327,339,358..359,361,363..366)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(240,242,245..247,259,261..262,371..372,379,383,390,
                     398,401..402,412..413,415,417)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 mqalkiavig ggssytpeli egiivryeql pvtelalvdv esgrekveii aaltrrmlkh
       61 kgleqvavsv hftldeairg asfvltqlrv gqlaaraade rlglkyhllg qettgvggfa
      121 kalrtipvil evarkveqla peafilnftn pagivteavs rystakiigl cnvpinmqhm
      181 ivgmlgaqes evklrfagln hmvwvhkvlq gredvtgkvi dmlcdgkals mnnikelpwp
      241 aeflralkai pcpyhryfwl tpamlaeeia aaktkgtrae qvmkveqelf alyadpqlee
      301 kpeqlsfrgg ayysevavel inaiynnlga emvvntrnng aihgldddav vetnsiidaq
      361 garplafgpl ppamngltqq vkaferltie aavhgcresa llalvanplv gnvtdaqall
      421 devltinrqw ltqfn