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

LOCUS       WP_003726689             438 aa            linear   BCT 14-DEC-2023
ACCESSION   WP_003726689
VERSION     WP_003726689.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 438)
  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..438
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..438
                     /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=48860
     Region          5..433
                     /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..89,112,132,148,150,288,310,
                     315)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(96,112,150,173,202,256,280,310..311,315)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(172,202)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(191,194,210,213,329,341,360..361,363,365..368)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(242,244,247..249,261,263..264,373..374,381,385,392,
                     400,403..404,414..415,417,419)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 mtkgikiati gggssytpel iegfikrqde lpvrelwlvd veagreklei vgnlakrmve
       61 kagvdmevhl tldreealkd adfvttqlrv glldarvkde ripnsygvvg qetngpggmf
      121 kglrtipvil dickdmerlc pdawlinfan pagmvteavl rysnqkkvvg lcngpigier
      181 niaetlgvdv seiyvefvgl nhmvfaktvy hngkdvtkdv vfkmtedeag sslkninatg
      241 wdktflrtln mipidylryy wqtkqqledq arayaehgtr aevvkkveae lfelykqeel
      301 aekpkqleqr ggayyseaac nlinsiyndk rdiqivntrn ngaildidpd savetncvit
      361 rqgpiplasg rlpiaingii qeiktferlt aeaavtgdyd kallamtinp ltpsesvare
      421 mldelleahk eylpnffk