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

LOCUS       WP_003721330             440 aa            linear   BCT 14-DEC-2023
ACCESSION   WP_003721330
VERSION     WP_003721330.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 440)
  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..440
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..440
                     /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=49143
     Region          6..435
                     /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(96,112,150,173,202,258,282,312..313,317)
                     /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(191,194,210,213,331,343,362..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..266,375..376,383,387,394,
                     402,405..406,416..417,419,421)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 mkkgvkivti gggssytpel vegfikryhe lpirelwlvd ieagreklei vgnmakrmvk
       61 aanidcevhl tldrrealkd adfvttqfrv glldarikde riplshgiig qetngaggmf
      121 kafrtipvil givedmrelc pdawlinftn pagmvteavl rygnwdkvig lcnvpigavk
      181 sasdvlekpe edlffkfagi nhlhwhrvfd kdgteltekv idglyapdan pgkvvenikn
      241 mrflyeqvkh lkmlpcpyhr yyymtdamle eelasfkneg trgevvkkle dslfelykdp
      301 nldykpeels krggahysda aceiinsiyn nkgtvmvvst rnngaiddvp ydsaveitsv
      361 irahgaepin fgkfppaqrg llqvmksmee ltieaavtgd yatalqafts nplvpsgdla
      421 ktildemlea hkeflpqfak