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

LOCUS       WP_000078785             451 aa            linear   BCT 21-MAR-2023
ACCESSION   WP_000078785
VERSION     WP_000078785.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 451)
  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..451
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..451
                     /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=50407
     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 legfikryhe lpvtelwlvd vedgkeklgi iydlcqrmid
       61 kagvplklyk tldrrealkg anfvttqlrv gqlkarelde riplshgylg qetngagglf
      121 kglrtipvif diikdveelc pnawvinftn pagmvteavy rhtnfkkfig vcnipvgmkm
      181 fihdvlalne nddlsidlfg lnhmvfikdv lvngtsrfae lldgvasgql kastvknifd
      241 lpfseglirs lnmlpcsyll yyfkqkemla iemgeyykgg araqvvqkve kqlfdlyknp
      301 elnvkpkele qrggayysda acevinaiyn dkqtehyvni phhghvenip adwavemtci
      361 lgrngatphp ritrfdekvl glihtikgfe vaasnaalsg nfndvllaln lsplvhsdrd
      421 aevlarelil ahekwlpnfa aciealkgkh h