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

LOCUS       WP_000078765             450 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_000078765
VERSION     WP_000078765.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Keyhani,N.O., Wang,L.X., Lee,Y.C. and Roseman,S.
  TITLE     The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by
            Escherichia coli and is transported/phosphorylated by the
            phosphoenolpyruvate:glycose phosphotransferase system
  JOURNAL   J. Biol. Chem. 275 (42), 33084-33090 (2000)
   PUBMED   10913117
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Thompson,J., Ruvinov,S.B., Freedberg,D.I. and Hall,B.G.
  TITLE     Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli:
            characterization and assignment to the unusual family 4 of
            glycosylhydrolases
  JOURNAL   J. Bacteriol. 181 (23), 7339-7345 (1999)
   PUBMED   10572139
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  :: BlastRule
            Evidence Accession :: NBR007105
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..450
                     /gene="celF"
                     /gene_synonym="chbF"
     Protein         1..450
                     /product="6-phospho-beta-glucosidase"
                     /EC_number="3.2.1.86"
                     /calculated_mol_wt=50382
     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 lpvselwlvd veggkpkldi ifdlcqrmid
       61 nagvpmklyk tldrrealkd adfvttqlrv gqlparelde riplshgylg qetngagglf
      121 kglrtipvif divkdveelc pnawvinftn pagmvteavy rhtgfkrfig vcnipigmkm
      181 firdvlmlkd sddlsidlfg lnhmvfikdv lingksrfae lldgvasgql kassvknifd
      241 lpfseglirs lnllpcsyll yyfkqkemla iemgeyykgg araqvvqkve kqlfelyknp
      301 elkvkpkele qrggayysda acevinaiyn dkqaehyvni phhgqidnip adwavemtck
      361 lgrdgatphp rithfddkvm glihtikgfe iaasnaalsg efndvllaln lsplvhsdrd
      421 aellaremil ahekwlpnfa dciaelkkah