ID   CASB_KLEOX              Reviewed;         464 AA.
AC   Q48409;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Phospho-cellobiase;
DE            EC=3.2.1.-;
GN   Name=casB;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P2;
RX   PubMed=9023916; DOI=10.1128/aem.63.2.355-363.1997;
RA   Lai X., Davis F.C., Hespell R.B., Ingram L.O.;
RT   "Cloning of cellobiose phosphoenolpyruvate-dependent phosphotransferase
RT   genes: functional expression in recombinant Escherichia coli and
RT   identification of a putative binding region for disaccharides.";
RL   Appl. Environ. Microbiol. 63:355-363(1997).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; U61727; AAB51564.1; -; Genomic_DNA.
DR   RefSeq; WP_004138567.1; NZ_MKCU01000013.1.
DR   AlphaFoldDB; Q48409; -.
DR   SMR; Q48409; -.
DR   STRING; 571.MC52_27495; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PATRIC; fig|571.110.peg.4028; -.
DR   eggNOG; COG2723; Bacteria.
DR   OrthoDB; 654705at2; -.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..464
FT                   /note="Phospho-cellobiase"
FT                   /id="PRO_0000063900"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        361
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   464 AA;  52242 MW;  92F744FE5ADF6C38 CRC64;
     MKTFPQAFLW GGATAANQVE GAYLEDGKGL TTSDVQPRGV FGDVVERVPG DSGIKDIAID
     FYHRYPEDIS LFAEMGFNCL RVSIAWARIF PHGDEAQPNE AGLAFYDKLF DEMAKHNITP
     LVTLSHYEMP WALVKNYGGW GNRKVIGFFE RYARTVFERY QAKVKLWLTF NEINMSLHAP
     MTGVGLPADS SKAEVYQAIH HQLVASALAA KACHDIVPEG KIGNMLLGGL MYPLSCKPDD
     IFETLQQNRS WQFFGDVQCR GAYPGYMLRY FRDNGINLDI TDADRAALKE TVDFISFSYY
     MTGCVTADEE LNKKARGNIL SMVPNPHLAS SEWGWQIDPL GLRTLLNVLW DRYQKPLFIV
     ENGLGAKDKV EADGSINDDY RISYLNDHLV QVREAIEDGV ELMGYTSWGP IDLVSASKAE
     MSKRYGFIYV DRDDDGNGTL ARSRKKSFWW YKEVIATNGG SLKE