ID   CEEP_RUMA7              Reviewed;         389 AA.
AC   E6UB41; A8CF79;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Cellobiose 2-epimerase {ECO:0000255|HAMAP-Rule:MF_00929};
DE            Short=CE {ECO:0000255|HAMAP-Rule:MF_00929};
DE            EC=5.1.3.11 {ECO:0000255|HAMAP-Rule:MF_00929};
GN   OrderedLocusNames=Rumal_0019;
OS   Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS   7).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=697329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7;
RX   PubMed=17612504; DOI=10.1016/j.bbrc.2007.06.091;
RA   Ito S., Hamada S., Yamaguchi K., Umene S., Ito H., Matsui H., Ozawa T.,
RA   Taguchi H., Watanabe J., Wasaki J., Ito S.;
RT   "Cloning and sequencing of the cellobiose 2-epimerase gene from an
RT   obligatory anaerobe, Ruminococcus albus.";
RL   Biochem. Biophys. Res. Commun. 360:640-645(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7;
RX   PubMed=21914885; DOI=10.1128/jb.05621-11;
RA   Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA   Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA   Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA   Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT   "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT   7.";
RL   J. Bacteriol. 193:5574-5575(2011).
CC   -!- FUNCTION: Catalyzes the reversible epimerization of cellobiose to 4-O-
CC       beta-D-glucopyranosyl-D-mannose (Glc-Man). {ECO:0000255|HAMAP-
CC       Rule:MF_00929}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-cellobiose = beta-D-glucosyl-(1->4)-D-mannopyranose;
CC         Xref=Rhea:RHEA:23384, ChEBI:CHEBI:17057, ChEBI:CHEBI:47931;
CC         EC=5.1.3.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00929};
CC   -!- SIMILARITY: Belongs to the cellobiose 2-epimerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00929}.
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DR   EMBL; AB301954; BAF81109.1; -; Genomic_DNA.
DR   EMBL; CP002403; ADU20582.1; -; Genomic_DNA.
DR   RefSeq; WP_013496783.1; NZ_KK211250.1.
DR   AlphaFoldDB; E6UB41; -.
DR   SMR; E6UB41; -.
DR   STRING; 697329.Rumal_0019; -.
DR   PRIDE; E6UB41; -.
DR   EnsemblBacteria; ADU20582; ADU20582; Rumal_0019.
DR   KEGG; ral:Rumal_0019; -.
DR   eggNOG; COG2942; Bacteria.
DR   HOGENOM; CLU_046651_3_0_9; -.
DR   OMA; WVQAETF; -.
DR   OrthoDB; 783590at2; -.
DR   Proteomes; UP000006919; Chromosome.
DR   GO; GO:0047736; F:cellobiose epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   HAMAP; MF_00929; Cellobiose_2_epim; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR028584; Cellobiose_2_epim.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..389
FT                   /note="Cellobiose 2-epimerase"
FT                   /id="PRO_0000421449"
FT   CONFLICT        38
FT                   /note="E -> G (in Ref. 1; BAF81109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="L -> P (in Ref. 1; BAF81109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="D -> Y (in Ref. 1; BAF81109)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  45260 MW;  D8AEE6FA7E11130D CRC64;
     MMISEIRQEL TDHIIPFWNK LRDDENGGFY GYLSYGLELD KKADKGVILH SRILWFYSNA
     YMTLGGDELL DNAKHAYEFI KNNCIDYEYG GVYWMMDFEG KPADTMKHTY NIAFAIYALS
     SYYRASGDKE ALALAYRLFE DIEKNTLDEY GYREAFDRQW RLVDNEALSE NGLKADKTMN
     AILHLIEAYT ELYKADGNEK VADRLKFQLG QMRDIVYTPD TNALKVFFDT AFNLVGDIHS
     YGHDIEATWL MDRACDVLGD EDLKKQFAEM DLKISHNIQD IALEDGALNN ERDKNEIDKT
     RVWWVQAEAV VGFINAYQHS GDEKFLESAK SVWENIKEYI IDKREGGEWY SEVTFDHTPH
     DYKETVGPWK CPYHNGRMCM EVITRGVDI