ID   A0A078RUT4_BACUN        Unreviewed;       417 AA.
AC   A0A078RUT4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Cellobiose 2-epimerase {ECO:0000256|HAMAP-Rule:MF_00929};
DE            Short=CE {ECO:0000256|HAMAP-Rule:MF_00929};
DE            EC=5.1.3.11 {ECO:0000256|HAMAP-Rule:MF_00929};
GN   ORFNames=M094_2995 {ECO:0000313|EMBL:KDS48063.1};
OS   Bacteroides uniformis str. 3978 T3 ii.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1339349 {ECO:0000313|EMBL:KDS48063.1, ECO:0000313|Proteomes:UP000028013};
RN   [1] {ECO:0000313|EMBL:KDS48063.1, ECO:0000313|Proteomes:UP000028013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3978 T3 ii {ECO:0000313|EMBL:KDS48063.1,
RC   ECO:0000313|Proteomes:UP000028013};
RA   Sears C., Carroll K., Sack B.R., Qadri F., Myers L.L., Chung G.-T.,
RA   Escheverria P., Fraser C.M., Sadzewicz L., Shefchek K.A., Tallon L.,
RA   Das S.P., Daugherty S., Mongodin E.F.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible epimerization of cellobiose to 4-O-
CC       beta-D-glucopyranosyl-D-mannose (Glc-Man). {ECO:0000256|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:0000256|ARBA:ARBA00001470,
CC         ECO:0000256|HAMAP-Rule:MF_00929};
CC   -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00008558}.
CC   -!- SIMILARITY: Belongs to the cellobiose 2-epimerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00929}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDS48063.1}.
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DR   EMBL; JNHN01000184; KDS48063.1; -; Genomic_DNA.
DR   RefSeq; WP_008662425.1; NZ_JNHN01000184.1.
DR   AlphaFoldDB; A0A078RUT4; -.
DR   PATRIC; fig|1339349.3.peg.4048; -.
DR   Proteomes; UP000028013; Unassembled WGS sequence.
DR   GO; GO:0047736; F:cellobiose epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR010819; AGE/CE.
DR   InterPro; IPR028584; Cellobiose_2_epim.
DR   PANTHER; PTHR15108:SF0; N-ACYLGLUCOSAMINE 2-EPIMERASE; 1.
DR   PANTHER; PTHR15108; N-ACYLGLUCOSAMINE-2-EPIMERASE; 1.
DR   Pfam; PF07221; GlcNAc_2-epim; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KDS48063.1};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00929}.
SQ   SEQUENCE   417 AA;  47917 MW;  5471001EF41DF515 CRC64;
     MKRMFSVFLL ITVWLLVTPF LQAQSHVDKV LKDEITSDLK ENILSFWERY SVDSSGGFYG
     SLGRDGAPIA DAPKGGVLNA RILWTFSTAY RMYGDTAYRK LADRAQRYFI DHFIDSQYGG
     VYWLIKADGT PLDTNKQTYG CSYAIYGLSE HFRATGNNES LQKAIELYRI MESKVKDPVN
     DGYIESFTRE WGTPQKLGYD GDGIAAKTMN THIHVLEAYT ALYKVWKDNS LCKRLAKVID
     LITTRLYNPQ THHLISYCDL NWNNLDDIDS YGHDIETSWL LTEAAEALGD PEVIGRCRKV
     ALELADASLK EGINPMGAMM YERHKDKIRK DASWWCQAET VVGCINAWQL TGEQSYLDSA
     VRTWNFIKSR MIDKEYGEWF RTVLEDGTPR YKEPKASMWN CPYHNSRMGF EIDTRLK
//