CEEP_BACFN
ID CEEP_BACFN Reviewed; 392 AA.
AC Q5LH66; B9X0V9;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
DE AltName: Full=Mannobiose 2-epimerase;
DE Short=MBE;
GN Name=bfce; OrderedLocusNames=BF0774; ORFNames=BF9343_0739;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=19202279; DOI=10.1271/bbb.80691;
RA Senoura T., Taguchi H., Ito S., Hamada S., Matsui H., Fukiya S., Yokota A.,
RA Watanabe J., Wasaki J., Ito S.;
RT "Identification of the cellobiose 2-epimerase gene in the genome of
RT Bacteroides fragilis NCTC 9343.";
RL Biosci. Biotechnol. Biochem. 73:400-406(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
RN [3]
RP FUNCTION AS A MANNOBIOSE 2-EPIMERASE, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=21539815; DOI=10.1016/j.bbrc.2011.04.095;
RA Senoura T., Ito S., Taguchi H., Higa M., Hamada S., Matsui H., Ozawa T.,
RA Jin S., Watanabe J., Wasaki J., Ito S.;
RT "New microbial mannan catabolic pathway that involves a novel
RT mannosylglucose phosphorylase.";
RL Biochem. Biophys. Res. Commun. 408:701-706(2011).
CC -!- FUNCTION: Catalyzes the reversible epimerization of cellobiose to 4-O-
CC beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also epimerize
CC cellotriose to Glc-Glc-Man, cellotetraose to Glc-Glc-Glc-Man, lactose
CC to epilactose, and mannobiose to 4-O-beta-D-mannopyranosyl-D-
CC glucopyranose (Man-Glc). May function as a mannobiose 2-epimerase in
CC vivo and be involved in a mannan catabolic pathway which feeds into
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_00929,
CC ECO:0000269|PubMed:19202279, ECO:0000269|PubMed:21539815}.
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 ECO:0000269|PubMed:19202279, ECO:0000269|PubMed:21539815};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.75 mM for cellobiose {ECO:0000269|PubMed:19202279,
CC ECO:0000269|PubMed:21539815};
CC KM=6.56 mM for lactose {ECO:0000269|PubMed:19202279,
CC ECO:0000269|PubMed:21539815};
CC KM=5.51 mM for mannobiose {ECO:0000269|PubMed:19202279,
CC ECO:0000269|PubMed:21539815};
CC Note=kcat is 67.6 sec(-1) for cellobiose. kcat is 79.5 sec(-1) for
CC lactose. kcat is 104 sec(-1) for mannobiose.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:19202279,
CC ECO:0000269|PubMed:21539815};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:19202279, ECO:0000269|PubMed:21539815};
CC -!- SIMILARITY: Belongs to the cellobiose 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00929}.
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DR EMBL; AB467284; BAH23773.1; -; Genomic_DNA.
DR EMBL; CR626927; CAH06520.1; -; Genomic_DNA.
DR RefSeq; WP_008658675.1; NC_003228.3.
DR AlphaFoldDB; Q5LH66; -.
DR SMR; Q5LH66; -.
DR STRING; 272559.BF9343_0739; -.
DR DNASU; 3288497; -.
DR EnsemblBacteria; CAH06520; CAH06520; BF9343_0739.
DR KEGG; bfs:BF9343_0739; -.
DR eggNOG; COG2942; Bacteria.
DR HOGENOM; CLU_046651_3_0_10; -.
DR OMA; WVQAETF; -.
DR OrthoDB; 783590at2; -.
DR BioCyc; BFRA272559:G1GHZ-808-MON; -.
DR BioCyc; MetaCyc:MON-18524; -.
DR BRENDA; 5.1.3.11; 755.
DR Proteomes; UP000006731; 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 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase; Reference proteome.
FT CHAIN 1..392
FT /note="Cellobiose 2-epimerase"
FT /id="PRO_0000421444"
SQ SEQUENCE 392 AA; 45778 MW; 6F93981D45ED114D CRC64;
MDEILKQEMQ KELTTRILPY WMERMVDQEN GGFYGRITGQ EELMPRADKG AILNARILWT
YSAAYRLLGR EEYKEMANRA KRYLIDHFYD SEFGGVYWSL NYRGEPLDTK KQIYAIGFAI
YGLSEFHRAT GDPEALMYAV RLFNDIESHS FDGLKNGYCE ALTREWNEIA DMRLSEKDAN
ERKTMNTHLH ILEPYTNLYR VWKDARLERQ LYNLIGLFTE KILDKDTSHL QLFFDNDWQS
KYPVVSYGHD IEASWLLHEA ARVLGDAGLI AEIEPVVKKI AAAASEGLTS DGGMIYEKNL
TTGHIDGDYH WWVQAETVVG YYNLFRYFGD RGALQHSIDC WEFIKRHLTD DVHGEWFWSL
RADGSLNRDD DKAGFWKCPY HNGRMCIELL GE
