CEEP_EUBCE
ID CEEP_EUBCE Reviewed; 405 AA.
AC B3XZI5;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 36.
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 Name=ce13;
OS Eubacterium cellulosolvens.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=29322;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NE13;
RX PubMed=18710396; DOI=10.1111/j.1574-6968.2008.01281.x;
RA Taguchi H., Senoura T., Hamada S., Matsui H., Kobayashi Y., Watanabe J.,
RA Wasaki J., Ito S.;
RT "Cloning and sequencing of the gene for cellobiose 2-epimerase from a
RT ruminal strain of Eubacterium cellulosolvens.";
RL FEMS Microbiol. Lett. 287:34-40(2008).
CC -!- FUNCTION: Catalyzes the reversible epimerization of cellobiose to 4-O-
CC beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also epimerize lactose
CC to epilactose. {ECO:0000255|HAMAP-Rule:MF_00929,
CC ECO:0000269|PubMed:18710396}.
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:18710396};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.3 mM for cellobiose {ECO:0000269|PubMed:18710396};
CC KM=72 mM for lactose {ECO:0000269|PubMed:18710396};
CC Vmax=36.4 umol/min/mg enzyme with cellobiose as substrate
CC {ECO:0000269|PubMed:18710396};
CC Vmax=41.5 umol/min/mg enzyme with lactose as substrate
CC {ECO:0000269|PubMed:18710396};
CC Note=kcat is 28.5 sec(-1) for cellobiose. kcat is 32.5 sec(-1) for
CC lactose.;
CC pH dependence:
CC Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:18710396};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:18710396};
CC -!- SIMILARITY: Belongs to the cellobiose 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00929}.
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DR EMBL; AB372003; BAG68451.1; -; Genomic_DNA.
DR AlphaFoldDB; B3XZI5; -.
DR SMR; B3XZI5; -.
DR BRENDA; 5.1.3.11; 8385.
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.
FT CHAIN 1..405
FT /note="Cellobiose 2-epimerase"
FT /id="PRO_0000421446"
SQ SEQUENCE 405 AA; 46964 MW; 617EB35E1DDB0CF6 CRC64;
MKNEVVYKQL TEKILPFWNA MRDDENGGFY GYMSEDLHID DHADKGCILN SRILWFYSTA
YMYLQDEKLL DNAKHAFEFL KTYCFDPMCG GIFWSVRYNG KPADTTKHTY NQAFAIYALS
AYYEATGSIE AIAIAEIIYE KIEDTMRDTK GYLEAFTRDF RPADNDKLSE NGVMAERTMN
TLLHIIEAYS ALVHALRKKV ADPAKGDVRD ELFMNVVENK LAAALELMRD KFYNSDRHRL
DVFFDKEYES LIDLTSYGHD IEASWLLEWA AGILDDEEIT ESLHPISSDL VEKVYKEAFD
GHSIVNECED GDVNTDRIWW VEAESVLGFL KAFEREGKEE YRKAAHEILA FILDKQVDKR
EGSEWFEMLK EDGTPCHKPM VREWKCPYHN GRMCLEILKS GIEIG