CEEP_DICTD
ID CEEP_DICTD Reviewed; 389 AA.
AC B8DZK4;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=Dtur_0652;
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=515635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310;
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 6724 / Z-1310;
RX PubMed=22782272; DOI=10.1007/s10529-012-0999-z;
RA Kim J.E., Kim Y.S., Kang L.W., Oh D.K.;
RT "Characterization of a recombinant cellobiose 2-epimerase from Dictyoglomus
RT turgidum that epimerizes and isomerizes beta-1,4- and alpha-1,4-gluco-
RT oligosaccharides.";
RL Biotechnol. Lett. 34:2061-2068(2012).
CC -!- FUNCTION: Catalyzes the reversible epimerization of cellobiose to 4-O-
CC beta-D-glucopyranosyl-D-mannose (Glc-Man). Catalyzes epimerization but
CC also isomerization for beta-1,4- and alpha-1,4-gluco-oligosaccharides.
CC Can use cellobiose, lactose, cellotriose, maltose and maltotriose.
CC {ECO:0000255|HAMAP-Rule:MF_00929, ECO:0000269|PubMed:22782272}.
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:22782272};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75.8 mM for cellobiose {ECO:0000269|PubMed:22782272};
CC KM=79.6 mM for lactose {ECO:0000269|PubMed:22782272};
CC Note=kcat is 169 min(-1) for cellobiose. kcat is 89.4 min(-1) for
CC lactose.;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:22782272};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:22782272};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22782272}.
CC -!- SIMILARITY: Belongs to the cellobiose 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00929}.
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DR EMBL; CP001251; ACK41937.1; -; Genomic_DNA.
DR RefSeq; WP_012583022.1; NC_011661.1.
DR RefSeq; YP_002352551.1; NC_011661.1.
DR AlphaFoldDB; B8DZK4; -.
DR SMR; B8DZK4; -.
DR STRING; 515635.Dtur_0652; -.
DR EnsemblBacteria; ACK41937; ACK41937; Dtur_0652.
DR KEGG; dtu:Dtur_0652; -.
DR eggNOG; COG2942; Bacteria.
DR HOGENOM; CLU_046651_3_0_0; -.
DR InParanoid; B8DZK4; -.
DR OMA; WVQAETF; -.
DR OrthoDB; 783590at2; -.
DR BRENDA; 5.1.3.11; 13721.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0047736; F:cellobiose epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050121; F:N-acylglucosamine 2-epimerase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IBA:GO_Central.
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 Isomerase; Reference proteome.
FT CHAIN 1..389
FT /note="Cellobiose 2-epimerase"
FT /id="PRO_0000421445"
SQ SEQUENCE 389 AA; 46393 MW; EF819E43953C6BA6 CRC64;
MDLKVLKSEI FEHLNNKIIP FWEELKDENN GGYISYVGFD LKPDPYAPKG LVLTSRILWF
FSRLYNQLRK EEFINFADHS YKFLIKSFLD KENKGFYWMV DYKGEPIDKR KHLYGQAFVL
YGLSEYYKAT QKKESLDLAL EIYKIIEEVC KNDVGYKEEF DEKWNPKENI IVSEYGIICE
RSMNTLLHIL EAYTNLFTAT YDQSIKKKIE DLIILFKEKI YDSKTNHLYV FFDKKMNPII
DAISYGHDIE ATWLIDEALR YIDNNKLIKE MSEINLKIAE KVLEEAFESG SLLNERVRGI
VDKNRIWWVQ AEALVGFLNA YQKSKLDKFL KAVFELWEFI KDFLVDKRAQ GEWFWKLDEN
YIPSPMPEVD LWKCPYHNGR MCLEVIKRI