CEEP_RHOMR
ID CEEP_RHOMR Reviewed; 412 AA.
AC F8WRK9;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 31.
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=ce;
OS Rhodothermus marinus (Rhodothermus obamensis).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Rhodothermus.
OX NCBI_TaxID=29549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-12, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=OKD7 / DSM 12399 / JCM 9785;
RX PubMed=22056431; DOI=10.1271/bbb.110456;
RA Ojima T., Saburi W., Sato H., Yamamoto T., Mori H., Matsui H.;
RT "Biochemical characterization of a thermophilic cellobiose 2-epimerase from
RT a thermohalophilic bacterium, Rhodothermus marinus JCM9785.";
RL Biosci. Biotechnol. Biochem. 75:2162-2168(2011).
CC -!- FUNCTION: Catalyzes the reversible epimerization of cellobiose to 4-O-
CC beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also use lactose,
CC epilactose, mannobiose and cellotriose. Highly specific for
CC oligosaccharides linked by the beta-1,4-glycosidic linkage. Shows
CC preference for lactose. {ECO:0000255|HAMAP-Rule:MF_00929,
CC ECO:0000269|PubMed:22056431}.
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:22056431};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.2 mM for cellobiose {ECO:0000269|PubMed:22056431};
CC KM=28.8 mM for lactose {ECO:0000269|PubMed:22056431};
CC Note=kcat is 80.8 sec(-1) for cellobiose. kcat is 111 sec(-1) for
CC lactose.;
CC pH dependence:
CC Optimum pH is 6.3. {ECO:0000269|PubMed:22056431};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:22056431};
CC -!- SIMILARITY: Belongs to the cellobiose 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00929}.
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DR EMBL; AB638764; BAK61777.1; -; Genomic_DNA.
DR PDB; 3WKF; X-ray; 1.74 A; A=1-412.
DR PDB; 3WKG; X-ray; 1.47 A; A=1-412.
DR PDB; 3WKH; X-ray; 1.64 A; A=1-412.
DR PDB; 3WKI; X-ray; 2.19 A; A=1-412.
DR PDBsum; 3WKF; -.
DR PDBsum; 3WKG; -.
DR PDBsum; 3WKH; -.
DR PDBsum; 3WKI; -.
DR AlphaFoldDB; F8WRK9; -.
DR SMR; F8WRK9; -.
DR PRIDE; F8WRK9; -.
DR BRENDA; 5.1.3.11; 5425.
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 3D-structure; Direct protein sequencing; Isomerase.
FT CHAIN 1..412
FT /note="Cellobiose 2-epimerase"
FT /id="PRO_0000421447"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:3WKG"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 81..97
FT /evidence="ECO:0007829|PDB:3WKG"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 123..140
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 143..159
FT /evidence="ECO:0007829|PDB:3WKG"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 215..231
FT /evidence="ECO:0007829|PDB:3WKG"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:3WKG"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:3WKG"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3WKG"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3WKG"
FT HELIX 389..406
FT /evidence="ECO:0007829|PDB:3WKG"
SQ SEQUENCE 412 AA; 47387 MW; 0EEE153737F40DBD CRC64;
MSTETIPDVR RLRALQAEVH EELTENILKF WATRTHDPVH GGFVGRVGPD GRPHPEAPRG
AILNARILWT FAAAYRQLGT PLYREMAERA YRYFVRHFVD AEHGGVYWMV AADGRPLDTR
KHVYAQSFAI YALSEWHRAT GGEAALALAR SIYDLIETHC ADRVHGGYVE ACDRAWRPLE
DARLSAKDAP EPRSMNTHLH VLEAYANLYR VWPETELAAR LQALIELFLR AIYHPATGHL
ILFFDERWRP RSRAVSFGHD IEASWLLLEA VDVLGQATLR PRVQQASLHL ARATLAEGRA
PDGSLYYEIG EQGHLDTDRH WWPQAEALVG FLNAYQESGE VLFYEAAEDV WRYIRERQRD
TRGGEWFARV RDDGAPYPDD KVDFWKGPYH NGRACLEAIQ RLRHLLEHVR SR
