DPES_ENTBW
ID DPES_ENTBW Reviewed; 301 AA.
AC A8RG82;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=D-psicose 3-epimerase {ECO:0000303|PubMed:23644747};
DE Short=DPEase {ECO:0000303|PubMed:23644747};
DE EC=5.1.3.30 {ECO:0000269|PubMed:23644747};
GN ORFNames=CLOBOL_00069;
OS Enterocloster bolteae (strain ATCC BAA-613 / DSM 15670 / CCUG 46953 / JCM
OS 12243 / WAL 16351) (Clostridium bolteae).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=411902;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-613 / DSM 15670 / CCUG 46953 / JCM 12243 / WAL 16351;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium bolteae (ATCC BAA-613).";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, COFACTOR, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC BAA-613 / DSM 15670 / CCUG 46953 / JCM 12243 / WAL 16351;
RX PubMed=23644747; DOI=10.1007/s00253-013-4924-8;
RA Jia M., Mu W., Chu F., Zhang X., Jiang B., Zhou L.L., Zhang T.;
RT "A D-psicose 3-epimerase with neutral pH optimum from Clostridium bolteae
RT for D-psicose production: cloning, expression, purification, and
RT characterization.";
RL Appl. Microbiol. Biotechnol. 98:717-725(2014).
CC -!- FUNCTION: Involved in the biosynthesis of D-psicose. Catalyzes the
CC reversible epimerization of D-fructose at the C3 position to yield D-
CC psicose. The enzyme is highly specific for D-psicose and shows very low
CC activity with D-tagatose. {ECO:0000269|PubMed:23644747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360,
CC ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1.3.30;
CC Evidence={ECO:0000269|PubMed:23644747};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23644747};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:23644747};
CC Note=Binds 1 Mn(2+) or Co(2+) ion per subunit.
CC {ECO:0000269|PubMed:23644747};
CC -!- ACTIVITY REGULATION: Completely inhibited by EDTA and partially
CC inhibited by Zn(2+), Mg(2+) and Cu(2+). {ECO:0000269|PubMed:23644747}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.4 mM for D-psicose (at pH 7 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:23644747};
CC KM=339 mM for D-tagatose (at pH 7 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:23644747};
CC Note=kcat is 49 sec(-1) for epimerase activity with D-psicose as
CC substrate (at pH 7 and 55 degrees Celsius). kcat is 4.7 sec(-1) for
CC epimerase activity with D-tagatose as substrate (at pH 7 and 55
CC degrees Celsius). {ECO:0000269|PubMed:23644747};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:23644747};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:23644747};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23644747}.
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
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DR EMBL; ABCC02000001; EDP19602.1; -; Genomic_DNA.
DR AlphaFoldDB; A8RG82; -.
DR SMR; A8RG82; -.
DR STRING; 411902.CLOBOL_00069; -.
DR EnsemblBacteria; EDP19602; EDP19602; CLOBOL_00069.
DR KEGG; ag:EDP19602; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_050006_8_2_9; -.
DR BRENDA; 5.1.3.30; 13725.
DR Proteomes; UP000005396; Unassembled WGS sequence.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:UniProtKB.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
PE 1: Evidence at protein level;
KW Cobalt; Isomerase; Manganese; Metal-binding.
FT CHAIN 1..301
FT /note="D-psicose 3-epimerase"
FT /id="PRO_0000435453"
FT ACT_SITE 162
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 256
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
FT BINDING 195..198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B8I944"
SQ SEQUENCE 301 AA; 34226 MW; 569D96081A5AE6A2 CRC64;
MRYFKEEVAG MKYGIYFAYW TKEWFADYKK YMDKVSALGF DVLEISCAAL RDVYTTKEQL
IELREYAKEK GLVLTAGYGP TKAENLCSED PEAVRRAMTF FKDLLPKLQL MDIHILGGGL
YSYWPVDFTI NNDKQGDRAR AVRNLRELSK TAEECDVVLG MEVLNRYEGY ILNTCEEAID
FVDEIGSSHV KIMLDTFHMN IEETNMADAI RKAGDRLGHL HLGEQNRLVP GKGSLPWAEI
GQALRDINYQ GAAVMEPFVM QGGTIGSEIK VWRDMVPDLS EEALDRDAKG ALEFCRHVFG
I
