DT3E_CERSP
ID DT3E_CERSP Reviewed; 295 AA.
AC C1KKR1;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=D-tagatose 3-epimerase {ECO:0000303|PubMed:19205890};
DE Short=DTE {ECO:0000303|PubMed:19205890};
DE EC=5.1.3.31 {ECO:0000269|PubMed:19205890};
DE AltName: Full=D-ribulose 3-epimerase {ECO:0000303|PubMed:19205890};
DE AltName: Full=Ketose 3-epimerase {ECO:0000303|PubMed:19205890};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=SK-011;
RX PubMed=19205890; DOI=10.1007/s10529-009-9942-3;
RA Zhang L., Mu W., Jiang B., Zhang T.;
RT "Characterization of D-tagatose-3-epimerase from Rhodobacter sphaeroides
RT that converts D-fructose into D-psicose.";
RL Biotechnol. Lett. 31:857-862(2009).
CC -!- FUNCTION: Catalyzes the epimerization of various ketoses at the C(3)
CC position. It is able to interconvert D-tagatose and D-fructose to D-
CC sorbose and D-psicose, respectively. The enzyme is also able to accept
CC other ketopentoses such as D-ribulose and D-xylulose with lower
CC efficiency. {ECO:0000269|PubMed:19205890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048,
CC ChEBI:CHEBI:13022, ChEBI:CHEBI:47693; EC=5.1.3.31;
CC Evidence={ECO:0000269|PubMed:19205890};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360,
CC ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1.3.31;
CC Evidence={ECO:0000269|PubMed:19205890};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose = D-xylulose; Xref=Rhea:RHEA:51544,
CC ChEBI:CHEBI:17140, ChEBI:CHEBI:17173; EC=5.1.3.31;
CC Evidence={ECO:0000269|PubMed:19205890};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19205890};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9. The enzyme is stable from 8 to 10.
CC {ECO:0000269|PubMed:19205890};
CC Temperature dependence:
CC Optimum temperature is around 40 degrees Celsius. The enzyme is
CC stable below 40 degrees Celsius, but decreases with increasing
CC temperature. {ECO:0000269|PubMed:19205890};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19205890}.
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ851309; ACO59490.1; -; Genomic_DNA.
DR RefSeq; WP_011842344.1; NZ_CP033443.1.
DR AlphaFoldDB; C1KKR1; -.
DR SMR; C1KKR1; -.
DR GeneID; 57472054; -.
DR BRENDA; 5.1.3.31; 5383.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Isomerase; Manganese; Metal-binding.
FT CHAIN 1..295
FT /note="D-tagatose 3-epimerase"
FT /id="PRO_0000435306"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 250
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 189..192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 189
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O50580"
SQ SEQUENCE 295 AA; 31788 MW; D72AAD42D0AFF3FF CRC64;
MKNPVGIISM QFIRPFTSES LHFLKKSRAL GFDFIELLVP EPEDGLDAAE VRRICEGEGL
GLVLAARVNL QRSIASEEAA ARAGGRDYLK YCIEAAEALG ATIVGGPLYG EPLVFAGRPP
FPWTAEQIAT RAARTVEGLA EVAPLAASAG KVFGLEPLNR FETDIVNTTA QAIEVVDAVG
SPGLGVMLDT FHMNMEERSI PDAIRATGAR LVHFQANENH RGFPGTGTMD WTAIARALGQ
AGYAGPVSLE PFRRDDERVA LPIAHWRAPH EDEDEKLRAG LGLIRSAITL AEVTH
