DT3E_PSECI
ID DT3E_PSECI Reviewed; 290 AA.
AC O50580;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=D-tagatose 3-epimerase {ECO:0000303|Ref.2};
DE Short=DTE {ECO:0000303|Ref.2};
DE EC=5.1.3.31 {ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2};
DE AltName: Full=D-ribulose 3-epimerase {ECO:0000303|Ref.2};
DE AltName: Full=Ketose 3-epimerase {ECO:0000303|Ref.2};
OS Pseudomonas cichorii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=36746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ST-24;
RA Ishida Y., Kamiya T., Itoh H., Kimura Y., Izumori K.;
RT "Cloning and characterization of D-tagatose 3-epimerase gene from
RT Pseudomonas cichorii ST-24.";
RL J. Ferment. Bioeng. 83:529-534(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBSTRATE SPECIFICITY, AND
RP SUBUNIT.
RC STRAIN=ST-24;
RA Itoh H., Okaya H., Khan A.R., Tajima S., Hayakawa S., Izumori K.;
RT "Purification and characterization of D-tagatose 3-epimerase from
RT Pseudomonas sp. ST-244.";
RL Biosci. Biotechnol. Biochem. 58:2168-2171(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH MANGANESE ION AND
RP SUBSTRATE ANALOGS, FUNCTION, COFACTOR, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=17936787; DOI=10.1016/j.jmb.2007.09.033;
RA Yoshida H., Yamada M., Nishitani T., Takada G., Izumori K., Kamitori S.;
RT "Crystal structures of D-tagatose 3-epimerase from Pseudomonas cichorii and
RT its complexes with D-tagatose and D-fructose.";
RL J. Mol. Biol. 374:443-453(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS IDF8 AND ILS6 IN COMPLEX
RP WITH MANGANESE ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF SER-37 AND GLN-183, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP SUBUNIT.
RX PubMed=25655925; DOI=10.1002/cbic.201402620;
RA Bosshart A., Hee C.S., Bechtold M., Schirmer T., Panke S.;
RT "Directed divergent evolution of a thermostable D-tagatose epimerase
RT towards improved activity for two hexose substrates.";
RL ChemBioChem 16:592-601(2015).
CC -!- FUNCTION: Catalyzes the epimerization of various ketoses at the C(3)
CC position. It is able to interconvert D-tagatose and D-ribulose to D-
CC sorbose and D-xylulose, respectively. The enzyme is also able to accept
CC other ketopentoses such as D-psicose with lower efficiency.
CC {ECO:0000269|PubMed:17936787, ECO:0000269|PubMed:25655925,
CC ECO:0000269|Ref.2}.
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:25655925, ECO:0000269|Ref.2};
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:25655925, ECO:0000269|Ref.2};
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|Ref.2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17936787, ECO:0000269|PubMed:25655925,
CC ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Strongly inhibited (about 90% of the enzyme
CC activity) by Ag(+), Hg(2+) and p-chloromercuribenzoic acid. Cu(2+) and
CC Zn(2+) inhibit about 60% of the enzyme activity. {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 mM for D-tagatose {ECO:0000269|Ref.2};
CC Vmax=30 umol/min/mg enzyme with D-tagatose as substrate
CC {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is between 7 and 9 at 30 degrees Celsius. The enzyme is
CC stable from 7 to 11 at 30 degrees Celsius. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is around 60 degrees Celsius. The enzyme is
CC stable up to 60 degrees Celsius for 10 minutes. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17936787,
CC ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
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DR EMBL; AB000361; BAA24429.1; -; Genomic_DNA.
DR PDB; 2OU4; X-ray; 2.50 A; A/B/C/D=1-290.
DR PDB; 2QUL; X-ray; 1.79 A; A/B/C/D=1-290.
DR PDB; 2QUM; X-ray; 2.28 A; A/B/C/D=1-290.
DR PDB; 2QUN; X-ray; 2.06 A; A/B/C/D=1-290.
DR PDB; 4PFH; X-ray; 1.90 A; A/B=1-290.
DR PDB; 4PGL; X-ray; 2.10 A; A/B/C/D=1-290.
DR PDB; 4XSL; X-ray; 1.60 A; A/B/C/D=1-290.
DR PDB; 4XSM; X-ray; 2.30 A; A/B/C/D=1-290.
DR PDB; 4YTQ; X-ray; 1.90 A; A/B/C/D=1-290.
DR PDB; 4YTR; X-ray; 1.90 A; A/B/C/D=1-290.
DR PDB; 4YTS; X-ray; 2.14 A; A/B/C/D=1-290.
DR PDB; 4YTT; X-ray; 1.80 A; A/B/C/D=1-290.
DR PDB; 4YTU; X-ray; 2.20 A; A/B/C/D=1-290.
DR PDB; 5J8L; X-ray; 1.73 A; A/B/C/D=1-290.
DR PDBsum; 2OU4; -.
DR PDBsum; 2QUL; -.
DR PDBsum; 2QUM; -.
DR PDBsum; 2QUN; -.
DR PDBsum; 4PFH; -.
DR PDBsum; 4PGL; -.
DR PDBsum; 4XSL; -.
DR PDBsum; 4XSM; -.
DR PDBsum; 4YTQ; -.
DR PDBsum; 4YTR; -.
DR PDBsum; 4YTS; -.
DR PDBsum; 4YTT; -.
DR PDBsum; 4YTU; -.
DR PDBsum; 5J8L; -.
DR AlphaFoldDB; O50580; -.
DR SMR; O50580; -.
DR BioCyc; MetaCyc:MON-17957; -.
DR BRENDA; 5.1.3.31; 5107.
DR EvolutionaryTrace; O50580; -.
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 3D-structure; Direct protein sequencing; Isomerase; Manganese;
KW Metal-binding.
FT CHAIN 1..290
FT /note="D-tagatose 3-epimerase"
FT /id="PRO_0000209107"
FT ACT_SITE 152
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 246
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17936787"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17936787,
FT ECO:0000269|PubMed:25655925"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17936787,
FT ECO:0000269|PubMed:25655925"
FT BINDING 185..188
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17936787,
FT ECO:0000269|PubMed:25655925"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17936787,
FT ECO:0000269|PubMed:25655925"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17936787,
FT ECO:0000269|PubMed:25655925"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17936787,
FT ECO:0000269|PubMed:25655925"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17936787,
FT ECO:0000269|PubMed:25655925"
FT MUTAGEN 37
FT /note="S->N: Moderate increase in catalytic efficiency for
FT D-fructose."
FT /evidence="ECO:0000269|PubMed:25655925"
FT MUTAGEN 183
FT /note="Q->H: Shows a pronounced increase in catalytic
FT efficiency for L-sorbose. It seems that this mutation
FT switches the substrate preference from hexoses with a 4S,5R
FT configuration to those with a 4R,5S configuration."
FT /evidence="ECO:0000269|PubMed:25655925"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4XSL"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:4PGL"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:4XSL"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:4XSL"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 80..100
FT /evidence="ECO:0007829|PDB:4XSL"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:4XSL"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4XSL"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:4XSL"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:4XSL"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:4XSL"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:4XSL"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:4XSL"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:4XSL"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:4PGL"
FT HELIX 271..290
FT /evidence="ECO:0007829|PDB:4XSL"
SQ SEQUENCE 290 AA; 32615 MW; 3AF54FC94DD83815 CRC64;
MNKVGMFYTY WSTEWMVDFP ATAKRIAGLG FDLMEISLGE FHNLSDAKKR ELKAVADDLG
LTVMCCIGLK SEYDFASPDK SVRDAGTEYV KRLLDDCHLL GAPVFAGLTF CAWPQSPPLD
MKDKRPYVDR AIESVRRVIK VAEDYGIIYA LEVVNRFEQW LCNDAKEAIA FADAVDSPAC
KVQLDTFHMN IEETSFRDAI LACKGKMGHF HLGEANRLPP GEGRLPWDEI FGALKEIGYD
GTIVMEPFMR KGGSVSRAVG VWRDMSNGAT DEEMDERARR SLQFVRDKLA
