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Protein

D-tagatose 3-epimerase

Gene
N/A
Organism
Pseudomonas cichorii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of various ketoses at the C3 position. It is able to interconvert D-tagatose and D-ribulose to D-sorbose and D-xylulose, respectively. The enzyme is also able to accept other ketopentoses such as D-psicose with lower efficiency.3 Publications

Catalytic activityi

D-tagatose = D-sorbose.2 Publications
D-psicose = D-fructose.2 Publications
D-ribulose = D-xylulose.1 Publication

Cofactori

Mn2+3 Publications

Enzyme regulationi

Strongly inhibited (about 90% of the enzyme activity) by Ag+, Hg2+ and p-chloromercuribenzoic acid. Cu2+ and Zn2+ inhibit about 60% of the enzyme activity.1 Publication

Kineticsi

  1. KM=55 mM for D-tagatose1 Publication
  1. Vmax=30 µmol/min/mg enzyme with D-tagatose as substrate1 Publication

pH dependencei

Optimum pH is between 7 and 9 at 30 degrees Celsius. The enzyme is stable from 7 to 11 at 30 degrees Celsius.1 Publication

Temperature dependencei

Optimum temperature is around 60 degrees Celsius. The enzyme is stable up to 60 degrees Celsius for 10 minutes.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661Substrate1 Publication
Metal bindingi152 – 1521Manganese2 Publications
Binding sitei158 – 1581Substrate2 Publications
Metal bindingi185 – 1851Manganese2 Publications
Metal bindingi211 – 2111Manganese; via pros nitrogen2 Publications
Binding sitei217 – 2171Substrate2 Publications
Metal bindingi246 – 2461Manganese2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17957.
BRENDAi5.1.3.31. 5107.

Names & Taxonomyi

Protein namesi
Recommended name:
D-tagatose 3-epimerase1 Publication (EC:5.1.3.312 Publications)
Short name:
DTE1 Publication
Alternative name(s):
D-ribulose 3-epimerase1 Publication (EC:5.1.3.-1 Publication)
Ketose 3-epimerase1 Publication
OrganismiPseudomonas cichorii
Taxonomic identifieri36746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371S → N: Moderate increase in catalytic efficiency for D-fructose. 1 Publication
Mutagenesisi183 – 1831Q → H: Shows a pronounced increase in catalytic efficiency for L-sorbose. It seems that this mutation switches the substrate preference from hexoses with a 4S,5R configuration to those with a 4R,5S configuration. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290D-tagatose 3-epimerasePRO_0000209107Add
BLAST

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Turni8 – 114Combined sources
Beta strandi13 – 153Combined sources
Helixi19 – 2810Combined sources
Beta strandi32 – 387Combined sources
Helixi41 – 433Combined sources
Helixi46 – 5914Combined sources
Beta strandi62 – 698Combined sources
Helixi71 – 733Combined sources
Helixi80 – 10021Combined sources
Beta strandi103 – 11412Combined sources
Helixi125 – 13612Combined sources
Helixi139 – 1457Combined sources
Beta strandi148 – 1525Combined sources
Turni156 – 1583Combined sources
Helixi165 – 17511Combined sources
Beta strandi180 – 1856Combined sources
Helixi186 – 1927Combined sources
Helixi196 – 2027Combined sources
Turni203 – 2064Combined sources
Beta strandi207 – 2126Combined sources
Helixi227 – 23610Combined sources
Beta strandi241 – 2455Combined sources
Helixi254 – 2596Combined sources
Turni265 – 2684Combined sources
Helixi271 – 29020Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OU4X-ray2.50A/B/C/D1-290[»]
2QULX-ray1.79A/B/C/D1-290[»]
2QUMX-ray2.28A/B/C/D1-290[»]
2QUNX-ray2.06A/B/C/D1-290[»]
4PFHX-ray1.90A/B1-290[»]
4PGLX-ray2.10A/B/C/D1-290[»]
4XSLX-ray1.60A/B/C/D1-290[»]
4XSMX-ray2.30A/B/C/D1-290[»]
4YTQX-ray1.90A/B/C/D1-290[»]
4YTRX-ray1.90A/B/C/D1-290[»]
4YTSX-ray2.14A/B/C/D1-290[»]
4YTTX-ray1.80A/B/C/D1-290[»]
4YTUX-ray2.20A/B/C/D1-290[»]
5J8LX-ray1.73A/B/C/D1-290[»]
ProteinModelPortaliO50580.
SMRiO50580. Positions 1-290.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO50580.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1884Substrate binding2 Publications

Sequence similaritiesi

Belongs to the hyi family.Curated

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.

Sequencei

Sequence statusi: Complete.

O50580-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKVGMFYTY WSTEWMVDFP ATAKRIAGLG FDLMEISLGE FHNLSDAKKR
60 70 80 90 100
ELKAVADDLG LTVMCCIGLK SEYDFASPDK SVRDAGTEYV KRLLDDCHLL
110 120 130 140 150
GAPVFAGLTF CAWPQSPPLD MKDKRPYVDR AIESVRRVIK VAEDYGIIYA
160 170 180 190 200
LEVVNRFEQW LCNDAKEAIA FADAVDSPAC KVQLDTFHMN IEETSFRDAI
210 220 230 240 250
LACKGKMGHF HLGEANRLPP GEGRLPWDEI FGALKEIGYD GTIVMEPFMR
260 270 280 290
KGGSVSRAVG VWRDMSNGAT DEEMDERARR SLQFVRDKLA
Length:290
Mass (Da):32,615
Last modified:June 1, 1998 - v1
Checksum:i3AF54FC94DD83815
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000361 Genomic DNA. Translation: BAA24429.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000361 Genomic DNA. Translation: BAA24429.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OU4X-ray2.50A/B/C/D1-290[»]
2QULX-ray1.79A/B/C/D1-290[»]
2QUMX-ray2.28A/B/C/D1-290[»]
2QUNX-ray2.06A/B/C/D1-290[»]
4PFHX-ray1.90A/B1-290[»]
4PGLX-ray2.10A/B/C/D1-290[»]
4XSLX-ray1.60A/B/C/D1-290[»]
4XSMX-ray2.30A/B/C/D1-290[»]
4YTQX-ray1.90A/B/C/D1-290[»]
4YTRX-ray1.90A/B/C/D1-290[»]
4YTSX-ray2.14A/B/C/D1-290[»]
4YTTX-ray1.80A/B/C/D1-290[»]
4YTUX-ray2.20A/B/C/D1-290[»]
5J8LX-ray1.73A/B/C/D1-290[»]
ProteinModelPortaliO50580.
SMRiO50580. Positions 1-290.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17957.
BRENDAi5.1.3.31. 5107.

Miscellaneous databases

EvolutionaryTraceiO50580.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of D-tagatose 3-epimerase gene from Pseudomonas cichorii ST-24."
    Ishida Y., Kamiya T., Itoh H., Kimura Y., Izumori K.
    J. Ferment. Bioeng. 83:529-534(1997)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ST-24.
  2. "Purification and characterization of D-tagatose 3-epimerase from Pseudomonas sp. ST-244."
    Itoh H., Okaya H., Khan A.R., Tajima S., Hayakawa S., Izumori K.
    Biosci. Biotechnol. Biochem. 58:2168-2171(1994)
    Cited for: PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT.
    Strain: ST-24.
  3. "Crystal structures of D-tagatose 3-epimerase from Pseudomonas cichorii and its complexes with D-tagatose and D-fructose."
    Yoshida H., Yamada M., Nishitani T., Takada G., Izumori K., Kamitori S.
    J. Mol. Biol. 374:443-453(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH MANGANESE ION AND SUBSTRATE ANALOGS, FUNCTION, COFACTOR, REACTION MECHANISM, SUBUNIT.
  4. "Directed divergent evolution of a thermostable D-tagatose epimerase towards improved activity for two hexose substrates."
    Bosshart A., Hee C.S., Bechtold M., Schirmer T., Panke S.
    ChemBioChem 16:592-601(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS IDF8 AND ILS6 IN COMPLEX WITH MANGANESE ION AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-37 AND GLN-183, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiDT3E_PSECI
AccessioniPrimary (citable) accession number: O50580
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.