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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)DescriptionActionsGraphical viewLength
Binding sitei66Substrate1 Publication1
Metal bindingi152Manganese2 Publications1
Binding sitei158Substrate2 Publications1
Metal bindingi185Manganese2 Publications1
Metal bindingi211Manganese; via pros nitrogen2 Publications1
Binding sitei217Substrate2 Publications1
Metal bindingi246Manganese2 Publications1

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)DescriptionActionsGraphical viewLength
Mutagenesisi37S → N: Moderate increase in catalytic efficiency for D-fructose. 1 Publication1
Mutagenesisi183Q → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002091071 – 290D-tagatose 3-epimeraseAdd BLAST290

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Turni8 – 11Combined sources4
Beta strandi13 – 15Combined sources3
Helixi19 – 28Combined sources10
Beta strandi32 – 38Combined sources7
Helixi41 – 43Combined sources3
Helixi46 – 59Combined sources14
Beta strandi62 – 69Combined sources8
Helixi71 – 73Combined sources3
Helixi80 – 100Combined sources21
Beta strandi103 – 114Combined sources12
Helixi125 – 136Combined sources12
Helixi139 – 145Combined sources7
Beta strandi148 – 152Combined sources5
Turni156 – 158Combined sources3
Helixi165 – 175Combined sources11
Beta strandi180 – 185Combined sources6
Helixi186 – 192Combined sources7
Helixi196 – 202Combined sources7
Turni203 – 206Combined sources4
Beta strandi207 – 212Combined sources6
Helixi227 – 236Combined sources10
Beta strandi241 – 245Combined sources5
Helixi254 – 259Combined sources6
Turni265 – 268Combined sources4
Helixi271 – 290Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO50580.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni185 – 188Substrate binding2 Publications4

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
PDB 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.
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...

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: November 2, 2016
This is version 53 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.