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Q51945 (TTUC_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tartrate dehydrogenase/decarboxylase
Short name=TDH
EC=1.1.1.93
EC=4.1.1.73
Alternative name(s):
D-malate dehydrogenase [decarboxylating]
EC=1.1.1.83
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has multiple catalytic activities. Apart from catalyzing the oxidation of (+)-tartrate to oxaloglycolate, also converts meso-tartrate to D-glycerate and catalyzes the oxidative decarboxylation of D-malate to pyruvate.

Catalytic activity

Tartrate + NAD+ = oxaloglycolate + NADH.

Meso-tartrate + NAD+ = oxaloglycolate + NADH.

(R,R)-tartrate + NAD+ = oxaloglycolate + NADH.

(R,R)-tartrate = D-glycerate + CO2.

(R)-malate + NAD+ = pyruvate + CO2 + NADH.

Cofactor

Manganese.

Magnesium.

Potassium.

Pathway

Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy-3-oxosuccinate from L-tartrate: step 1/1.

Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy-3-oxosuccinate from meso-tartrate: step 1/1.

Carbohydrate acid metabolism; tartrate degradation; D-glycerate from L-tartrate: step 1/1.

Subunit structure

Homodimer Probable.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Biophysicochemical properties

Kinetic parameters:

KM=0.06 mM for D-malate Ref.3 Ref.4

Temperature dependence:

Thermostable. Fully active after heating 10 min at 65 degrees Celsius and retains half its catalytic activity after 10 min at 72 degrees Celsius. Inactive after heating 10 min at 78 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 365364Tartrate dehydrogenase/decarboxylase
PRO_0000083819

Secondary structure

1 ................................................................. 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q51945 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B26682F137DB49D9

FASTA36540,630
        10         20         30         40         50         60 
MPAHSFRIAA IPGDGIGLEV LPEGIRVLEA AALKHGLALE FDTFEWASCD YYLQHGKMMP 

        70         80         90        100        110        120 
DDWAEQLKQY DAIYFGAVDW PDKVPDHISL WGSLLKFRRE FDQYVNIRPV RLFPGVPCAL 

       130        140        150        160        170        180 
ANRKVGDIDF VVVRENTEGE YSSLGGIMFE NTENEIVIQE SIFTRRGVDR ILKYAFDLAE 

       190        200        210        220        230        240 
KRERKHVTSA TKSNGMAISM PYWDKRTEAM AAHYPHVSWD KQHIDILCAR FVLQPERFDV 

       250        260        270        280        290        300 
VVVASNLFGD ILSDLGPACA GTIGIAPSAN LNPERNFPSL FEPVHGSAPD IFGKNIANPI 

       310        320        330        340        350        360 
AMIWSGALML EFLGQGDERY QRAHDDMLNA IERVIADGSV TPDMGGTLST QQVGAAISDT 


LARLD

« Hide

References

[1]"Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases."
Tipton P.A., Beecher B.S.
Arch. Biochem. Biophys. 313:15-21(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 276-294.
Strain: ATCC 17642 / NCIMB 10804 / 276.
[2]"Characterization of the multiple catalytic activities of tartrate dehydrogenase."
Tipton P.A., Peisach J.
Biochemistry 29:1749-1756(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Intermediate partitioning in the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate."
Tipton P.A.
Biochemistry 32:2822-2827(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME KINETICS.
[4]"Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD."
Karsten W.E., Tipton P.A., Cook P.F.
Biochemistry 41:12193-12199(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME KINETICS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U05986 Genomic DNA. Translation: AAA60327.1.
PIRS48640.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FLKX-ray2.00A/B/C/D1-365[»]
3FMXX-ray2.95X1-365[»]
ProteinModelPortalQ51945.
ModBaseSearch...

Proteomic databases

PRIDEQ51945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00839; UER00800.
UPA00839; UER00801.
UPA00839; UER00803.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR011829. TTC_DH.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR02089. TTC. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ51945.

Entry information

Entry nameTTUC_PSEPU
AccessionPrimary (citable) accession number: Q51945
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents