Reviewed,
UniProtKB/Swiss-Prot Q51945 (TTUC_PSEPU)
Last modified
February 9, 2010.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| Organism | Pseudomonas putida |
| Taxonomic identifier | 303 [NCBI] |
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 365 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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; D-glycerate from L-tartrate: step 1/1. |
| Subunit structure | Homodimer Probable. |
| Subcellular location | |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Magnesium Manganese NAD |
| Molecular function | Lyase Oxidoreductase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | D-malate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: EC NAD or NADH bindingInferred from electronic annotation. Source: InterPro magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW tartrate decarboxylase activityInferred from electronic annotation. Source: EC tartrate dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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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: 8053675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 276-294. Strain: ATCC 17642 / 276. |
| [2] | "Characterization of the multiple catalytic activities of tartrate dehydrogenase." Tipton P.A., Peisach J. Biochemistry 29:1749-1756(1990) [PubMed: 2184888] [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: 8457548] [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: 12356321] [Abstract] Cited for: ENZYME KINETICS. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U05986 Genomic DNA. Translation: AAA60327.1. | ||||||||||||
| PIR | S48640. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.1.1.83. 403. 1.1.1.93. 403. 4.1.1.73. 403. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR011829. TTC_DH. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.718.10. IDH_IMDH. 1 hit. | ||||||||||||
| PANTHER | PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF8. TTC_DH. 1 hit. | ||||||||||||
| Pfam | PF00180. Iso_dh. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR02089. TTC. 1 hit. | ||||||||||||
| PROSITE | PS00470. IDH_IMDH. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | TTUC_PSEPU | ||||||||
| Accession | Primary (citable) accession number: Q51945 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
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 |

Clusters with


