Reviewed, UniProtKB/Swiss-Prot Q51945 (TTUC_PSEPU)

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; 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.

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 binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW tartrate decarboxylase activity Inferred from electronic annotation. Source: EC tartrate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 365	364	Tartrate dehydrogenase/decarboxylase		PRO_0000083819

Sequences

	Sequence		Length	Mass (Da)
	Q51945-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B26682F137DB49D9	FASTA	365	40,630
	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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FLK	X-ray	2.00	A/B/C/D	1-365	[»]

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

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Entry information

Entry name

TTUC_PSEPU

Accession

Primary (citable) accession number: Q51945

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)