[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-22 AND 276-294. STRAIN=ATCC 17642 / 276; DOI=10.1006/abbi.1994.1352; PubMed=8053675 [NCBI, ExPASy, EBI, Israel, Japan] Tipton P.A., Beecher B.S.; "Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases."; Arch. Biochem. Biophys. 313:15-21(1994).
[2]	CHARACTERIZATION. DOI=10.1021/bi00459a013; PubMed=2184888 [NCBI, ExPASy, EBI, Israel, Japan] Tipton P.A., Peisach J.; "Characterization of the multiple catalytic activities of tartrate dehydrogenase."; Biochemistry 29:1749-1756(1990).
[3]	ENZYME KINETICS. DOI=10.1021/bi00062a013; PubMed=8457548 [NCBI, ExPASy, EBI, Israel, Japan] Tipton P.A.; "Intermediate partitioning in the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate."; Biochemistry 32:2822-2827(1993).
[4]	ENZYME KINETICS. DOI=10.1021/bi026278g; PubMed=12356321 [NCBI, ExPASy, EBI, Israel, Japan] Karsten W.E., Tipton P.A., Cook P.F.; "Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD."; Biochemistry 41:12193-12199(2002).

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.
CATALYTIC ACTIVITY: Meso-tartrate + NAD⁺ = oxaloglycolate + NADH.
CATALYTIC ACTIVITY: (R,R)-tartrate + NAD⁺ = oxaloglycolate + NADH.
CATALYTIC ACTIVITY: (R,R)-tartrate = D-glycerate + CO₂.
CATALYTIC ACTIVITY: (R)-malate + NAD⁺ = pyruvate + CO₂ + NADH.
COFACTOR: Manganese.
COFACTOR: Magnesium.
COFACTOR: Potassium.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.06 mM for D-malate;
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;

PATHWAY: Carbohydrate acid metabolism; tartaric acid degradation; 2-hydroxy-3-oxosuccinic acid from L-tartaric acid: step 1/1 .
PATHWAY: Carbohydrate acid metabolism; tartaric acid degradation; 2-hydroxy-3-oxosuccinic acid from meso-tartaric acid: step 1/1 .
PATHWAY: Carbohydrate acid metabolism; tartaric acid degradation; D-glyceric acid from L-tartaric acid: step 1/1 .
SUBUNIT: Homodimer (Probable).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U05986; AAA60327.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48640; S48640.

3D structure databases

HSSP

P00351; 1XAA. [HSSP ENTRY / PDB]

ModBase

Q51945.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0046553;	Molecular function: D-malate dehydrogenase (decarboxylating) activity (inferred from electronic annotation from EC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050319;	Molecular function: tartrate decarboxylase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001804; IsoCit_IM_DHase.
IPR011829; TTC_DH.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF8; TTC_DH; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02089; TTC; 1.

PROSITE

PS00470; IDH_IMDH; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; Lyase; Magnesium; Manganese; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 365`	`364`	`Tartrate dehydrogenase/decarboxylase.`	`PRO_0000083819`

Sequence information

Length: 365 AA [This is the length of the unprocessed precursor]

Molecular weight: 40630 Da [This is the MW of the unprocessed precursor]

CRC64: B26682F137DB49D9 [This is a checksum on the sequence]

        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

Q51945 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools