[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=AB4; Salomone J.-Y., Szegedi E., Cobanov P., Otten L.; Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.

Comments

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.
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 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
INDUCTION: By tartrate.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Copyright

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Cross-references

Sequence databases

EMBL

AF010261; AAB65746.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00351; 1DR8. [HSSP ENTRY / PDB]

ModBase

O34295.

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:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050319;	Molecular function: tartrate decarboxylase activity (inferred from electronic annotation from EC).
GO:0009027;	Molecular function: tartrate dehydrogenase activity (inferred from electronic annotation from InterPro).
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

ProtoNet

O34295.

UniRef

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

Keywords

Cytoplasm; Lyase; NAD; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 358`	`358`		`Probable tartrate dehydrogenase/decarboxylase ttuC'.`	`PRO_0000083817`

Sequence information

Length: 358 AA [This is the length of the unprocessed precursor]

Molecular weight: 38730 Da [This is the MW of the unprocessed precursor]

CRC64: BD24225EA131B5E7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MREYKIAAIP ADGIGPEVIA AGLQVLEALE QRSGDFKIHT ETFDWGSDYY KKHGVMMPAD 

        70         80         90        100        110        120 
GLDKLKKFDA IFFGAVGAPD VPDHITLWGL RLPICQGFDQ YANVRPTKIL PGITPPLRNC 

       130        140        150        160        170        180 
GPGDLDWVIV RENSEGEYSG HGGRAHRGLP EEVGTEVAIF TRVGVTRIMR YAFKLAQARP 

       190        200        210        220        230        240 
RKLLTVVTKS NAQRHGMVMW DEIAAEVATE FPDVTWDKML VDAMTVRMTL KPETLDTIVA 

       250        260        270        280        290        300 
TNLHADILSD LAGALAGSLG VAPTANIDPE RRFPSMFEPI HGSAFDITGK GIANPIATFW 

       310        320        330        340        350 
TAAQMLEHLG ERDAAARLMG AVERVTEAGI LTPDVGGTAN TSQVTEAVCN AIAGSNII

O34295 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