[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan] Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.; "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."; DNA Res. 3:379-392(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

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.
INTERACTION:
P0A6F5:groL; NbExp=1; IntAct=EBI-560661, EBI-543750;
P0A6N1:tufA; NbExp=1; IntAct=EBI-560661, EBI-301077;
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

U00096; AAC74870.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15595.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H64940; H64940.

RefSeq

AP_002419.1; -.
NP_416314.1; -.

3D structure databases

HSSP

P30125; 1CM7. [HSSP ENTRY / PDB]

ModBase

P76251.

Protein-protein interaction databases

DIP

DIP:11800N; -.

IntAct

P76251; -.

Enzyme and pathway databases

BioCyc

EcoCyc:G6986-MON; -.
MetaCyc:G6986-MON; -.

Organism-specific databases

EchoBASE

EB3280; -.

EcoGene

EG13507; yeaU.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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.

Genome annotation databases

GeneID

946319; -.

GenomeReviews

U00096_GR; b1800.
AP009048_GR; JW1789.

KEGG

ecj:JW1789; -.
eco:b1800; -.

Phylogenomic databases

HOGENOM

P76251; -.

Other

LinkHub

P76251; -.

Genome annotation databases

CMR

P76251; b1800.

Other

UniRef

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

Keywords

Complete proteome; Cytoplasm; Lyase; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 361`	`361`		`Probable tartrate dehydrogenase/decarboxylase.`	`PRO_0000083818`

Sequence information

Length: 361 AA [This is the length of the unprocessed precursor]

Molecular weight: 40315 Da [This is the MW of the unprocessed precursor]

CRC64: 6D77B609729925D7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMKTMRIAAI PGDGIGKEVL PEGIRVLQAA AERWGFALSF EQMEWASCEY YSHHGKMMPD 

        70         80         90        100        110        120 
DWHEQLSRFD AIYFGAVGWP DTVPDHISLW GSLLKFRREF DQYVNLRPVR LFPGVPCPLA 

       130        140        150        160        170        180 
GKQPGDIDFY VVRENTEGEY SSLGGRVNEG TEHEVVIQES VFTRRGVDRI LRYAFELAQS 

       190        200        210        220        230        240 
RPRKTLTSAT KSNGLAISMP YWDERVEAMA ENYPEIRWDK QHIDILCARF VMQPERFDVV 

       250        260        270        280        290        300 
VASNLFGDIL SDLGPACTGT IGIAPSANLN PERTFPSLFE PVHGSAPDIY GKNIANPIAT 

       310        320        330        340        350        360 
IWAGAMMLDF LGNGDERFQQ AHNGILAAIE EVIAHGPKTP DMKGNATTPQ VADAICKIIL 


R

P76251 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