ID   TTUC3_AGRVI             Reviewed;         358 AA.
AC   O34296;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Probable tartrate dehydrogenase/decarboxylase ttuC';
DE            Short=TDH;
DE            EC=1.1.1.93;
DE            EC=4.1.1.73;
DE   AltName: Full=D-malate dehydrogenase [decarboxylating];
DE            EC=1.1.1.83;
GN   Name=ttuC';
OS   Agrobacterium vitis (Rhizobium vitis).
OG   Plasmid pTiAB3.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AB3;
RA   Salomone J.-Y., Szegedi E., Cobanov P., Otten L.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Tartrate + NAD(+) = oxaloglycolate + NADH.
CC   -!- CATALYTIC ACTIVITY: Meso-tartrate + NAD(+) = oxaloglycolate +
CC       NADH.
CC   -!- CATALYTIC ACTIVITY: (R,R)-tartrate + NAD(+) = oxaloglycolate +
CC       NADH.
CC   -!- CATALYTIC ACTIVITY: (R,R)-tartrate = D-glycerate + CO(2).
CC   -!- CATALYTIC ACTIVITY: (R)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC   -!- PATHWAY: Carbohydrate acid metabolism; tartaric acid degradation;
CC       2-hydroxy-3-oxosuccinic acid from L-tartaric acid: step 1/1.
CC   -!- PATHWAY: Carbohydrate acid metabolism; tartaric acid degradation;
CC       2-hydroxy-3-oxosuccinic acid from meso-tartaric acid: step 1/1.
CC   -!- PATHWAY: Carbohydrate acid metabolism; tartaric acid degradation;
CC       D-glyceric acid from L-tartaric acid: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- INDUCTION: By tartrate.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AF010263; AAB65748.1; -; Genomic_DNA.
DR   HSSP; P00351; 1DR8.
DR   BRENDA; 1.1.1.83; 97084.
DR   BRENDA; 1.1.1.93; 97084.
DR   BRENDA; 4.1.1.73; 97084.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) ac...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0050319; F:tartrate decarboxylase activity; IEA:EC.
DR   GO; GO:0009027; F:tartrate dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR011829; TTC_DH.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   PANTHER; PTHR11835:SF8; TTC_DH; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR02089; TTC; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; NAD; Oxidoreductase; Plasmid.
FT   CHAIN         1    358       Probable tartrate
FT                                dehydrogenase/decarboxylase ttuC'.
FT                                /FTId=PRO_0000083815.
SQ   SEQUENCE   358 AA;  38760 MW;  0820225EA131A9FA CRC64;
     MREYKIAAIP ADGIGPEVIA AGLQVLEALE QRSGDFKIHT ETFDWGSDYY KKHGVMMPAD
     GLDKLKKFDA IFFGAVGAPD VPDHITLWGL RLPICQGFDQ YANVRPTKIL PGITPPLRNC
     GPGDLDWVIV RENSEGEYSG HGGRAHRGLP EEVGTEVAIF TRVGVTRIMR YAFKLAQARP
     RKLLTVVTKS NAQRHGMVMW DEIAAEVATE FPDVTWDKML VDAMTVRMTL KPETLDTIVA
     TNLHADILSD LAGALAGSLG VAPTANIDPE RRFPSMFEPI HGSAFDITGK GIANPIATFW
     TAAQMLEHLG ERDAAARLMS AVERVTEAGI LTPDVGGTAN TSQVTEAVCN AIAGSNII
//