ID   TTUC1_AGRVI             Reviewed;         364 AA.
AC   Q44471;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 55.
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 pTrAB4, and 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=AB4; PLASMID=pTrAB4;
RX   MEDLINE=96062236; PubMed=7592429;
RA   Crouzet P., Otten L.;
RT   "Sequence and mutational analysis of a tartrate utilization operon
RT   from Agrobacterium vitis.";
RL   J. Bacteriol. 177:6518-6526(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AB3; PLASMID=pTiAB3;
RA   Salomone J.-Y., Szegedi E., Cobanov P., Otten L.;
RL   Submitted (AUG-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; U25634; AAA68698.1; -; Genomic_DNA.
DR   EMBL; AF010262; AAB65747.1; -; 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    364       Probable tartrate
FT                                dehydrogenase/decarboxylase ttuC.
FT                                /FTId=PRO_0000083813.
SQ   SEQUENCE   364 AA;  39431 MW;  1F0212418434BE8B 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 TRQVTEAVCN AIAGSNILKM
     AAAE
//