TTUC1_AGRVI
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 03-AUG-2022, entry version 99.
DE RecName: Full=Probable tartrate dehydrogenase/decarboxylase TtuC;
DE Short=TDH;
DE EC=1.1.1.93 {ECO:0000250|UniProtKB:Q51945};
DE EC=4.1.1.73 {ECO:0000250|UniProtKB:Q51945};
DE AltName: Full=D-malate dehydrogenase [decarboxylating];
DE EC=1.1.1.83 {ECO:0000250|UniProtKB:Q51945};
GN Name=ttuC;
OS Agrobacterium vitis (Rhizobium vitis).
OG Plasmid pTrAB4, and Plasmid pTiAB3.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX NCBI_TaxID=373;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AB4; PLASMID=pTrAB4;
RX PubMed=7592429; DOI=10.1128/jb.177.22.6518-6526.1995;
RA Crouzet P., Otten L.;
RT "Sequence and mutational analysis of a tartrate utilization operon from
RT 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 -!- FUNCTION: Has multiple catalytic activities. Apart from catalyzing the
CC oxidation of (+)-tartrate to oxaloglycolate, also converts meso-
CC tartrate to D-glycerate and catalyzes the oxidative decarboxylation of
CC D-malate to pyruvate. {ECO:0000250|UniProtKB:Q51945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + tartrate = 2-hydroxy-3-oxosuccinate + H(+) + NADH;
CC Xref=Rhea:RHEA:18853, ChEBI:CHEBI:15378, ChEBI:CHEBI:30929,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58265; EC=1.1.1.93;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) +
CC NADH; Xref=Rhea:RHEA:16457, ChEBI:CHEBI:15378, ChEBI:CHEBI:30928,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58265; EC=1.1.1.93;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) +
CC NADH; Xref=Rhea:RHEA:15209, ChEBI:CHEBI:15378, ChEBI:CHEBI:30924,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58265; EC=1.1.1.93;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-tartrate + H(+) = (R)-glycerate + CO2;
CC Xref=Rhea:RHEA:13317, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16659, ChEBI:CHEBI:30924; EC=4.1.1.73;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:18365, ChEBI:CHEBI:15361, ChEBI:CHEBI:15588,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.83;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000250|UniProtKB:P37412};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q51945};
CC -!- PATHWAY: Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy-
CC 3-oxosuccinate from L-tartrate: step 1/1.
CC -!- PATHWAY: Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy-
CC 3-oxosuccinate from meso-tartrate: step 1/1.
CC -!- PATHWAY: Carbohydrate acid metabolism; tartrate degradation; D-
CC glycerate from L-tartrate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By tartrate.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; U25634; AAA68698.1; -; Genomic_DNA.
DR EMBL; AF010262; AAB65747.1; -; Genomic_DNA.
DR RefSeq; WP_032489007.1; NZ_WPID01000009.1.
DR AlphaFoldDB; Q44471; -.
DR SMR; Q44471; -.
DR GeneID; 60683900; -.
DR UniPathway; UPA00839; UER00800.
DR UniPathway; UPA00839; UER00801.
DR UniPathway; UPA00839; UER00803.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050319; F:tartrate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009027; F:tartrate dehydrogenase activity; IEA:UniProtKB-EC.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011829; TTC_DH.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR02089; TTC; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lyase; Manganese; Metal-binding; NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..364
FT /note="Probable tartrate dehydrogenase/decarboxylase TtuC"
FT /id="PRO_0000083813"
FT BINDING 222
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
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
