TTUC2_AGRVI
ID TTUC2_AGRVI Reviewed; 364 AA.
AC P70787;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 pTrAB3.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX NCBI_TaxID=373;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AB3;
RX PubMed=8672817; DOI=10.1094/mpmi-9-0401;
RA Salomone J.-Y., Crouzet P., de Ruffray P., Otten L.;
RT "Characterization and distribution of tartrate utilization genes in the
RT grapevine pathogen Agrobacterium vitis.";
RL Mol. Plant Microbe Interact. 9:401-408(1996).
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; U32375; AAB61623.1; -; Genomic_DNA.
DR RefSeq; WP_032488976.1; NZ_WPHQ01000033.1.
DR AlphaFoldDB; P70787; -.
DR SMR; P70787; -.
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_0000083814"
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; 39271 MW; D05BED66A360BA3E CRC64;
MREYKIAAIP ADGIGPEVIA AGLQVLEALE KRSGDFSIHT ETFDWGSDYY KKNGVMMPAD
GLEQLKKFDA IFFGAVGAPD VPDHITLWGL RLPICQGFDQ YANVRPTKVL PGITPPLRNC
GPGDLDWVIV RENSEGEYSG HGGRAHKGLP EEVGTEVAIF TRVGVTRIMR YAFKLAQARP
RKLLTVVTKS NAQRHGMVMW DEIAAEVSKE FPDVTWDKML VDAMTVRMTL KPQSLDTIVA
TNLHADILSD LAGALAGSLG VAPTANIDPE RRFPSMFEPI HGSAFDITGK GIANPVATFW
TAAQMLEHLG EKDAATRLMS AVERVTEAGI LTPDVGGTAD TQQVTDAVCE AIAGSNILNM
AAVG
