TTUC_PSEPU
ID TTUC_PSEPU Reviewed; 365 AA.
AC Q51945;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Tartrate dehydrogenase/decarboxylase;
DE Short=TDH;
DE EC=1.1.1.93 {ECO:0000269|PubMed:2184888};
DE EC=4.1.1.73 {ECO:0000269|PubMed:2184888};
DE AltName: Full=D-malate dehydrogenase [decarboxylating];
DE EC=1.1.1.83 {ECO:0000269|PubMed:2184888};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-22 AND
RP 276-294.
RC STRAIN=ATCC 17642 / NCIMB 10804 / 276;
RX PubMed=8053675; DOI=10.1006/abbi.1994.1352;
RA Tipton P.A., Beecher B.S.;
RT "Tartrate dehydrogenase, a new member of the family of metal-dependent
RT decarboxylating R-hydroxyacid dehydrogenases.";
RL Arch. Biochem. Biophys. 313:15-21(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2184888; DOI=10.1021/bi00459a013;
RA Tipton P.A., Peisach J.;
RT "Characterization of the multiple catalytic activities of tartrate
RT dehydrogenase.";
RL Biochemistry 29:1749-1756(1990).
RN [3]
RP ENZYME KINETICS.
RX PubMed=8457548; DOI=10.1021/bi00062a013;
RA Tipton P.A.;
RT "Intermediate partitioning in the tartrate dehydrogenase-catalyzed
RT oxidative decarboxylation of D-malate.";
RL Biochemistry 32:2822-2827(1993).
RN [4]
RP ENZYME KINETICS.
RX PubMed=12356321; DOI=10.1021/bi026278g;
RA Karsten W.E., Tipton P.A., Cook P.F.;
RT "Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of
RT D-malate with both NAD and thio-NAD.";
RL Biochemistry 41:12193-12199(2002).
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:0000269|PubMed:2184888}.
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:0000269|PubMed:2184888};
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:0000269|PubMed:2184888};
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:0000269|PubMed:2184888};
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:0000269|PubMed:2184888};
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:0000269|PubMed:2184888};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:2184888};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:2184888};
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:0000269|PubMed:2184888};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.058 mM for D-malate {ECO:0000269|PubMed:2184888};
CC KM=1.08 mM for (+)-tartrate {ECO:0000269|PubMed:2184888};
CC KM=0.12 mM for NAD(+) (for (+)-tartrate oxidation)
CC {ECO:0000269|PubMed:2184888};
CC KM=0.05 mM for NAD(+) (for D-malate oxidation)
CC {ECO:0000269|PubMed:2184888};
CC Temperature dependence:
CC Thermostable. Fully active after heating 10 min at 65 degrees Celsius
CC and retains half its catalytic activity after 10 min at 72 degrees
CC Celsius. Inactive after heating 10 min at 78 degrees Celsius.
CC {ECO:0000269|PubMed:2184888};
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 -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; U05986; AAA60327.1; -; Genomic_DNA.
DR PIR; S48640; S48640.
DR PDB; 3FLK; X-ray; 2.00 A; A/B/C/D=1-365.
DR PDB; 3FMX; X-ray; 2.95 A; X=1-365.
DR PDBsum; 3FLK; -.
DR PDBsum; 3FMX; -.
DR AlphaFoldDB; Q51945; -.
DR SMR; Q51945; -.
DR UniPathway; UPA00839; UER00800.
DR UniPathway; UPA00839; UER00801.
DR UniPathway; UPA00839; UER00803.
DR EvolutionaryTrace; Q51945; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Lyase; Magnesium;
KW Manganese; Metal-binding; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8053675"
FT CHAIN 2..365
FT /note="Tartrate dehydrogenase/decarboxylase"
FT /id="PRO_0000083819"
FT BINDING 225
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"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3FLK"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3FMX"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3FLK"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3FMX"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3FMX"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3FLK"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3FLK"
FT TURN 289..293
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 318..337
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3FLK"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:3FLK"
SQ SEQUENCE 365 AA; 40630 MW; B26682F137DB49D9 CRC64;
MPAHSFRIAA IPGDGIGLEV LPEGIRVLEA AALKHGLALE FDTFEWASCD YYLQHGKMMP
DDWAEQLKQY DAIYFGAVDW PDKVPDHISL WGSLLKFRRE FDQYVNIRPV RLFPGVPCAL
ANRKVGDIDF VVVRENTEGE YSSLGGIMFE NTENEIVIQE SIFTRRGVDR ILKYAFDLAE
KRERKHVTSA TKSNGMAISM PYWDKRTEAM AAHYPHVSWD KQHIDILCAR FVLQPERFDV
VVVASNLFGD ILSDLGPACA GTIGIAPSAN LNPERNFPSL FEPVHGSAPD IFGKNIANPI
AMIWSGALML EFLGQGDERY QRAHDDMLNA IERVIADGSV TPDMGGTLST QQVGAAISDT
LARLD
