TTUC_BACSU
ID TTUC_BACSU Reviewed; 354 AA.
AC P42958; O31481;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable tartrate dehydrogenase/decarboxylase;
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=ycsA; OrderedLocusNames=BSU04000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8574415; DOI=10.1099/13500872-141-12-3241;
RA Akagawa E., Kurita K., Sugawara T., Nakamura K., Kasahara Y., Ogasawara N.,
RA Yamane K.;
RT "Determination of a 17,484 bp nucleotide sequence around the 39 degrees
RT region of the Bacillus subtilis chromosome and similarity analysis of the
RT products of putative ORFs.";
RL Microbiology 141:3241-3245(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [5]
RP SEQUENCE REVISION TO 241; 256 AND 263.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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 -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07352.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA09031.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D38161; BAA07352.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D50453; BAA09031.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12208.3; -; Genomic_DNA.
DR PIR; A69765; A69765.
DR RefSeq; NP_388282.3; NC_000964.3.
DR RefSeq; WP_003234436.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P42958; -.
DR SMR; P42958; -.
DR STRING; 224308.BSU04000; -.
DR jPOST; P42958; -.
DR PaxDb; P42958; -.
DR PRIDE; P42958; -.
DR EnsemblBacteria; CAB12208; CAB12208; BSU_04000.
DR GeneID; 938262; -.
DR KEGG; bsu:BSU04000; -.
DR PATRIC; fig|224308.43.peg.416; -.
DR eggNOG; COG0473; Bacteria.
DR InParanoid; P42958; -.
DR OMA; GTSMFEP; -.
DR PhylomeDB; P42958; -.
DR BioCyc; BSUB:BSU04000-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 3: Inferred from homology;
KW Lyase; Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..354
FT /note="Probable tartrate dehydrogenase/decarboxylase"
FT /id="PRO_0000083820"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P37412"
FT CONFLICT 241
FT /note="N -> K (in Ref. 1; BAA07352 and 2; BAA09031)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="G -> E (in Ref. 1; BAA07352 and 2; BAA09031)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="S -> P (in Ref. 1; BAA07352 and 2; BAA09031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38728 MW; 816DC5A21FC23D14 CRC64;
MTMKQFEIAA IPGDGVGKEV VAAAEKVLHT AAEVHGGLSF SFTAFPWSCD YYLEHGKMMP
EDGIHTLTQF EAVFLGAVGN PKLVPDHISL WGLLLKIRRE LELSINMRPA KQMAGITSPL
LHPNDFDFVV IRENSEGEYS EVGGRIHRGD DEIAIQNAVF TRKATERVMR FAFELAKKRR
SHVTSATKSN GIYHAMPFWD EVFQQTAADY SGIETSSQHI DALAAFFVTR PETFDVIVAS
NLFGDILTDI SSSLMGSIGI APSANINPSG KYPSMFEPVH GSAPDIAGQG LANPIGQIWT
AKLMLDHFGE EELGAKILDV MEQVTADGIK TRDIGGQSTT AEVTDEICSR LRKL
