ID   MDH_THETK               Reviewed;         308 AA.
AC   Q704B2; G4RKG3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:O08349};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:O08349};
GN   Name=mdh; OrderedLocusNames=TTX_1427;
OS   Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS   / Kra 1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=768679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX   PubMed=15028704; DOI=10.1128/jb.186.7.2179-2194.2004;
RA   Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA   Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.;
RT   "Reconstruction of the central carbohydrate metabolism of Thermoproteus
RT   tenax using genomic and biochemical data.";
RL   J. Bacteriol. 186:2179-2194(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX   PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA   Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA   Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA   Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA   Hensel R.;
RT   "The complete genome sequence of Thermoproteus tenax: a physiologically
RT   versatile member of the Crenarchaeota.";
RL   PLoS ONE 6:E24222-E24222(2011).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:O08349}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000250|UniProtKB:O08349};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR   EMBL; AJ621301; CAF18482.1; -; Genomic_DNA.
DR   EMBL; FN869859; CCC82058.1; -; Genomic_DNA.
DR   RefSeq; WP_014127312.1; NC_016070.1.
DR   AlphaFoldDB; Q704B2; -.
DR   SMR; Q704B2; -.
DR   STRING; 768679.TTX_1427; -.
DR   EnsemblBacteria; CCC82058; CCC82058; TTX_1427.
DR   GeneID; 11262306; -.
DR   KEGG; ttn:TTX_1427; -.
DR   PATRIC; fig|768679.9.peg.1448; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_2_1_2; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 69007at2157; -.
DR   Proteomes; UP000002654; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..308
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113496"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         6..11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         31
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         93
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         116..118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
SQ   SEQUENCE   308 AA;  32861 MW;  6DB990BB5CFF19F2 CRC64;
     MITVVGSGRV GATTAAMLGV LGVDNKIVLI DIIKGLPQGE ALDLNHMSSI LGLDVYYTGS
     NDYADMKGSD LVIVTAGLAR KPGMTREQLL EQNAQIVANI GKEIAKYAPD SVVILTTNPL
     DAMTYVMWRA TGFSRERVVG FSGVLDGGRL AFYAGQKLGI SPASIIPIVL GQHGESMFPV
     PSKSFVFGVP LDKLLKPEEI KEAVEETVKA GARITELRGF SSNWAPGAGV AIMAKAVKRD
     ERRALIASVV LDGEYGVRGI PVEVPVVLGR GGAIKVLEVE LSPEEKQRFQ QSVEAISKLL
     NSLPAQYK