ID   MDH_THEAC               Reviewed;         325 AA.
AC   Q9HJL5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:O08349};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:O08349};
GN   Name=mdh; OrderedLocusNames=Ta0952;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Martinez D., Trejo F., Gelpi J.L., Busquets M., Cortes A.;
RT   "Cloning and sequencing of the gene for the L-malate dehydrogenase from the
RT   thermoacidophilic archaebacterium Thermoplasma acidophilum.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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; AF199510; AAG28562.1; -; Genomic_DNA.
DR   EMBL; AL445066; CAC12081.1; -; Genomic_DNA.
DR   RefSeq; WP_010901363.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJL5; -.
DR   SMR; Q9HJL5; -.
DR   STRING; 273075.Ta0952; -.
DR   EnsemblBacteria; CAC12081; CAC12081; CAC12081.
DR   GeneID; 1456484; -.
DR   KEGG; tac:Ta0952; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_2_1_2; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 69007at2157; -.
DR   Proteomes; UP000001024; 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   HAMAP; MF_00487; Malate_dehydrog_3; 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.
DR   TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..325
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113495"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         124..126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
SQ   SEQUENCE   325 AA;  35524 MW;  D6126D95B7EB1B31 CRC64;
     MARKKISVIG AGNVGATVAQ FLAAKQLGDV YLFDVVDGIP EGKALDIQEG APHWRYDLDV
     VGFSTSDETK YKNMEGSDVI VVTAGLARKP GMSRDDLFDK NVEIISDVSR NIKKYSPDSI
     IVVVSNPADI MAYALQKFTG IDPSKIMGLG GSLDSSRFRT FLAKELNVSV EDVNAFVIGG
     HGDDMVPFIR YSSVAGIPIE NLLSKEKIDE IVKRTRFGGG EIVNYLKTGS AFYAPGISIT
     AMVESVIMDK KRVIPCAAYI TGKHADHYGI RDKFIGVPIK IGEKGVEQIY DIDFKPDELE
     LWKKSVASVE ASSKKVDEWI AKHAH