ID   MDH_METST               Reviewed;         317 AA.
AC   Q2NGI3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:Q9YEA1};
DE            EC=1.1.1.299 {ECO:0000250|UniProtKB:Q9YEA1};
GN   Name=mdh; OrderedLocusNames=Msp_0672;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:Q9YEA1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate;
CC         Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.299; Evidence={ECO:0000250|UniProtKB:Q9YEA1};
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;
CC         EC=1.1.1.299; Evidence={ECO:0000250|UniProtKB:Q9YEA1};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR   EMBL; CP000102; ABC57070.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2NGI3; -.
DR   SMR; Q2NGI3; -.
DR   STRING; 339860.Msp_0672; -.
DR   EnsemblBacteria; ABC57070; ABC57070; Msp_0672.
DR   KEGG; mst:Msp_0672; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_2_1_2; -.
DR   OMA; ASCAEYI; -.
DR   Proteomes; UP000001931; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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; 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; NADP; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..317
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000241971"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         8..14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q60176"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         98
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q60176"
FT   BINDING         121..123
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q60176"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
SQ   SEQUENCE   317 AA;  34857 MW;  62C3D986993DE8D0 CRC64;
     MVKITIMGAS GTIGKTVAFN LAEKDVIDEI IMFSRPASHE RVKGEILDMY DALAAEDIDC
     ELKASSDYAD LAGSSIVLIT SGVPRKEGMS RLDLAVPNSK IVQEYSKQIA IHAPDSVILI
     VTNPVDVMTS IALKTSGFDK KRVIGLGNHL DSLRLKTLLS KHFHINSREI HTRVIGEHGD
     HMVPLLSSTT IGGILLKSFV EYMDLDVPKL VETLKNSGNN IISKKGATEY GPSYAISNLI
     LTIANDTRKI LTVSTYLEGE VEGVYDVSLG VPVILCKHGI KRIVPLKMND EERTEFFDAA
     RTVKKTTYEL EKMLNKE