ID   MDH_METKA               Reviewed;         317 AA.
AC   Q8TWG5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:Q9YEA1};
DE            EC=1.1.1.299 {ECO:0000250|UniProtKB:Q9YEA1};
GN   Name=mdh; OrderedLocusNames=MK1069;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02282.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TWG5; -.
DR   SMR; Q8TWG5; -.
DR   STRING; 190192.MK1069; -.
DR   PRIDE; Q8TWG5; -.
DR   EnsemblBacteria; AAM02282; AAM02282; MK1069.
DR   KEGG; mka:MK1069; -.
DR   PATRIC; fig|190192.8.peg.1123; -.
DR   HOGENOM; CLU_045401_1_1_2; -.
DR   OMA; ASCAEYI; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
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; IPR018177; L-lactate_DH_AS.
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_0000113486"
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;  34609 MW;  D2AC04B7C0B6C26E CRC64;
     MSKVAVIGAT GRVGSTAAAR LALLDCVNEV TLIARPKSVD KLRGLRRDIL DSLAAAQKDA
     EITIGCERDD YVDADVIVMT AGIPRKPGQT RLDLTKDNAA IIKKYLEGVA EENPEAIVLV
     VTNPVDVLTY VALKVSGLPK NRVIGLGTHL DSMRFKVLIA KHFNVHMSEV HTRIIGEHGD
     TMVPVISSTS VGGIPVTRMP GWEDFDVEEA VREVKEAGQR IIETWGGSQF GPAQAITNLV
     RTILQDERRV LTVSAYLDGE IDGIRDVCIG VPARLGREGV LEIVPIELEE DEMRAFRRSV
     KVVKEATREA MEAISER