ID   MDH_METMP               Reviewed;         314 AA.
AC   Q6LZI3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:Q9YEA1};
DE            EC=1.1.1.299 {ECO:0000250|UniProtKB:Q9YEA1};
GN   Name=mdh; OrderedLocusNames=MMP0645;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF30201.1; -; Genomic_DNA.
DR   RefSeq; WP_011170589.1; NC_005791.1.
DR   AlphaFoldDB; Q6LZI3; -.
DR   SMR; Q6LZI3; -.
DR   STRING; 267377.MMP0645; -.
DR   EnsemblBacteria; CAF30201; CAF30201; MMP0645.
DR   GeneID; 37875176; -.
DR   KEGG; mmp:MMP0645; -.
DR   PATRIC; fig|267377.15.peg.662; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_2_2_2; -.
DR   OrthoDB; 2596at2157; -.
DR   Proteomes; UP000000590; 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   CDD; cd05294; LDH-like_MDH_nadp; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 1.
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; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD; NADP; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..314
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113488"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         7..13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q60176"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         99
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   314 AA;  34468 MW;  D24887E741943821 CRC64;
     MDVSIIGASG KIGSVLSLLL AKESHIKNIN LIARSSSINK LKGLKMDLYD AMAAAGQDTD
     IDICCDDDLS CTANSDITII TAGMARTGEM SRIDLMKGNA KIVKNYVKNI ANFGDTKIFM
     ISNPVDLMTY KALIESGYEK NQVFGLGTHL DSMRFKVAVA KHFEVHLDDV RTRIVGEHGD
     SMVPVISATA VGGIPIKRLP KYEDFPYEKI LERIKGYGQE IINLKNGSEY GPASAIVNIV
     RCIAHDEKRL LTLSTYIEDE IEGIEGGCCI GVPVKVGKNG IEEVIHIKME DDEIEGFKKS
     FELVKGYCRQ IESI
//