MDH_METMP
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 03-AUG-2022, entry version 107.
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 OMA; ASCAEYI; -.
DR OrthoDB; 69007at2157; -.
DR BioCyc; MMAR267377:MMP_RS03390-MON; -.
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 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..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