ID   MDH_METTH               Reviewed;         325 AA.
AC   O26290;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:Q9YEA1};
DE            EC=1.1.1.299 {ECO:0000250|UniProtKB:Q9YEA1};
GN   Name=mdh; OrderedLocusNames=MTH_188;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000666; AAB84694.1; -; Genomic_DNA.
DR   PIR; E69118; E69118.
DR   RefSeq; WP_010875827.1; NC_000916.1.
DR   AlphaFoldDB; O26290; -.
DR   SMR; O26290; -.
DR   STRING; 187420.MTH_188; -.
DR   EnsemblBacteria; AAB84694; AAB84694; MTH_188.
DR   GeneID; 1470149; -.
DR   KEGG; mth:MTH_188; -.
DR   PATRIC; fig|187420.15.peg.160; -.
DR   HOGENOM; CLU_045401_2_2_2; -.
DR   OMA; ASCAEYI; -.
DR   BioCyc; MetaCyc:MON-14545; -.
DR   Proteomes; UP000005223; 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..325
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113489"
FT   ACT_SITE        177
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         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q60176"
FT   BINDING         120..122
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q60176"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
SQ   SEQUENCE   325 AA;  35933 MW;  AA9C2E5B8827F9C9 CRC64;
     MKVSIIGSTG RVGRATALCL AEEEAVKTLH LISRKESLEQ NLGEVLDMSD ALAAKGVSVK
     LENSADIENV YGSRIVVITA GVPRTADMDR DDLAFKNGRI VADYARQIAR FAPDSIILVV
     TNPVDVMTYV ALRYSGFHPS RVFGLGNHLD SLRLKNYMAR HFNVHVSEVH TRVIGQHGPY
     MVPLISSTSI GGIPIEHYAR RDYFSGYKKF DLKKTIDKVI HAGSNIISRK GATEYGPAFA
     ISNIVTTILN DERRILTVST LMEGEIDGIR DVCLGVPVKL GKNGIEGVVP VLMDRDEREA
     FREAANHVRD STRRVMEFLD EELPL