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 27-MAR-2024, entry version 96.
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 KEGG; mst:Msp_0672; -.
DR eggNOG; arCOG00246; Archaea.
DR HOGENOM; CLU_045401_2_1_2; -.
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 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; 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..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
//
