ID   MDHM_SCHMA              Reviewed;         142 AA.
AC   P37227;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 119.
DE   RecName: Full=Malate dehydrogenase, mitochondrial;
DE            EC=1.1.1.37;
DE   Flags: Fragment;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Neodermata; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8396206; DOI=10.1016/0166-6851(93)90032-s;
RA   Skelly P.J., Stein L.D., Shoemaker C.B.;
RT   "Expression of Schistosoma mansoni genes involved in anaerobic and
RT   oxidative glucose metabolism during the cercaria to adult transformation.";
RL   Mol. Biochem. Parasitol. 60:93-104(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = oxaloacetate + NADH + H(+);
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- DEVELOPMENTAL STAGE: Expressed in relatively high level in adults as
CC       compared to larval worms.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; L10108; AAA29901.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37227; -.
DR   SMR; P37227; -.
DR   STRING; 6183.P37227; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   HOGENOM; CLU_047181_0_1_1; -.
DR   InParanoid; P37227; -.
DR   SABIO-RK; P37227; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:TreeGrafter.
DR   FunFam; 3.40.50.720:FF:000013; Malate dehydrogenase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           <1..>142
FT                   /note="Malate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000113340"
FT   BINDING         1..6
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         86
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         109..111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   NON_TER         1
FT   NON_TER         142
SQ   SEQUENCE   142 AA;  14956 MW;  C06BC6726566AE72 CRC64;
     ASGGIGEPLS LLLKQSPLIS QLALYDIAHV KGVAADLSHI ETQAHVTAHL GPGELAECLT
     GANVVIIPAG LPRKPGMTRD DLFNTNASIV AELIDSCAKN CPKAMICIIT NPVNSTVPIA
     AEILKRHNVY DPKRLFGVTT LD
//