ID   MDHM_BRANA              Reviewed;         341 AA.
AC   Q43744;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   13-SEP-2023, entry version 117.
DE   RecName: Full=Malate dehydrogenase, mitochondrial;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   Name=MDH;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Andor; TISSUE=Leaf;
RA   Witt U., Gruneberg-Seiler M., Abel W.O.;
RT   "A full-length cDNA coding for mitochondrial malate dehydrogenase from
RT   Brassica napus L.";
RL   (er) Plant Gene Register PGR95-068(1995).
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; EC=1.1.1.37;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; X89451; CAA61621.1; -; mRNA.
DR   PIR; S57958; S57958.
DR   RefSeq; NP_001302862.1; NM_001315933.1.
DR   AlphaFoldDB; Q43744; -.
DR   SMR; Q43744; -.
DR   GeneID; 106360426; -.
DR   OrthoDB; 5059897at2759; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 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; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF58; MALATE DEHYDROGENASE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..341
FT                   /note="Malate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000018623"
FT   BINDING         36..42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         145..147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  35711 MW;  F27AC7D2680601C6 CRC64;
     MFRSALVRSS ASAKQSLLRR SFSSGSVPER KVAILGAAGG IGQPLALLMK LNPLVSSLSL
     YDIANTPGVA ADVGHINTRS QVVGYMGDDN LAKALEGADL VIIPAGVPRK PGMTRDDLFN
     INAGIVKNLW SAIAKYCPHA LVNMISNPVN STVPIAAEIF KKAGMYDEKK LFGVTTLDVV
     RVKTSYAGKA NVPVAEVNVP AIVGHAGVTI LPLFSQATPQ AILSGDALTV TTKRTQDGGT
     EVEEAKAGKG SATLSMAYAG ALFADACLKG LNGVPDVVEC SYVQSTITEL PFFASKVRLG
     KNGVEEVLDL GPLSDFEKEG LEALRPGIKS TIEKGVKFAN Q
//