ID   MDHM_CHLRE              Reviewed;         373 AA.
AC   Q42686;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Malate dehydrogenase, mitochondrial;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Krishnasamy S., Chang T.E., Makaroff C.A., Wang W.Y.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
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; U40212; AAA84971.1; -; Genomic_DNA.
DR   PIR; T08077; T08077.
DR   RefSeq; XP_001703167.1; XM_001703115.1.
DR   AlphaFoldDB; Q42686; -.
DR   SMR; Q42686; -.
DR   STRING; 3055.EDO96543; -.
DR   PRIDE; Q42686; -.
DR   ProMEX; Q42686; -.
DR   EnsemblPlants; PNW74437; PNW74437; CHLRE_12g483950v5.
DR   GeneID; 5728707; -.
DR   Gramene; PNW74437; PNW74437; CHLRE_12g483950v5.
DR   KEGG; cre:CHLRE_12g483950v5; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   HOGENOM; CLU_047181_0_2_1; -.
DR   OrthoDB; 976445at2759; -.
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:0006108; P:malate 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; -; 1.
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; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..373
FT                   /note="Malate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000018624"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  38510 MW;  0FCFEBFC58FD19BD CRC64;
     MSLQSSIRAD SNCTLPNNPV CVLLPVDFIV AAMASSTSSA MAKWAAQAAR GFAAAAPSSG
     KGRKVAVLGA AGGIGQPLSM LMKMNSQVSS LSLYDIAGTP GVAADVSHIN TKAQVKGFDK
     DGLAEALRGC DLVIIPAGVP RKPGMTRDDL FKINAGIVRD LVTAVGQHCP GAVLNIISNP
     VNSTVPIAAE QLKKMGVYDK RKVMGVTTLD VVRAKTFYAE KNGLDVASVD VPVVGGHAGV
     TILPLFSQAT PKATMSAEVL DALTKRTQDG GTEVVQAKAG KGSATLSMAY AAALFADSCL
     RGLNGAPVVE CTYVESTVTD APYFASKVKL STEGVDKIHD LGPLSDYEKA GLKAMMPELL
     ASIEKGVQFV KGA