ID   MDHC_MEDSA              Reviewed;         332 AA.
AC   O48905;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
GN   Name=CMDH;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Saranac; TISSUE=Root nodule;
RX   PubMed=9721676; DOI=10.1046/j.1365-313x.1998.00192.x;
RA   Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P.;
RT   "Alfalfa malate dehydrogenase (MDH): molecular cloning and characterization
RT   of five different forms reveals a unique nodule-enhanced MDH.";
RL   Plant J. 15:173-184(1998).
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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF020272; AAB99756.1; -; mRNA.
DR   PIR; T09291; T09291.
DR   AlphaFoldDB; O48905; -.
DR   SMR; O48905; -.
DR   PRIDE; O48905; -.
DR   BioCyc; MetaCyc:MON-17412; -.
DR   GO; GO:0005737; C:cytoplasm; 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; cd01336; MDH_cytoplasmic_cytosolic; 1.
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; IPR001252; Malate_DH_AS.
DR   InterPro; IPR011274; Malate_DH_NAD-dep_euk.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   TIGRFAMs; TIGR01758; MDH_euk_cyt; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..332
FT                   /note="Malate dehydrogenase, cytoplasmic"
FT                   /id="PRO_0000113416"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P11708"
FT   BINDING         16..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         43
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         99
FT                   /ligand="oxaloacetate"
FT                   /ligand_id="ChEBI:CHEBI:16452"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         132
FT                   /ligand="oxaloacetate"
FT                   /ligand_id="ChEBI:CHEBI:16452"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         163
FT                   /ligand="oxaloacetate"
FT                   /ligand_id="ChEBI:CHEBI:16452"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         188
FT                   /ligand="oxaloacetate"
FT                   /ligand_id="ChEBI:CHEBI:16452"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
FT   BINDING         243
FT                   /ligand="oxaloacetate"
FT                   /ligand_id="ChEBI:CHEBI:16452"
FT                   /evidence="ECO:0000250|UniProtKB:P93819"
SQ   SEQUENCE   332 AA;  35547 MW;  D9F38F868DE3D628 CRC64;
     MAKDPVRVLV TGAAGQIGYA LVPMIARGVM LGPDQPVILH MLDIAPAAES LNGVKMELVD
     AAFPLLKGVV ATTDVVEACT GVNIAVMVGG FPRKEGMERK DVMSKNVSIY KSQASALEKH
     AAANCKVLVV ANPANTNALI LKEFAPSIPE RNISCLTRLD HNRALGQISE RLNVQVSDVK
     NVIIWGNHSS TQYPDVNHAT VNTPAGEKPV RQLVSDDAWL NGEFISTVQQ RGAAIIKARK
     LSSALSAASA ACDHIRDWVL GTPQGTFVSM GVYSDGSYNV PSGLIYSFPV TCANGEWKIV
     QGLSIDEFSR KKLDLTAEEL TEEKNLAHSC LS