ID   MDHC_MESCR              Reviewed;         332 AA.
AC   O24047;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
GN   Name=MDH;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Green leaf;
RX   PubMed=9358050; DOI=10.1016/s0378-1119(97)00361-2;
RA   Ocheretina O., Scheibe R.;
RT   "Cloning and sequence analysis of cDNAs encoding plant cytosolic malate
RT   dehydrogenase.";
RL   Gene 199:145-148(1997).
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.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X96539; CAA65384.1; -; mRNA.
DR   PIR; T12433; T12433.
DR   AlphaFoldDB; O24047; -.
DR   SMR; O24047; -.
DR   PRIDE; O24047; -.
DR   BRENDA; 1.1.1.37; 3238.
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_0000113417"
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;  35498 MW;  E5AF1F3013CEEAE6 CRC64;
     MAVEPLRVLV TGAAGQIGYA LVPMIARGIM LGANQPVILH MLDIPPAAEA LNGVKMELVD
     AAFPLLKGVV ATTDAAEACK GVNVAVMVGG FPRKEGMERK DVMSKNVSIY KAQASALEQH
     AAPNCKVLVV ANPANTNALI LKEFAPSIPE KNISCLTRLD HNRALGQISE RLNVQVSDVK
     NVIIWGNHSS TQYPDVNHAT VKTQGVDKPV RELVADDAWL NGEFITTVQQ RGAAIIKARK
     LSSALSAASS ACDHIHDWVL GTPEGTWVSM GVYSDGSYNV PAGIIYSFPV TCKNGEWTIV
     QGLPIDDDSR KKMDATAAEL VEEKTLAYSC LT