ID   MDHC_BETVU              Reviewed;         332 AA.
AC   Q9SML8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
GN   Name=NR1;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RA   Juergensen K., Buck F., Lange S., Kleine M., Grundler F.M.W.;
RT   "A Beta vulgaris cDNA coding for a putative cytoplasmatic malate
RT   dehydrogenase.";
RL   (er) Plant Gene Register PGR00-023(2000).
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; AJ251083; CAB61618.1; -; mRNA.
DR   RefSeq; NP_001290006.1; NM_001303077.1.
DR   AlphaFoldDB; Q9SML8; -.
DR   SMR; Q9SML8; -.
DR   PRIDE; Q9SML8; -.
DR   GeneID; 104887939; -.
DR   KEGG; bvg:104887939; -.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..332
FT                   /note="Malate dehydrogenase, cytoplasmic"
FT                   /id="PRO_0000113414"
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;  35434 MW;  2B9E6495EF0CD12A CRC64;
     MAVEPLRVLV TGAAGQIGYA LVPMIARGVM LGANQPVILH MLDIPPAAEA LNGVKMELVD
     AAFPLLKGVV ATTDVAEACK GVNVAVMVGG FPRKEGMERK DVMPKNVSIY KSQASALEQY
     AAPNCKVLVV ANPANTNALI LKEFAPSIPE KNITCLTRLD HNRALGQISE RLNAQVSDVK
     NVIIWGNHSS SQYPDVNPCT VKTGSGEKAV RELVADDAWL NGEFITTVQQ RGAAIIKARK
     LSSALSAASS ACDHIRDWVL GTPEGTWVSM GVYSDGSYNV PAGIIYSFPV TCKDGEWKIV
     QGLPIDEVSR QKMDATGAEL VEEKALAYSC LT