ID   MDHC_MAIZE              Reviewed;         332 AA.
AC   Q08062; B2ZAF9; C4IZW9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic {ECO:0000303|Ref.1};
DE            EC=1.1.1.37 {ECO:0000269|PubMed:23313174};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Yedan 4; TISSUE=Leaf;
RA   Hu J., Zhao X., Yuan Z., Qian X., Yang J.;
RT   "Cloning and characterization of cytoplasmic malate dehydrogenase over-
RT   expressed in hybrid maize.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Wang J., Cheng B., Xiang Y., Zhu S., Jiang H., Chen D., Zhang Y.;
RT   "Cloning of Malate Dehydrogenase from Zea mays and Construction of its RNAi
RT   Expression Vector.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. B73;
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-73.
RC   STRAIN=cv. B73; TISSUE=Leaf, and Sheath;
RX   PubMed=8278499; DOI=10.1104/pp.101.1.329;
RA   Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., Thai H.,
RA   Baysdorfer C.;
RT   "Partial sequence analysis of 130 randomly selected maize cDNA clones.";
RL   Plant Physiol. 101:329-332(1993).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY
RP   MASS SPECTROMETRY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   TISSUE SPECIFICITY, AND SUBUNIT.
RX   PubMed=23313174; DOI=10.1016/j.jprot.2012.12.015;
RA   Menckhoff L., Mielke-Ehret N., Buck F., Vuletic M., Luethje S.;
RT   "Plasma membrane-associated malate dehydrogenase of maize (Zea mays L.)
RT   roots: native versus recombinant protein.";
RL   J. Proteomics 80:66-77(2013).
CC   -!- FUNCTION: Malate dehydrogenase; catalyzes a reversible NAD-dependent
CC       dehydrogenase reaction involved in central metabolism and redox
CC       homeostasis. {ECO:0000305|PubMed:23313174}.
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:0000269|PubMed:23313174};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25 uM for NADH for the native enzyme
CC         {ECO:0000269|PubMed:23313174};
CC         KM=29 uM for NADH for the recombinant enzyme
CC         {ECO:0000269|PubMed:23313174};
CC         KM=126 uM for oxaloacetate for the native enzyme
CC         {ECO:0000269|PubMed:23313174};
CC         KM=289 uM for oxaloacetate for the recombinant enzyme
CC         {ECO:0000269|PubMed:23313174};
CC         KM=1810 uM for malate for the native enzyme
CC         {ECO:0000269|PubMed:23313174};
CC         KM=266 uM for malate for the recombinant enzyme
CC         {ECO:0000269|PubMed:23313174};
CC       pH dependence:
CC         Optimum pH is 7.41 for the native enzyme.
CC         {ECO:0000269|PubMed:23313174};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23313174}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23313174};
CC       Peripheral membrane protein {ECO:0000269|PubMed:23313174}.
CC   -!- TISSUE SPECIFICITY: Expressed constitutively in roots.
CC       {ECO:0000269|PubMed:23313174}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF007581; AAB64290.1; -; mRNA.
DR   EMBL; EU625276; ACD02021.1; -; mRNA.
DR   EMBL; BT084116; ACR34469.1; -; mRNA.
DR   EMBL; M95069; AAA18556.2; -; mRNA.
DR   PIR; T02935; T02935.
DR   PIR; T03650; T03650.
DR   RefSeq; NP_001105603.1; NM_001112133.2.
DR   AlphaFoldDB; Q08062; -.
DR   SMR; Q08062; -.
DR   STRING; 4577.GRMZM2G415359_P02; -.
DR   PaxDb; Q08062; -.
DR   PRIDE; Q08062; -.
DR   ProMEX; Q08062; -.
DR   EnsemblPlants; Zm00001eb045790_T004; Zm00001eb045790_P004; Zm00001eb045790.
DR   GeneID; 542598; -.
DR   Gramene; Zm00001eb045790_T004; Zm00001eb045790_P004; Zm00001eb045790.
DR   KEGG; zma:542598; -.
DR   eggNOG; KOG1496; Eukaryota.
DR   HOGENOM; CLU_040727_2_0_1; -.
DR   OMA; TKGMERG; -.
DR   OrthoDB; 1118998at2759; -.
DR   Proteomes; UP000007305; Chromosome 1.
DR   ExpressionAtlas; Q08062; baseline and differential.
DR   Genevisible; Q08062; ZM.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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   Cell membrane; Direct protein sequencing; Membrane; NAD; Oxidoreductase;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..332
FT                   /note="Malate dehydrogenase, cytoplasmic"
FT                   /id="PRO_0000113415"
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"
FT   CONFLICT        202
FT                   /note="K -> E (in Ref. 2; ACD02021)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="H -> Y (in Ref. 2; ACD02021)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   332 AA;  35590 MW;  05D82B33FF0CE26F CRC64;
     MAKEPMRVLV TGAAGQIGYA LVPMIARGVM LGADQPVILH MLDIPPAAEA LNGVKMELVD
     AAFPLLKGVV ATTDVVEACT GVNVAVMVGG FPRKEGMERK DVMSKNVSIY KSQASALEAH
     AAPNCKVLVV ANPANTNALI LKEFAPSIPE KNVTCLTRLD HNRALGQISE RLNVQVSDVK
     NVIIWGNHSS SQYPDVNHAT VKTSTGEKPV RELVSDDEWL NGEFITTVQQ RGAAIIKARK
     FSSALSAASS ACDHIRDWVL GTPEGTFVSM GVYSDGSYGV PSGLIYSFPV TCSGGEWKIV
     QGLPIDEFSR KKMDATAQEL TEEKTLAYSC LE