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 27-MAR-2024, entry version 163.
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.Q08062; -.
DR PaxDb; 4577-GRMZM2G415359_P02; -.
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 InParanoid; Q08062; -.
DR OMA; DHMRDWT; -.
DR OrthoDB; 501358at2759; -.
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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR NCBIfam; TIGR01758; MDH_euk_cyt; 1.
DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF3; MALATE DEHYDROGENASE, CYTOPLASMIC; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
