ID MDH_TOBAC Reviewed; 332 AA. AC Q9FSF0; DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 08-NOV-2023, entry version 93. DE RecName: Full=Malate dehydrogenase; DE Short=NtRed-2; DE EC=1.1.1.37; GN Name=MD1; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Shen W.H.; RT "Nicotiana tabacum cDNA encoding cytosolic malate dehydrogenase."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 127-138, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17945329; DOI=10.1016/j.bioorg.2007.08.005; RA Matsushima A., Sato Y., Otsuka M., Watanabe T., Yamamoto H., Hirata T.; RT "An enone reductase from Nicotiana tabacum: cDNA cloning, expression in RT Escherichia coli, and reduction of enones with the recombinant proteins."; RL Bioorg. Chem. 36:23-28(2008). CC -!- FUNCTION: Catalyzes the reduction of the carbonyl group of oxalacetic CC acid. No activity with pulegone. {ECO:0000269|PubMed:17945329}. 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 ECO:0000269|PubMed:17945329}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ299256; CAC12826.1; -; mRNA. DR RefSeq; NP_001312078.1; NM_001325149.1. DR AlphaFoldDB; Q9FSF0; -. DR SMR; Q9FSF0; -. DR STRING; 4097.Q9FSF0; -. DR PaxDb; 4097-Q9FSF0; -. DR GeneID; 107772922; -. DR KEGG; nta:107772922; -. DR OMA; TKGMERG; -. DR OrthoDB; 501358at2759; -. DR PhylomeDB; Q9FSF0; -. DR Proteomes; UP000084051; Unplaced. DR GO; GO:0005737; C:cytoplasm; 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 Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; KW Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..332 FT /note="Malate dehydrogenase" FT /id="PRO_0000423025" 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; 35408 MW; 726816BDB9049A9C CRC64; MAKDPVRVLV TGAAGQIGYA LVPMIARGVM LGADQPVILH MLDIPPAAEA LNGVKMELVD AAFPLLKGVV ATTDAVEACT GVNVAVMVGG FPRKEGMERK DVMSKNVSIY KSQASALEKH AAPNCKVLVV ANPANTNALI LKEYAPSIPE KNISCLTRLD HNRALGQISE RLNVQVSDVK NVIIWGNHSS SQYPDVNHAT VATPAGEKPV RELVADDAWL NGEFISTVQQ RGAAIIKARK LSSALSAASS ACDHIRDWVL GTPEGTWVSM GVYSDGSYNV PAGLIYSFPV ACKNGEWSIV QGLPIDEFSR KKLDATAEEL SEEKALAYSC LT //