MDH_TOBAC
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 03-AUG-2022, entry version 89.
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}.
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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 GeneID; 107772922; -.
DR KEGG; nta:107772922; -.
DR OMA; TKGMERG; -.
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; -; 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 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
