ID   MAON_SOLTU              Reviewed;         601 AA.
AC   P37225;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=NAD-dependent malic enzyme 59 kDa isoform, mitochondrial;
DE            Short=NAD-ME;
DE            EC=1.1.1.39;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=8106447; DOI=10.1016/s0021-9258(17)37612-3;
RA   Winning B.M., Bourguignon J., Leaver C.J.;
RT   "Plant mitochondrial NAD+-dependent malic enzyme. cDNA cloning, deduced
RT   primary structure of the 59- and 62-kDa subunits, import, gene complexity
RT   and expression analysis.";
RL   J. Biol. Chem. 269:4780-4786(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.39;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of two related subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; Z23002; CAA80547.1; -; mRNA.
DR   PIR; A53318; A53318.
DR   AlphaFoldDB; P37225; -.
DR   SMR; P37225; -.
DR   IntAct; P37225; 1.
DR   STRING; 4113.PGSC0003DMT400000066; -.
DR   PRIDE; P37225; -.
DR   eggNOG; KOG1257; Eukaryota.
DR   SABIO-RK; P37225; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P37225; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; Mitochondrion; NAD;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT   CHAIN           19..601
FT                   /note="NAD-dependent malic enzyme 59 kDa isoform,
FT                   mitochondrial"
FT                   /id="PRO_0000018544"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            295
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   601 AA;  66272 MW;  D6C2A128CC9E971C CRC64;
     MWRVARSAAS TFRRTRRLST AISAPCIVHK RGADILHDPW FNKDTGFPMT ERDRLGLRGL
     LPPRVISFEQ QYDRFMESFR SLEKNTEGQP DSVVSLAKWR ILNRLHDRNE TLYYRVLIDN
     IKDFAPIIYT PTVGLVCQNY SGLFRRPRGM YFSAKDKGEM MSMIFNWPST QVDMIVLTDG
     SRILGLGDLG VQGIGIPIGK LDMYVAAAGI NPQRVLPVML DVGTNNQKLL EDPLYLGLRQ
     PRLEGEEYLS IVDEFVEAVH ARWPKAVVQF EDFQAKWAFE TLDRYRKKFC MFNDDIQGTA
     GVALAGLLGT VRAQGRPLTD FANQKIVVVG AGSAGLGVLK MALQAVSRMT GPSADPHFFL
     LDKNGLITKD RKDIDPAALP FAKAHHEIEG LGLQEGAGLA EVVKKVKPHV LLGLSGVGGI
     FHEEVLRAMK ESDSVRPAIF AMSNPTNNAE CCPVDAFKLA GEDIVFASGS PFANVDLGNG
     KIGHVNQANN MYLFPGIGLG ALLSGARNIS DTMLEAAAEC LASYMSDDEI NRGILYPSID
     DIRDITAEVG AAVLRAAVAE DLAEGHGDVG VKELQHMSKE ETIEHVRQNM WYPVYGPLVH
     E