ID   MAOM_SOLTU              Reviewed;         626 AA.
AC   P37221;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=NAD-dependent malic enzyme 62 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; Z23023; CAA80559.1; -; mRNA.
DR   PIR; B53318; B53318.
DR   RefSeq; NP_001275278.1; NM_001288349.1.
DR   AlphaFoldDB; P37221; -.
DR   SMR; P37221; -.
DR   PRIDE; P37221; -.
DR   GeneID; 102598070; -.
DR   KEGG; sot:102598070; -.
DR   OrthoDB; 435571at2759; -.
DR   SABIO-RK; P37221; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P37221; 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..34
FT                   /note="Mitochondrion"
FT   CHAIN           35..626
FT                   /note="NAD-dependent malic enzyme 62 kDa isoform,
FT                   mitochondrial"
FT                   /id="PRO_0000018543"
FT   ACT_SITE        146
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            312
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   626 AA;  69953 MW;  8548B532B70A917C CRC64;
     MAIFSNQMRL SSTLLKRLHQ RVAAAVNSSS SRNFTTTEGH RPTIVHKRSL DILHDPWFNK
     GTAFSFTERD RLHIRGLLPP NVMSFEQQIA RFMADLKRLE VQARDGPSDP YVLAKWRILN
     RLHDRNETLY YKVLMENIEE YAPIVYTPTV GLVCQKYSGL FRRPRGMYFS AEDRGEMMSM
     VYNWPADQVD MIVVTDGSRI LGLGDLGIQG IGIAIGKLDL YVAAAGINPQ RVLPVMIDVG
     TDNENLLKDP LYLGLQDHRL DGEEYIEVID EFMEAVFTRW PHVIVQFEDF QSKWAFKLLQ
     RYRNNYRMFN DDIQGTAGVA IAGLLGAVRA QGRPMIDFPK MKIVVAGAGS AGIGVLNAAR
     KTMARMLGNT EIAFESARSQ FWVVDAKGLI TEARENVDPD ARPFARKIKE IERQGLSEGA
     TLAEVVREVK PDVLLGLSAC GGLFSKEVLE ALKHSTSTRP AIFPMSNPTR NAECTPEEAF
     SILGENIIFA SGSPFKDVDL GNGHVGHCNQ ANNMFLFPGI GLGTLLSGSR IVSDGMLQAA
     AECLAAYITE EEVLKGIIYP SISRIRDITK EVAAAVVKEA IEEDLAEGYR EMDSRELRKL
     DEAQISEFVE NNMWSPDYPT LVYKKD