ID   MAOX_VITVI              Reviewed;         591 AA.
AC   P51615;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=NADP-dependent malic enzyme;
DE            Short=NADP-ME;
DE            EC=1.1.1.40;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Thompson; TISSUE=Fruit;
RX   PubMed=7716227; DOI=10.1104/pp.107.3.1009;
RA   Franke K.E., Adams D.O.;
RT   "Cloning of a full-length cDNA for malic enzyme (EC 1.1.1.40) from grape
RT   berries.";
RL   Plant Physiol. 107:1009-1010(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate;
CC         Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=1.1.1.40;
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: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; L34836; AAA67087.1; -; mRNA.
DR   RefSeq; NP_001268142.1; NM_001281213.1.
DR   AlphaFoldDB; P51615; -.
DR   SMR; P51615; -.
DR   STRING; 29760.VIT_11s0016g03210.t01; -.
DR   PRIDE; P51615; -.
DR   GeneID; 100233140; -.
DR   KEGG; vvi:100233140; -.
DR   eggNOG; KOG1257; Eukaryota.
DR   OrthoDB; 435571at2759; -.
DR   ExpressionAtlas; P51615; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..591
FT                   /note="NADP-dependent malic enzyme"
FT                   /id="PRO_0000160204"
FT   ACT_SITE        139
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         335..351
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            306
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   591 AA;  65227 MW;  FD78B0976A7C4744 CRC64;
     MESTLKDIRD GASVLDLDPK ATVGGGVEDL YGEDFATEDQ LVTPWTVSVA SGYSLLRDPR
     HNKGLAFNDK ERDAHYLCGL LPPVVSTQEL QERKLMNSIR QYQVPLQKYM AMMDLQERNE
     RLFYKLLIDN VEELLPVVYT PTVGEACQKY GSIFRRPQGL YISLKEKGKI LEVLKNWPER
     RIQVIVVTDG ERILGLGDLG CQGMGIPVGK LSLYTALGGV RPSACLPITI DVGTNNEKLL
     ANEFYIGLKQ RRATGKEYSE FLQEFMSPVK QNYGEKVLIQ FEDFANHNAF DLLAKYGTTH
     LAFNDDIQGT ASVVLAGIVS ALRLLGGTLA DHKFLFLGAG EAGTGIAELI ALEMSKQTKC
     PIEETRKKIW LVDSKGLIVG SRKDSLQQFK KPWAHEHEPV KDLLDAVKVI KPTVLIGSSG
     VGKAFTKEVI EAMASCNEKP LILALSNPTS QSECTAEEAY TWTQGRAIFA SGSPFDPVEY
     NGKTFVPGQA NNAYIFPGLG MGLVISGAIR VHDEMLLAAS EALARQVTQE NFDKGLIYPP
     FSNIRKISAH IAANVAAKAY ELGLATRLPQ PENLVKYAES CMYSPVYRSY R