ID   MAOX_ANAPL              Reviewed;         557 AA.
AC   P28227;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-NOV-2008, entry version 53.
DE   RecName: Full=NADP-dependent malic enzyme;
DE            Short=NADP-ME;
DE            EC=1.1.1.40;
GN   Name=ME1;
OS   Anas platyrhynchos (Domestic duck) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Anseriformes; Anatidae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND COFACTOR.
RC   TISSUE=Liver;
RX   MEDLINE=92322014; PubMed=1622402;
RA   Hsu R.Y., Glynias M.J., Satterlee J.D., Feeney R., Clarke A.R.,
RA   Emery D.S., Roe B.A., Wilson R.K., Goodridge A.G., Holbrook J.J.;
RT   "Duck liver 'malic' enzyme. Expression in Escherichia coli and
RT   characterization of the wild-type enzyme and site-directed mutants.";
RL   Biochem. J. 284:869-876(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 86-107.
RC   TISSUE=Liver;
RX   MEDLINE=92002141; PubMed=1911848; DOI=10.1016/0167-4838(91)90065-8;
RA   Satterlee J.D., Hsu R.Y.;
RT   "Duck liver malic enzyme: sequence of a tryptic peptide containing the
RT   cysteine residue labeled by the substrate analog bromopyruvate.";
RL   Biochim. Biophys. Acta 1079:247-252(1991).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = pyruvate + CO(2) +
CC       NADPH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
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DR   EMBL; X66418; CAA47049.1; -; mRNA.
DR   PIR; S23435; S23435.
DR   HSSP; P40927; 1GQ2.
DR   HOVERGEN; P28227; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004473; F:malate dehydrogenase (oxaloacetate-decarbox...; IEA:EC.
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; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N.
DR   InterPro; IPR012302; Malic_NAD_bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    557       NADP-dependent malic enzyme.
FT                                /FTId=PRO_0000160196.
FT   NP_BIND     290    307       NADP (By similarity).
FT   ACT_SITE     91     91       Proton donor (By similarity).
FT   ACT_SITE    162    162       Proton acceptor (By similarity).
FT   METAL       234    234       Divalent metal cation (By similarity).
FT   METAL       235    235       Divalent metal cation (By similarity).
FT   METAL       258    258       Divalent metal cation (By similarity).
FT   BINDING     144    144       NADP (By similarity).
FT   BINDING     258    258       NADP (By similarity).
FT   BINDING     397    397       NADP (By similarity).
FT   SITE        258    258       Important for activity (By similarity).
SQ   SEQUENCE   557 AA;  61898 MW;  BE6ED42C7017EF19 CRC64;
     MKRGYEVLRD PHLNKGMAFT LEERQQLNIH GLLPPCFLGQ DVQVFSILKN FERLTSDLDR
     YILLMSLQDR NEKLFYKVLT SDIERFMPIV YTPTVGLACQ QYGLAFRRPR GLFITIHDRG
     HIATMLKSWP ESVIKAIVVT DGERILGLGD LGCYGMGIPV GKLALYTACG GVKPHECLPV
     MLDVGTDNEA LLKDPLYIGL RHKRIRGQAY DDLLDEFMEA VTSRYGMNCL IQFEDFANAN
     AFRLLHKYRN KYCTFNDDIQ GTASVAVAGL LAALRITKNR LSDHTVLFQG AGEAALGIAN
     LIVMAMEKEG VSKEAAVKRI WMVDSKGLIV KGRASLTAEK TRFAHEHAEM KNLEDIVKDI
     KPSVLIGVAA IGGAFTKEIL QDMAAFNKRP IIFALSNPTS KAECTAEQCY KYTEGRGIFA
     SGSPFDPVTL PNGKTLYPGQ GNNSYVFPGV ALGVIACGLK HIGEDVFLTT AEVIAEQVSE
     ENLQEGRLYP PLVTIQHVSL KIAVRIAEEA YRNNTASTYP QPKDLEAFIQ SQIYSTDYNS
     FVADSYTWPE EAMKVKL
//