MAOX_ANAPL
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 03-AUG-2022, entry version 111.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40;
GN Name=ME1;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=1622402; DOI=10.1042/bj2840869;
RA Hsu R.Y., Glynias M.J., Satterlee J.D., Feeney R., Clarke A.R., Emery D.S.,
RA 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 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:
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;
CC Evidence={ECO:0000269|PubMed:1622402};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:1622402};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000269|PubMed:1622402};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; X66418; CAA47049.1; -; mRNA.
DR PIR; S23435; S23435.
DR RefSeq; XP_005024853.1; XM_005024796.2.
DR AlphaFoldDB; P28227; -.
DR SMR; P28227; -.
DR OrthoDB; 435571at2759; -.
DR SABIO-RK; P28227; -.
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 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 Cytoplasm; Direct protein sequencing; Metal-binding; NADP; Oxidoreductase.
FT CHAIN 1..557
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160196"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 290..307
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 258
FT /note="Important for activity"
FT /evidence="ECO:0000250"
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
