ID Q9NIW0_DROME Unreviewed; 578 AA.
AC Q9NIW0;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 146.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN Name=Men {ECO:0000313|EMBL:AAF43603.1,
GN ECO:0000313|FlyBase:FBgn0002719};
GN ORFNames=CG10120 {ECO:0000313|FlyBase:FBgn0002719};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF43603.1};
RN [1] {ECO:0000313|EMBL:AAF43603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Oregon R {ECO:0000313|EMBL:AAF43603.1};
RA Cordes R., Tegethoff S., Schaefer U., Schaefer M.A.;
RT "Molecular characterisation of the P-element insertion line ms(3)1100A.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABA19464.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dpf_3.0 {ECO:0000313|EMBL:ABA19464.1}, Dpf_90.2
RC {ECO:0000313|EMBL:ABA19471.1}, Dpf_94.1 {ECO:0000313|EMBL:ABA19472.1},
RC Hfl97_12 {ECO:0000313|EMBL:ABA19476.1}, Hfl97_13
RC {ECO:0000313|EMBL:ABA19477.1}, Hfl97_17 {ECO:0000313|EMBL:ABA19480.1},
RC Hfl97_20 {ECO:0000313|EMBL:ABA19482.1}, Hfl97_28
RC {ECO:0000313|EMBL:ABA19483.1}, Hfl97_74 {ECO:0000313|EMBL:ABA19486.1},
RC Sc96_12.3 {ECO:0000313|EMBL:ABA19473.1}, and Sc96_19.4
RC {ECO:0000313|EMBL:ABA19474.1};
RX PubMed=16143603; DOI=10.1534/genetics.105.048249;
RA Merritt T.J., Duvernell D., Eanes W.F.;
RT "Natural and synthetic alleles provide complementary insights into the
RT nature of selection acting on the Men polymorphism of Drosophila
RT melanogaster.";
RL Genetics 171:1707-1718(2005).
RN [3] {ECO:0000313|EMBL:AFB81555.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SON08 {ECO:0000313|EMBL:AFB81555.1}, SON09
RC {ECO:0000313|EMBL:AFB81556.1}, SON11 {ECO:0000313|EMBL:AFB81558.1},
RC SON12 {ECO:0000313|EMBL:AFB81559.1}, SON17
RC {ECO:0000313|EMBL:AFB81562.1}, SON18 {ECO:0000313|EMBL:AFB81563.1},
RC SON25 {ECO:0000313|EMBL:AFB81570.1}, SON28
RC {ECO:0000313|EMBL:AFB81572.1}, SON30 {ECO:0000313|EMBL:AFB81574.1},
RC SON31 {ECO:0000313|EMBL:AFB81575.1}, SON34
RC {ECO:0000313|EMBL:AFB81577.1}, SON37 {ECO:0000313|EMBL:AFB81578.1},
RC SON44 {ECO:0000313|EMBL:AFB81581.1}, and SON46
RC {ECO:0000313|EMBL:AFB81583.1};
RX PubMed=22733181; DOI=10.1007/s10528-012-9523-3;
RA Rzezniczak T.Z., Lum T.E., Harniman R., Merritt T.J.;
RT "A Combination of Structural and Cis-Regulatory Factors Drives Biochemical
RT Differences in Drosophila melanogaster Malic Enzyme.";
RL Biochem. Genet. 50:823-837(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR EMBL; AF188000; AAF43603.1; -; mRNA.
DR EMBL; DQ148977; ABA19464.1; -; mRNA.
DR EMBL; DQ148984; ABA19471.1; -; mRNA.
DR EMBL; DQ148985; ABA19472.1; -; mRNA.
DR EMBL; DQ148986; ABA19473.1; -; mRNA.
DR EMBL; DQ148987; ABA19474.1; -; mRNA.
DR EMBL; DQ148989; ABA19476.1; -; mRNA.
DR EMBL; DQ148990; ABA19477.1; -; mRNA.
DR EMBL; DQ148993; ABA19480.1; -; mRNA.
DR EMBL; DQ148995; ABA19482.1; -; mRNA.
DR EMBL; DQ148996; ABA19483.1; -; mRNA.
DR EMBL; DQ148999; ABA19486.1; -; mRNA.
DR EMBL; JQ690829; AFB81555.1; -; mRNA.
DR EMBL; JQ690830; AFB81556.1; -; mRNA.
DR EMBL; JQ690832; AFB81558.1; -; mRNA.
DR EMBL; JQ690833; AFB81559.1; -; mRNA.
DR EMBL; JQ690836; AFB81562.1; -; mRNA.
DR EMBL; JQ690837; AFB81563.1; -; mRNA.
DR EMBL; JQ690844; AFB81570.1; -; mRNA.
DR EMBL; JQ690846; AFB81572.1; -; mRNA.
DR EMBL; JQ690848; AFB81574.1; -; mRNA.
DR EMBL; JQ690849; AFB81575.1; -; mRNA.
DR EMBL; JQ690851; AFB81577.1; -; mRNA.
DR EMBL; JQ690852; AFB81578.1; -; mRNA.
DR EMBL; JQ690855; AFB81581.1; -; mRNA.
DR EMBL; JQ690857; AFB81583.1; -; mRNA.
DR AlphaFoldDB; Q9NIW0; -.
DR AGR; FB:FBgn0002719; -.
DR FlyBase; FBgn0002719; Men.
DR VEuPathDB; VectorBase:FBgn0002719; -.
DR HOGENOM; CLU_011405_4_1_1; -.
DR ExpressionAtlas; Q9NIW0; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) 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:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR GO; GO:0030431; P:sleep; IMP:FlyBase.
DR CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_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 PANTHER; PTHR23406:SF80; GH17657P-RELATED; 1.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426,
KW ECO:0000313|EMBL:AAF43603.1}.
FT DOMAIN 97..278
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 288..541
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 263
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 578 AA; 63958 MW; 3273ABD6F03100C5 CRC64;
MSKPDSKLDK YAQRDRLGLW GTGDNEVVGS LSGFTRLLDK RYSKGLAFTH EERQQLGIHG
MLPYVVREPS EQVEHCRALL ARLDQDLDKY MYLISLSERN ERLFYNVLSS DIGYMMPLVY
TPTVGLACQR YSLIHQNAKG MFISIKDKGH IYDVLKNWPE TDVRAIVVTD GERILGLGDL
GANGMGIPVG KLSLYTALAG IKPSQCLPIT LDVGTNTESI LEDPLYIGLR ERRATGDLYD
EFIDEFMHAC VRRFGQNCLI QFEDFANANA FRLLSKYRDS FCTFNDDIQG TASVAVAGLL
ASLKIKKTQL KDNTLLFLGA GEAALGIANL CLMAMKVEGL TEEEAKARIW MVDSRGVITR
DRPKGGLTEH KLHFAQLHEP IDTLAEAVRK VRPNVLIGAA AQGGAFNQEI LELMADINET
PIIFALSNPT SKAECTAEEA YTYTKGRCIF ASGSPFAPVT YNNKKFYPGQ GNNSYIFPGV
ALGVLCAGML NIPEQVFLVA AERLAELVSK DDLAKGSLYP PLSSIVSCSM AIAERIVEYA
YKNGLATVRP EPVNKLAFIK AQMYDLDYPR SVPATYKM
//
