ID   MAOM_YEAST              Reviewed;         669 AA.
AC   P36013; D6VXQ5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   04-NOV-2026, entry version 203.
DE   RecName: Full=NAD-dependent malic enzyme, mitochondrial;
DE            Short=NAD-ME;
DE            EC=1.1.1.38 {ECO:0000250|UniProtKB:P23368};
DE   Flags: Precursor;
GN   Name=MAE1; OrderedLocusNames=YKL029C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX   PubMed=9603875; DOI=10.1128/jb.180.11.2875-2882.1998;
RA   Boles E., de Jong-Gubbels P., Pronk J.T.;
RT   "Identification and characterization of MAE1, the Saccharomyces cerevisiae
RT   structural gene encoding mitochondrial malic enzyme.";
RL   J. Bacteriol. 180:2875-2882(1998).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC   -!- FUNCTION: NAD-dependent mitochondrial malic enzyme that catalyzes the
CC       oxidative decarboxylation of malate to pyruvate.
CC       {ECO:0000250|UniProtKB:P23368}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = pyruvate + CO2 + NADH;
CC         Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC         Evidence={ECO:0000250|UniProtKB:P23368};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + H(+) = pyruvate + CO2; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=1.1.1.38;
CC         Evidence={ECO:0000250|UniProtKB:P23368};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P23368};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P23368};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000250|UniProtKB:P23368};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9603875}.
CC   -!- MISCELLANEOUS: Present with 10500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; Z28029; CAA81865.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09125.1; -; Genomic_DNA.
DR   PIR; S37846; S37846.
DR   RefSeq; NP_012896.1; NM_001179595.1.
DR   AlphaFoldDB; P36013; -.
DR   SMR; P36013; -.
DR   BioGRID; 34102; 292.
DR   DIP; DIP-4444N; -.
DR   FunCoup; P36013; 1136.
DR   IntAct; P36013; 80.
DR   STRING; 4932.YKL029C; -.
DR   CarbonylDB; P36013; -.
DR   iPTMnet; P36013; -.
DR   PaxDb; 4932-YKL029C; -.
DR   PeptideAtlas; P36013; -.
DR   EnsemblFungi; YKL029C_mRNA; YKL029C; YKL029C.
DR   GeneID; 853839; -.
DR   KEGG; sce:YKL029C; -.
DR   AGR; SGD:S000001512; -.
DR   SGD; S000001512; MAE1.
DR   VEuPathDB; FungiDB:YKL029C; -.
DR   eggNOG; KOG1257; Eukaryota.
DR   HOGENOM; CLU_011405_5_2_1; -.
DR   InParanoid; P36013; -.
DR   OMA; AACERPM; -.
DR   OrthoDB; 5365701at2759; -.
DR   BioCyc; MetaCyc:YKL029C-MONOMER; -.
DR   BioCyc; YEAST:YKL029C-MONOMER; -.
DR   BioGRID-ORCS; 853839; 4 hits in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
DR   PRO; PR:P36013; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36013; protein.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0004470; F:malic enzyme activity; IDA:SGD.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; ISS:UniProtKB.
DR   GO; GO:0006520; P:amino acid metabolic process; IMP:SGD.
DR   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   FunFam; 3.40.50.10380:FF:000001; NAD-dependent malic enzyme; 1.
DR   FunFam; 3.40.50.720:FF:000055; NAD-dependent malic enzyme; 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   NCBIfam; NF010052; maeA; 1.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF34; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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   1: Evidence at protein level;
KW   Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..669
FT                   /note="NAD-dependent malic enzyme, mitochondrial"
FT                   /id="PRO_0000160206"
FT   REGION          33..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         142
FT                   /ligand="fumarate"
FT                   /ligand_id="ChEBI:CHEBI:29806"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         330
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         331
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         354
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         387
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         390
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         499
FT                   /ligand="(S)-malate"
FT                   /ligand_id="ChEBI:CHEBI:15589"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
FT   BINDING         539
FT                   /ligand="(S)-malate"
FT                   /ligand_id="ChEBI:CHEBI:15589"
FT                   /evidence="ECO:0000250|UniProtKB:P23368"
SQ   SEQUENCE   669 AA;  74376 MW;  0122B52E846B748F CRC64;
     MLRTRLSVSV AARSQLTRSL TASRTAPLRR WPIQQSRLYS SNTRSHKATT TRENTFQKPY
     SDEEVTKTPV GSRARKIFEA PHPHATRLTV EGAIECPLES FQLLNSPLFN KGSAFTQEER
     EAFNLEALLP PQVNTLDEQL ERSYKQLCYL KTPLAKNDFM TSLRVQNKVL YFALIRRHIK
     ELVPIIYTPT EGDAIAAYSH RFRKPEGVFL DITEPDSIEC RLATYGGDKD VDYIVVSDSE
     GILGIGDQGI GGVRIAISKL ALMTLCGGIH PGRVLPVCLD VGTNNKKLAR DELYMGNKFS
     RIRGKQYDDF LEKFIKAVKK VYPSAVLHFE DFGVKNARRL LEKYRYELPS FNDDIQGTGA
     VVMASLIAAL KHTNRDLKDT RVLIYGAGSA GLGIADQIVN HMVTHGVDKE EARKKIFLMD
     RRGLILQSYE ANSTPAQHVY AKSDAEWAGI NTRSLHDVVE NVKPTCLVGC STQAGAFTQD
     VVEEMHKHNP RPIIFPLSNP TRLHEAVPAD LMKWTNNNAL VATGSPFPPV DGYRISENNN
     CYSFPGIGLG AVLSRATTIT DKMISAAVDQ LAELSPLREG DSRPGLLPGL DTITNTSARL
     ATAVILQALE EGTARIEQEQ VPGGAPGETV KVPRDFDECL QWVKAQMWEP VYRPMIKVQH
     DPSVHTNQL
//