MAOM_YEAST
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 03-AUG-2022, entry version 183.
DE RecName: Full=NAD-dependent malic enzyme, mitochondrial;
DE Short=NAD-ME;
DE EC=1.1.1.38;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
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 -!- 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=1.1.1.38;
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 -!- 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; 172.
DR DIP; DIP-4444N; -.
DR IntAct; P36013; 74.
DR MINT; P36013; -.
DR STRING; 4932.YKL029C; -.
DR CarbonylDB; P36013; -.
DR MaxQB; P36013; -.
DR PaxDb; P36013; -.
DR PRIDE; P36013; -.
DR EnsemblFungi; YKL029C_mRNA; YKL029C; YKL029C.
DR GeneID; 853839; -.
DR KEGG; sce:YKL029C; -.
DR SGD; S000001512; MAE1.
DR VEuPathDB; FungiDB:YKL029C; -.
DR eggNOG; KOG1257; Eukaryota.
DR GeneTree; ENSGT00950000183134; -.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; P36013; -.
DR OMA; QMWDPVY; -.
DR BioCyc; MetaCyc:YKL029C-MON; -.
DR BioCyc; YEAST:YKL029C-MON; -.
DR PRO; PR:P36013; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36013; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004470; F:malic enzyme activity; IDA:SGD.
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:0006520; P:cellular amino acid metabolic process; IMP:SGD.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IMP:SGD.
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 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..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 354
FT /note="Important for activity"
FT /evidence="ECO:0000250"
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
