MDHC_YEAST
ID MDHC_YEAST Reviewed; 377 AA.
AC P22133; D6W1U2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Malate dehydrogenase, cytoplasmic;
DE EC=1.1.1.37;
GN Name=MDH2; OrderedLocusNames=YOL126C;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17.
RX PubMed=1986231; DOI=10.1128/mcb.11.1.370-380.1991;
RA Minard K.I., McAlister-Henn L.;
RT "Isolation, nucleotide sequence analysis, and disruption of the MDH2 gene
RT from Saccharomyces cerevisiae: evidence for three isozymes of yeast malate
RT dehydrogenase.";
RL Mol. Cell. Biol. 11:370-380(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896265;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1013::aid-yea980%3e3.0.co;2-5;
RA Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E.,
RA Arino J.;
RT "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome
RT XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase,
RT the ribosomal L25 gene and four new open reading frames.";
RL Yeast 12:1013-1020(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-35.
RX PubMed=3552052; DOI=10.1016/0167-4838(87)90044-6;
RA Kopetzki E., Entian K.-D., Lottspeich F., Mecke D.;
RT "Purification procedure and N-terminal amino acid sequence of yeast malate
RT dehydrogenase isoenzymes.";
RL Biochim. Biophys. Acta 912:398-403(1987).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP DOMAIN, AND PROTEASOMAL DEGRADATION.
RX PubMed=28126757; DOI=10.1126/science.aal3655;
RA Chen S.J., Wu X., Wadas B., Oh J.H., Varshavsky A.;
RT "An N-end rule pathway that recognizes proline and destroys gluconeogenic
RT enzymes.";
RL Science 355:0-0(2017).
CC -!- FUNCTION: The isoenzyme MDH2 may function primarily in the glyoxylate
CC cycle.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40926}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By acetate as carbon source in the growth medium. Is
CC inactivated by addition of glucose (catabolite inactivation).
CC -!- DOMAIN: The Pro/N-degron targets the protein for proteasomal
CC degradation when cells are shifted to glucose-containing growth medium.
CC {ECO:0000269|PubMed:28126757}.
CC -!- PTM: Targeted for proteasomal degradation when cells are shifted to
CC glucose-containing growth medium. {ECO:0000269|PubMed:28126757}.
CC -!- MISCELLANEOUS: Yeast contains at least 3 malate dehydrogenase
CC isoenzymes: a mitochondrial (MDH1), a cytoplasmic (MDH2) and a
CC peroxisomal (MDH3).
CC -!- MISCELLANEOUS: Present with 5260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49466.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M62808; AAA34766.1; -; Genomic_DNA.
DR EMBL; U41293; AAC49466.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74868; CAA99145.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10658.1; -; Genomic_DNA.
DR PIR; S63444; DEBYMC.
DR RefSeq; NP_014515.2; NM_001183380.1.
DR AlphaFoldDB; P22133; -.
DR SMR; P22133; -.
DR BioGRID; 34249; 169.
DR DIP; DIP-4211N; -.
DR IntAct; P22133; 33.
DR MINT; P22133; -.
DR STRING; 4932.YOL126C; -.
DR iPTMnet; P22133; -.
DR MaxQB; P22133; -.
DR PaxDb; P22133; -.
DR PRIDE; P22133; -.
DR EnsemblFungi; YOL126C_mRNA; YOL126C; YOL126C.
DR GeneID; 853994; -.
DR KEGG; sce:YOL126C; -.
DR SGD; S000005486; MDH2.
DR VEuPathDB; FungiDB:YOL126C; -.
DR eggNOG; KOG1494; Eukaryota.
DR GeneTree; ENSGT00390000016686; -.
DR HOGENOM; CLU_047181_1_0_1; -.
DR InParanoid; P22133; -.
DR OMA; FGCAVEL; -.
DR BioCyc; YEAST:YOL126C-MON; -.
DR BRENDA; 1.1.1.37; 984.
DR SABIO-RK; P22133; -.
DR PRO; PR:P22133; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22133; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:SGD.
DR GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:SGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1986231,
FT ECO:0000269|PubMed:3552052"
FT CHAIN 2..377
FT /note="Malate dehydrogenase, cytoplasmic"
FT /id="PRO_0000113338"
FT MOTIF 2..5
FT /note="Pro/N-degron"
FT /evidence="ECO:0000269|PubMed:28126757"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00346"
FT BINDING 20..26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 144..146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 377 AA; 40731 MW; CAF4784FA7DD6E27 CRC64;
MPHSVTPSIE QDSLKIAILG AAGGIGQSLS LLLKAQLQYQ LKESNRSVTH IHLALYDVNQ
EAINGVTADL SHIDTPISVS SHSPAGGIEN CLHNASIVVI PAGVPRKPGM TRDDLFNVNA
GIISQLGDSI AECCDLSKVF VLVISNPVNS LVPVMVSNIL KNHPQSRNSG IERRIMGVTK
LDIVRASTFL REINIESGLT PRVNSMPDVP VIGGHSGETI IPLFSQSNFL SRLNEDQLKY
LIHRVQYGGD EVVKAKNGKG SATLSMAHAG YKCVVQFVSL LLGNIEQIHG TYYVPLKDAN
NFPIAPGADQ LLPLVDGADY FAIPLTITTK GVSYVDYDIV NRMNDMERNQ MLPICVSQLK
KNIDKGLEFV ASRSASS
