ID   MDHP_YEAST              Reviewed;         343 AA.
AC   P32419; Q12689;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 84.
DE   RecName: Full=Malate dehydrogenase, peroxisomal;
DE            EC=1.1.1.37;
GN   Name=MDH3; OrderedLocusNames=YDL078C; ORFNames=D2468;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16; 23-36
RP   AND 153-167.
RX   MEDLINE=93077569; PubMed=1447211;
RA   Steffan J.S., McAlister-Henn L.;
RT   "Isolation and characterization of the yeast gene encoding the MDH3
RT   isozyme of malate dehydrogenase.";
RL   J. Biol. Chem. 267:24708-24715(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-10598, EBI-10598;
CC       P43582:-; NbExp=1; IntAct=EBI-10598, EBI-22766;
CC       P22696:ESS1; NbExp=1; IntAct=EBI-10598, EBI-6679;
CC       P33203:PRP40; NbExp=1; IntAct=EBI-10598, EBI-701;
CC       P39940:RSP5; NbExp=1; IntAct=EBI-10598, EBI-16219;
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
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 3300 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
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DR   EMBL; M98763; AAA34767.1; -; Genomic_DNA.
DR   EMBL; Z74126; CAA98644.1; -; Genomic_DNA.
DR   PIR; S67614; DEBYMP.
DR   RefSeq; NP_010205.1; -.
DR   HSSP; P00346; 1MLD.
DR   DIP; DIP:6473N; -.
DR   IntAct; P32419; -.
DR   PeptideAtlas; P32419; -.
DR   Ensembl; YDL078C; Saccharomyces cerevisiae.
DR   GeneID; 851481; -.
DR   GenomeReviews; Z71256_GR; YDL078C.
DR   KEGG; sce:YDL078C; -.
DR   NMPDR; fig|4932.3.peg.945; -.
DR   CYGD; YDL078c; -.
DR   SGD; S000002236; MDH3.
DR   HOGENOM; P32419; -.
DR   LinkHub; P32419; -.
DR   NextBio; 968795; -.
DR   GermOnline; YDL078C; Saccharomyces cerevisiae.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; TAS:SGD.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006735; P:NADH regeneration; TAS:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001557; L-lactate/malate_DHase.
DR   InterPro; IPR001236; Lactate/malate_DHase.
DR   InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DHase_AS.
DR   InterPro; IPR010097; Malate_DHase_NAD-dep_euk_g_bac.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11540:SF1; MDH_euk_g_bac; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Glyoxylate bypass; NAD;
KW   Oxidoreductase; Peroxisome; Tricarboxylic acid cycle.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    343       Malate dehydrogenase, peroxisomal.
FT                                /FTId=PRO_0000113342.
FT   NP_BIND       8     14       NAD (By similarity).
FT   NP_BIND     116    118       NAD (By similarity).
FT   ACT_SITE    187    187       Proton acceptor (By similarity).
FT   BINDING      34     34       NAD (By similarity).
FT   BINDING      80     80       Substrate (By similarity).
FT   BINDING      86     86       Substrate (By similarity).
FT   BINDING      93     93       NAD (By similarity).
FT   BINDING     118    118       Substrate (By similarity).
FT   BINDING     152    152       Substrate (By similarity).
FT   BINDING     237    237       NAD (By similarity).
FT   CONFLICT    240    240       A -> R (in Ref. 1; AAA34767).
SQ   SEQUENCE   343 AA;  37186 MW;  54725114B2CAD6A5 CRC64;
     MVKVAILGAS GGVGQPLSLL LKLSPYVSEL ALYDIRAAEG IGKDLSHINT NSSCVGYDKD
     SIENTLSNAQ VVLIPAGVPR KPGLTRDDLF KMNAGIVKSL VTAVGKFAPN ARILVISNPV
     NSLVPIAVET LKKMGKFKPG NVMGVTNLDL VRAETFLVDY LMLKNPKIGQ EQDKTTMHRK
     VTVIGGHSGE TIIPIITDKS LVFQLDKQYE HFIHRVQFGG DEIVKAKQGA GSATLSMAFA
     GAKFAEEVLR SFHNEKPETE SLSAFVYLPG LKNGKKAQQL VGDNSIEYFS LPIVLRNGSV
     VSIDTSVLEK LSPREEQLVN TAVKELRKNI EKGKSFILDS SKL
//