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UniProtKB/Swiss-Prot entry P32419


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MDHP_YEAST
Primary accession number P32419
Secondary accession number Q12689
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 82)
Name and origin of the protein
Protein name Malate dehydrogenase, peroxisomal
Synonym EC 1.1.1.37
Gene name
Name: MDH3
OrderedLocusNames: YDL078C
ORFNames: D2468
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16; 23-36 AND 153-167.
PubMed=1447211 [NCBI, ExPASy, EBI, Israel, Japan]
Steffan J.S., McAlister-Henn L.;
"Isolation and characterization of the yeast gene encoding the MDH3 isozyme of malate dehydrogenase.";
J. Biol. Chem. 267:24708-24715(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M98763; AAA34767.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74126; CAA98644.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S67614; DEBYMP.
RefSeq NP_010205.1; -.
3D structure databases
HSSP P00346; 1MLD. [HSSP ENTRY / PDB]
ModBase P32419.
Protein-protein interaction databases
DIP DIP:6473N; -.
IntAct P32419; -.
Organism-specific databases
CYGD YDL078c; -.
SGD S000002236; MDH3.
Yeast-GFP YDL078C.
Gene expression databases
GermOnline YDL078C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0030060; Molecular function: L-malate dehydrogenase activity (inferred from mutant phenotype from SGD).
GO:0006635; Biological process: fatty acid beta-oxidation (traceable author statement from SGD).
GO:0006097; Biological process: glyoxylate cycle (traceable author statement from SGD).
GO:0006108; Biological process: malate metabolic process (traceable author statement from SGD).
GO:0006735; Biological process: NADH regeneration (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR010097; Malate_DHase_NAD-dep_euk_g_bac.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11540:SF1; MDH_euk_g_bac; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
TIGRFAMs TIGR01772; MDH_euk_gproteo; 1.
PROSITE PS00068; MDH; 1.
BLOCKS P32419.
Proteomic databases
PeptideAtlas P32419; -.
Genome annotation databases
Ensembl YDL078C; Saccharomyces cerevisiae. [Contig view]
GeneID 851481; -.
GenomeReviews Z71256_GR; YDL078C.
KEGG sce:YDL078C; -.
NMPDR fig|4932.3.peg.945; -.
Phylogenomic databases
HOGENOM P32419; -.
Other
LinkHub P32419; -.
ProtoNet P32419.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Glyoxylate bypass; NAD; Oxidoreductase; Peroxisome; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   343  342     Malate dehydrogenase, peroxisomal. PRO_0000113342
NP_BIND   8    14  7     NAD (By similarity). 
NP_BIND   116   118  3     NAD (By similarity). 
ACT_SITE   187   187        Proton acceptor (By similarity). 
BINDING   34    34        NAD (By similarity). 
BINDING   80    80        Substrate (By similarity). 
BINDING   86    86        Substrate (By similarity). 
BINDING   93    93        NAD (By similarity). 
BINDING   118   118        Substrate (By similarity). 
BINDING   152   152        Substrate (By similarity). 
BINDING   237   237        NAD (By similarity). 
CONFLICT   240   240        A -> R (in Ref. 1; AAA34767). 
Sequence information
Length: 343 AA [This is the length of the unprocessed precursor] Molecular weight: 37186 Da [This is the MW of the unprocessed precursor] CRC64: 54725114B2CAD6A5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKVAILGAS GGVGQPLSLL LKLSPYVSEL ALYDIRAAEG IGKDLSHINT NSSCVGYDKD 

        70         80         90        100        110        120 
SIENTLSNAQ VVLIPAGVPR KPGLTRDDLF KMNAGIVKSL VTAVGKFAPN ARILVISNPV 

       130        140        150        160        170        180 
NSLVPIAVET LKKMGKFKPG NVMGVTNLDL VRAETFLVDY LMLKNPKIGQ EQDKTTMHRK 

       190        200        210        220        230        240 
VTVIGGHSGE TIIPIITDKS LVFQLDKQYE HFIHRVQFGG DEIVKAKQGA GSATLSMAFA 

       250        260        270        280        290        300 
GAKFAEEVLR SFHNEKPETE SLSAFVYLPG LKNGKKAQQL VGDNSIEYFS LPIVLRNGSV 

       310        320        330        340 
VSIDTSVLEK LSPREEQLVN TAVKELRKNI EKGKSFILDS SKL 

P32419 in FASTA format

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