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UniProtKB/Swiss-Prot entry P20967


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

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Entry information
Entry name ODO1_YEAST
Primary accession number P20967
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1995 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name 2-oxoglutarate dehydrogenase E1 component, mitochondrial [Precursor]
Synonyms EC 1.2.4.2
Alpha-ketoglutarate dehydrogenase
Gene name
Name: KGD1
Synonyms: OGD1
OrderedLocusNames: YIL125W
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 FUNCTION.
STRAIN=ATCC 208353 / W303-1A;
PubMed=2503710 [NCBI, ExPASy, EBI, Israel, Japan]
Repetto B., Tzagoloff A.;
"Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase.";
Mol. Cell. Biol. 9:2695-2705(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169870 [NCBI, ExPASy, EBI, Israel, Japan]
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
FUNCTION.
DOI=10.1007/BF00351844; PubMed=8299151 [NCBI, ExPASy, EBI, Israel, Japan]
Mockovciakova D., Janitorova V., Zigova M., Kaclikova E., Zagulski M., Subik J.;
"The ogd1 and kgd1 mutants lacking 2-oxoglutarate dehydrogenase activity in yeast are allelic and can be differentiated by the cloned amber suppressor.";
Curr. Genet. 24:377-381(1993).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1007/s007090200005; PubMed=11926067 [NCBI, ExPASy, EBI, Israel, Japan]
Sato H., Tachifuji A., Tamura M., Miyakawa I.;
"Identification of the YMN-1 antigen protein and biochemical analyses of protein components in the mitochondrial nucleoid fraction of the yeast Saccharomyces cerevisiae.";
Protoplasma 219:51-58(2002).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
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).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-901, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • ENZYME REGULATION: Catabolite repressed.
  • SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid.
  • MISCELLANEOUS: Present with 14300 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
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
M26390; AAA34721.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46833; CAA86867.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S49884; DEBY.
RefSeq NP_012141.1; -.
3D structure databases
ModBase P20967.
Protein-protein interaction databases
DIP DIP:365N; -.
IntAct P20967; -.
Organism-specific databases
CYGD YIL125w; -.
SGD S000001387; KGD1.
Yeast-GFP YIL125W.
Gene expression databases
ArrayExpress P20967; -.
GermOnline YIL125W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0042645; Cellular component: mitochondrial nucleoid (inferred from direct assay from SGD).
GO:0009353; Cellular component: mitochondrial oxoglutarate dehydrogenase complex (inferred from direct assay from SGD).
GO:0004591; Molecular function: oxoglutarate dehydrogenase (succinyl-transferring) activity (inferred from electronic annotation from InterPro).
GO:0030976; Molecular function: thiamin pyrophosphate binding (inferred from electronic annotation from InterPro).
GO:0006103; Biological process: 2-oxoglutarate metabolic process (traceable author statement from SGD).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR011603; 2oxoglutarate_DHase_E1.
IPR001017; DHase_E1.
IPR005475; Transketo_Cen_R.
Graphical view of domain structure.
PANTHER PTHR23152; 2oxoglutarate_DH_E1; 1.
Pfam PF00676; E1_dh; 1.
PF02779; Transket_pyr; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000157; Oxoglu_dh_E1; 1.
TIGRFAMs TIGR00239; 2oxo_dh_E1; 1.
ProtoNet P20967.
Proteomic databases
PeptideAtlas P20967; -.
Genome annotation databases
Ensembl YIL125W; Saccharomyces cerevisiae. [Contig view]
GeneID 854681; -.
GenomeReviews Z47047_GR; YIL125W.
KEGG sce:YIL125W; -.
NMPDR fig|4932.3.peg.1665; -.
Phylogenomic databases
HOGENOM P20967; -.
Other
LinkHub P20967; -.
NextBio 977289; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     30  30     Mitochondrion (Potential). 
CHAIN   31   1014  984     2-oxoglutarate dehydrogenase E1 component, mitochondrial. PRO_0000020436
MOD_RES   901    901        Phosphotyrosine. 
CONFLICT   325    327        SEF -> LNL (in Ref. 1; AAA34721). 
CONFLICT   513    513        Q -> R (in Ref. 1; AAA34721). 
CONFLICT   568    568        A -> T (in Ref. 1; AAA34721). 
Sequence information
Length: 1014 AA [This is the length of the unprocessed precursor] Molecular weight: 114416 Da [This is the MW of the unprocessed precursor] CRC64: EF987C4DECE3F09F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRFVSSQTC RYSSRGLLKT SLLKNASTVK IVGRGLATTG TDNFLSTSNA TYIDEMYQAW 

        70         80         90        100        110        120 
QKDPSSVHVS WDAYFKNMSN PKIPATKAFQ APPSISNFPQ GTEAAPLGTA MTGSVDENVS 

       130        140        150        160        170        180 
IHLKVQLLCR AYQVRGHLKA HIDPLGISFG SNKNNPVPPE LTLDYYGFSK HDLDKEINLG 

       190        200        210        220        230        240 
PGILPRFARD GKSKMSLKEI VDHLEKLYCS SYGVQYTHIP SKQKCDWLRE RIEIPEPYQY 

       250        260        270        280        290        300 
TVDQKRQILD RLTWATSFES FLSTKFPNDK RFGLEGLESV VPGIKTLVDR SVELGVEDIV 

       310        320        330        340        350        360 
LGMAHRGRLN VLSNVVRKPN ESIFSEFKGS SARDDIEGSG DVKYHLGMNY QRPTTSGKYV 

       370        380        390        400        410        420 
NLSLVANPSH LESQDPVVLG RTRALLHAKN DLKEKTKALG VLLHGDAAFA GQGVVYETMG 

       430        440        450        460        470        480 
FLTLPEYSTG GTIHVITNNQ IGFTTDPRFA RSTPYPSDLA KAIDAPIFHV NANDVEAVTF 

       490        500        510        520        530        540 
IFNLAAEWRH KFHTDAIIDV VGWRKHGHNE TDQPSFTQPL MYKKIAKQKS VIDVYTEKLI 

       550        560        570        580        590        600 
SEGTFSKKDI DEHKKWVWNL FEDAFEKAKD YVPSQREWLT AAWEGFKSPK ELATEILPHE 

       610        620        630        640        650        660 
PTNVPESTLK ELGKVLSSWP EGFEVHKNLK RILKNRGKSI ETGEGIDWAT GEALAFGTLV 

       670        680        690        700        710        720 
LDGQNVRVSG EDVERGTFSQ RHAVLHDQQS EAIYTPLSTL NNEKADFTIA NSSLSEYGVM 

       730        740        750        760        770        780 
GFEYGYSLTS PDYLVMWEAQ FGDFANTAQV IIDQFIAGGE QKWKQRSGLV LSLPHGYDGQ 

       790        800        810        820        830        840 
GPEHSSGRLE RFLQLANEDP RYFPSEEKLQ RQHQDCNFQV VYPTTPANLF HILRRQQHRQ 

       850        860        870        880        890        900 
FRKPLALFFS KQLLRHPLAR SSLSEFTEGG FQWIIEDIEH GKSIGTKEET KRLVLLSGQV 

       910        920        930        940        950        960 
YTALHKRRES LGDKTTAFLK IEQLHPFPFA QLRDSLNSYP NLEEIVWCQE EPLNMGSWAY 

       970        980        990       1000       1010 
TEPRLHTTLK ETDKYKDFKV RYCGRNPSGA VAAGSKSLHL AEEDAFLKDV FQQS 

P20967 in FASTA format

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