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Database: UniProt/SWISS-PROT
Entry: ODO1_YEAST
LinkDB: ODO1_YEAST
Original site: ODO1_YEAST 
ID   ODO1_YEAST              Reviewed;        1014 AA.
AC   P20967; D6VVG2;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   28-MAR-2018, entry version 167.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE            EC=1.2.4.2;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE            Short=OGDC-E1;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE   Flags: Precursor;
GN   Name=KGD1; Synonyms=OGD1; OrderedLocusNames=YIL125W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=2503710; DOI=10.1128/MCB.9.6.2695;
RA   Repetto B., Tzagoloff A.;
RT   "Structure and regulation of KGD1, the structural gene for yeast
RT   alpha-ketoglutarate dehydrogenase.";
RL   Mol. Cell. Biol. 9:2695-2705(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
RA   Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
RA   Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
RA   Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=8299151; DOI=10.1007/BF00351844;
RA   Mockovciakova D., Janitorova V., Zigova M., Kaclikova E., Zagulski M.,
RA   Subik J.;
RT   "The ogd1 and kgd1 mutants lacking 2-oxoglutarate dehydrogenase
RT   activity in yeast are allelic and can be differentiated by the cloned
RT   amber suppressor.";
RL   Curr. Genet. 24:377-381(1993).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11926067; DOI=10.1007/s007090200005;
RA   Sato H., Tachifuji A., Tamura M., Miyakawa I.;
RT   "Identification of the YMN-1 antigen protein and biochemical analyses
RT   of protein components in the mitochondrial nucleoid fraction of the
RT   yeast Saccharomyces cerevisiae.";
RL   Protoplasma 219:51-58(2002).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
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.,
RA   Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
RA   Rehling P., Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-
CC       oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC       succinyltransferase (E2) and lipoamide dehydrogenase (E3).
CC       {ECO:0000269|PubMed:11926067, ECO:0000269|PubMed:2503710,
CC       ECO:0000269|PubMed:8299151}.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- ENZYME REGULATION: Catabolite repressed.
CC   -!- INTERACTION:
CC       P19262:KGD2; NbExp=8; IntAct=EBI-12459, EBI-12464;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion matrix,
CC       mitochondrion nucleoid.
CC   -!- MISCELLANEOUS: Present with 14300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000305}.
DR   EMBL; M26390; AAA34721.1; -; Genomic_DNA.
DR   EMBL; Z46833; CAA86867.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08428.1; -; Genomic_DNA.
DR   PIR; S49884; DEBY.
DR   RefSeq; NP_012141.1; NM_001179473.1.
DR   ProteinModelPortal; P20967; -.
DR   SMR; P20967; -.
DR   BioGrid; 34866; 119.
DR   DIP; DIP-365N; -.
DR   IntAct; P20967; 48.
DR   MINT; P20967; -.
DR   STRING; 4932.YIL125W; -.
DR   iPTMnet; P20967; -.
DR   MaxQB; P20967; -.
DR   PaxDb; P20967; -.
DR   PRIDE; P20967; -.
DR   EnsemblFungi; YIL125W; YIL125W; YIL125W.
DR   GeneID; 854681; -.
DR   KEGG; sce:YIL125W; -.
DR   EuPathDB; FungiDB:YIL125W; -.
DR   SGD; S000001387; KGD1.
DR   GeneTree; ENSGT00530000063092; -.
DR   HOGENOM; HOG000259586; -.
DR   InParanoid; P20967; -.
DR   KO; K00164; -.
DR   OMA; IDMVCYR; -.
DR   OrthoDB; EOG092C0B3K; -.
DR   BioCyc; YEAST:YIL125W-MONOMER; -.
DR   Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-SCE-71064; Lysine catabolism.
DR   Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR   PRO; PR:P20967; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IDA:SGD.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; TAS:SGD.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; TAS:SGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; TAS:SGD.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Mitochondrion; Mitochondrion nucleoid;
KW   Oxidoreductase; Reference proteome; Thiamine pyrophosphate;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     30       Mitochondrion. {ECO:0000255}.
FT   CHAIN        31   1014       2-oxoglutarate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000020436.
FT   CONFLICT    325    327       SEF -> LNL (in Ref. 1; AAA34721).
FT                                {ECO:0000305}.
FT   CONFLICT    513    513       Q -> R (in Ref. 1; AAA34721).
FT                                {ECO:0000305}.
FT   CONFLICT    568    568       A -> T (in Ref. 1; AAA34721).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1014 AA;  114416 MW;  EF987C4DECE3F09F CRC64;
     MLRFVSSQTC RYSSRGLLKT SLLKNASTVK IVGRGLATTG TDNFLSTSNA TYIDEMYQAW
     QKDPSSVHVS WDAYFKNMSN PKIPATKAFQ APPSISNFPQ GTEAAPLGTA MTGSVDENVS
     IHLKVQLLCR AYQVRGHLKA HIDPLGISFG SNKNNPVPPE LTLDYYGFSK HDLDKEINLG
     PGILPRFARD GKSKMSLKEI VDHLEKLYCS SYGVQYTHIP SKQKCDWLRE RIEIPEPYQY
     TVDQKRQILD RLTWATSFES FLSTKFPNDK RFGLEGLESV VPGIKTLVDR SVELGVEDIV
     LGMAHRGRLN VLSNVVRKPN ESIFSEFKGS SARDDIEGSG DVKYHLGMNY QRPTTSGKYV
     NLSLVANPSH LESQDPVVLG RTRALLHAKN DLKEKTKALG VLLHGDAAFA GQGVVYETMG
     FLTLPEYSTG GTIHVITNNQ IGFTTDPRFA RSTPYPSDLA KAIDAPIFHV NANDVEAVTF
     IFNLAAEWRH KFHTDAIIDV VGWRKHGHNE TDQPSFTQPL MYKKIAKQKS VIDVYTEKLI
     SEGTFSKKDI DEHKKWVWNL FEDAFEKAKD YVPSQREWLT AAWEGFKSPK ELATEILPHE
     PTNVPESTLK ELGKVLSSWP EGFEVHKNLK RILKNRGKSI ETGEGIDWAT GEALAFGTLV
     LDGQNVRVSG EDVERGTFSQ RHAVLHDQQS EAIYTPLSTL NNEKADFTIA NSSLSEYGVM
     GFEYGYSLTS PDYLVMWEAQ FGDFANTAQV IIDQFIAGGE QKWKQRSGLV LSLPHGYDGQ
     GPEHSSGRLE RFLQLANEDP RYFPSEEKLQ RQHQDCNFQV VYPTTPANLF HILRRQQHRQ
     FRKPLALFFS KQLLRHPLAR SSLSEFTEGG FQWIIEDIEH GKSIGTKEET KRLVLLSGQV
     YTALHKRRES LGDKTTAFLK IEQLHPFPFA QLRDSLNSYP NLEEIVWCQE EPLNMGSWAY
     TEPRLHTTLK ETDKYKDFKV RYCGRNPSGA VAAGSKSLHL AEEDAFLKDV FQQS
//
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