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   04-NOV-2026, entry version 213.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE            Short=OGDH;
DE            EC=1.2.4.2;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE            Short=OGDC-E1;
DE            Short=OGDHC subunit E1;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase complex subunit E1;
DE            Short=alpha-KGDHC subunit E1;
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; Saccharomycetes;
OC   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.9.6.2695-2705.1989;
RA   Repetto B., Tzagoloff A.;
RT   "Structure and regulation of KGD1, the structural gene for yeast alpha-
RT   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; DOI=10.1038/387s084;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   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., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBUNIT.
RX   PubMed=2072900; DOI=10.1128/mcb.11.8.3931-3939.1991;
RA   Repetto B., Tzagoloff A.;
RT   "In vivo assembly of yeast mitochondrial alpha-ketoglutarate dehydrogenase
RT   complex.";
RL   Mol. Cell. Biol. 11:3931-3939(1991).
RN   [5]
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 activity in
RT   yeast are allelic and can be differentiated by the cloned amber
RT   suppressor.";
RL   Curr. Genet. 24:377-381(1993).
RN   [6]
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 of
RT   protein components in the mitochondrial nucleoid fraction of the yeast
RT   Saccharomyces cerevisiae.";
RL   Protoplasma 219:51-58(2002).
RN   [7]
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   [8]
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   [9]
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., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [10]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=25165143; DOI=10.1091/mbc.e14-07-1178;
RA   Heublein M., Burguillos M.A., Voegtle F.N., Teixeira P.F., Imhof A.,
RA   Meisinger C., Ott M.;
RT   "The novel component Kgd4 recruits the E3 subunit to the mitochondrial
RT   alpha-ketoglutarate dehydrogenase.";
RL   Mol. Biol. Cell 25:3342-3349(2014).
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-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3). {ECO:0000269|PubMed:11926067,
CC       ECO:0000269|PubMed:2503710, ECO:0000269|PubMed:8299151}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q02218};
CC   -!- ACTIVITY REGULATION: Catabolite repressed.
CC   -!- SUBUNIT: Component of the 2-oxoglutarate dehydrogenase complex (OGDC),
CC       also called alpha-ketoglutarate dehydrogenase (KGDH) complex. The
CC       complex is composed of the catalytic subunits OGDH (2-oxoglutarate
CC       dehydrogenase KGD1; also called E1 subunit), DLST (dihydrolipoamide
CC       succinyltransferase KGD2; also called E2 subunit) and DLD
CC       (dihydrolipoamide dehydrogenase LPD1; also called E3 subunit), and the
CC       assembly factor KGD4. {ECO:0000269|PubMed:2072900,
CC       ECO:0000269|PubMed:25165143}.
CC   -!- INTERACTION:
CC       P20967; P19262: KGD2; NbExp=7; IntAct=EBI-12459, EBI-12464;
CC       P20967; P19955: YMR31; NbExp=6; IntAct=EBI-12459, EBI-16295;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25165143}.
CC       Mitochondrion matrix. Mitochondrion matrix, 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 family.
CC       {ECO:0000305}.
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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   AlphaFoldDB; P20967; -.
DR   SMR; P20967; -.
DR   BioGRID; 34866; 187.
DR   ComplexPortal; CPX-1293; Mitochondrial 2-oxoglutarate dehydrogenase complex.
DR   DIP; DIP-365N; -.
DR   FunCoup; P20967; 771.
DR   IntAct; P20967; 71.
DR   STRING; 4932.YIL125W; -.
DR   iPTMnet; P20967; -.
DR   PaxDb; 4932-YIL125W; -.
DR   PeptideAtlas; P20967; -.
DR   EnsemblFungi; YIL125W_mRNA; YIL125W; YIL125W.
DR   GeneID; 854681; -.
DR   KEGG; sce:YIL125W; -.
DR   AGR; SGD:S000001387; -.
DR   SGD; S000001387; KGD1.
DR   VEuPathDB; FungiDB:YIL125W; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; P20967; -.
DR   OMA; AAANKMC; -.
DR   OrthoDB; 413077at2759; -.
DR   BioCyc; YEAST:YIL125W-MONOMER; -.
DR   Reactome; R-SCE-6783984; Glycine degradation.
DR   Reactome; R-SCE-9837999; Mitochondrial protein degradation.
DR   Reactome; R-SCE-9853506; OGDH complex synthesizes succinyl-CoA from 2-OG.
DR   BioGRID-ORCS; 854681; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P20967; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P20967; protein.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IDA:SGD.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:ComplexPortal.
DR   GO; GO:0045333; P:cellular respiration; TAS:SGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   FunFam; 1.10.287.1150:FF:000002; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   FunFam; 3.40.50.12470:FF:000003; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   FunFam; 3.40.50.970:FF:000002; 2-oxoglutarate dehydrogenase, E1 component; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Mitochondrion; Mitochondrion nucleoid;
KW   Oxidoreductase; Reference proteome; Thiamine pyrophosphate;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..1014
FT                   /note="2-oxoglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000020436"
FT   BINDING         306
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:Q02218"
FT   BINDING         406
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q02218"
FT   BINDING         406
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:Q02218"
FT   BINDING         439
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q02218"
FT   BINDING         439
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:Q02218"
FT   BINDING         441
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q02218"
FT   BINDING         441
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:Q02218"
FT   CONFLICT        325..327
FT                   /note="SEF -> LNL (in Ref. 1; AAA34721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        513
FT                   /note="Q -> R (in Ref. 1; AAA34721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="A -> T (in Ref. 1; AAA34721)"
FT                   /evidence="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
//