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 03-AUG-2022, entry version 195.
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; 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;
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 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 [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 of
RT protein components in the mitochondrial nucleoid fraction of the yeast
RT 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., 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 [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., 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).
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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC -!- ACTIVITY REGULATION: Catabolite repressed.
CC -!- INTERACTION:
CC P20967; P19262: KGD2; NbExp=6; 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 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; 135.
DR ComplexPortal; CPX-1293; Mitochondrial 2-oxoglutarate dehydrogenase complex.
DR DIP; DIP-365N; -.
DR IntAct; P20967; 47.
DR MINT; P20967; -.
DR STRING; 4932.YIL125W; -.
DR iPTMnet; P20967; -.
DR MaxQB; P20967; -.
DR PaxDb; P20967; -.
DR PRIDE; P20967; -.
DR EnsemblFungi; YIL125W_mRNA; YIL125W; YIL125W.
DR GeneID; 854681; -.
DR KEGG; sce:YIL125W; -.
DR SGD; S000001387; KGD1.
DR VEuPathDB; FungiDB:YIL125W; -.
DR eggNOG; KOG0450; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; P20967; -.
DR OMA; RDSYCRT; -.
DR BioCyc; YEAST:YIL125W-MON; -.
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 RNAct; P20967; protein.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IPI:ComplexPortal.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
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:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.11610; -; 1.
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; IPR042179; KGD_C_sf.
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 Mitochondrion; Mitochondrion nucleoid; Oxidoreductase; Reference proteome;
KW Thiamine pyrophosphate; 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 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
