ID   ODO1_DICDI              Reviewed;        1013 AA.
AC   Q54JE4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=ogdh; ORFNames=DDB_G0288127;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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) (By similarity). {ECO:0000250}.
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         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Catabolite repressed. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000109; EAL63408.1; -; Genomic_DNA.
DR   RefSeq; XP_636906.1; XM_631814.1.
DR   AlphaFoldDB; Q54JE4; -.
DR   SMR; Q54JE4; -.
DR   STRING; 44689.DDB0234117; -.
DR   PaxDb; Q54JE4; -.
DR   PRIDE; Q54JE4; -.
DR   EnsemblProtists; EAL63408; EAL63408; DDB_G0288127.
DR   GeneID; 8626461; -.
DR   KEGG; ddi:DDB_G0288127; -.
DR   dictyBase; DDB_G0288127; ogdh.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; Q54JE4; -.
DR   OMA; RDSYCRT; -.
DR   PhylomeDB; Q54JE4; -.
DR   Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-DDI-71064; Lysine catabolism.
DR   Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR   PRO; PR:Q54JE4; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; ISS:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Glycolysis; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..1013
FT                   /note="2-oxoglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000328590"
SQ   SEQUENCE   1013 AA;  114068 MW;  CE908E70E8394632 CRC64;
     MFTLKQVINK SIQTSMKNGV MSSAVKRSFS TVGGINQPKS RKELSESFLD GTSSTYVEDM
     FANWVKDPKS VHPSWASFFE SSERGVPAGE AFMSPPTLGS SVATKATPST YTSSGSPKQV
     SDSMRLLLLV RAYQVRGHAL ANLDPLGLEV KEEPAEFNPA KYGFTEADMD RPIFVGEGFI
     SGFLTNKQPE TTLRQVLKRL KETYCGDIGI EYMHIQDREM CDWIRDKFET SQPVEIPDKE
     KIKILERLSW ADQFEGFLGL KYRATRRFGL DGCESLIPGM KAMIDTATED GVESIVLGMP
     HRGRLNVLAN VVRKPLPAIF NEFNGGVISI EGEYSATGDV KYHLGTSYDR VTSSGKKVHL
     SLVANPSHLE AVNPLVEGKV RAKQHYSKDT EQKKSMAVQL HGDASVAGQG VVYETLHLSN
     LDNYSTGGTV HIVVNNQIGF TTNPKYSRSS KYCTDVAKTI DIPVFHVNGD NVEAVVKVCK
     IAAEWRQKFK RDVFVDIVCY RKHGHNETDQ PKFTQPIMYD KIGKQQPIIE KYSNKLIAEK
     VITQEQYLQM KNIIHESYEK GYQDGMKHVP NAEDWLESRW EGFKSPIELG NPGRTGIDQD
     LLQKIGKVLY TEPSGFEVHS TIKRLLKEKK DMFDKGTGFD WATAEALAFG SLLLDGNHVR
     LSGQDVERGT FSHRHAVWHD QKTDQTYAPL TKLATALGKK DAAEFVASNS SLSEFAVLGF
     ELGYSLENPD ALILWEAQFG DFSNGAQVII DQFISSGEQK WMRQSGLTML LPHGYDGAGP
     EHSSCRIERY LQLCDSDPNK IPPKEEAERK QSQHCNMQVL NCSTPVNYFH ALRRQVHRDF
     RKPLVIATPK YLLRYEKSFS TAKEFSNDSF TRLYPEAFPD QINKPEKINR IVFCTGQVYY
     NLIASRESNN IKDVAIIRVE QLHPFPFDLV AEQLQHYPNA KAIWCQEEPM NMGYWNYIYP
     YFISTFKHIN RPADITYTGR PSSASPAVAS HTLHKLQLEN FLSNALTGQV GSK