ID   ODO1_SCHPO              Reviewed;        1009 AA.
AC   O74378;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 133.
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; ORFNames=SPBC3H7.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, 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; CU329671; CAA20299.1; -; Genomic_DNA.
DR   PIR; T40412; T40412.
DR   RefSeq; NP_595772.1; NM_001021673.2.
DR   AlphaFoldDB; O74378; -.
DR   SMR; O74378; -.
DR   BioGRID; 277507; 4.
DR   STRING; 284812.O74378; -.
DR   iPTMnet; O74378; -.
DR   MaxQB; O74378; -.
DR   PaxDb; 4896-SPBC3H7-03c-1; -.
DR   EnsemblFungi; SPBC3H7.03c.1; SPBC3H7.03c.1:pep; SPBC3H7.03c.
DR   GeneID; 2540991; -.
DR   KEGG; spo:SPBC3H7.03c; -.
DR   PomBase; SPBC3H7.03c; kgd1.
DR   VEuPathDB; FungiDB:SPBC3H7.03c; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_1_1; -.
DR   InParanoid; O74378; -.
DR   OMA; RDSYCRT; -.
DR   PhylomeDB; O74378; -.
DR   Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-SPO-71064; Lysine catabolism.
DR   Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR   PRO; PR:O74378; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:PomBase.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
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:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd02016; TPP_E1_OGDC_like; 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; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 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   3: Inferred from homology;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Thiamine pyrophosphate;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..1009
FT                   /note="2-oxoglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000315629"
SQ   SEQUENCE   1009 AA;  114164 MW;  4CB2598CE2B5E6AB CRC64;
     MLRFIPSSAK ARALRRSAVT AYRLNRLTCL SSLQQNRTFA TQPTDDFLTG GAADYVDEMY
     DAWKKDPNSV HASWQAYFKN VQERGVSPSK AFQAPPLLDY ADSYTALDSS LINGNNYADI
     DVGIYMKVQL LVRAYQSRGH HLAKLDPLGI NVNHNRPSEL TLEHYGFTES DLNRTIHLGP
     GILPNFREAG RKTMTLREIV ETCEKIYCGS FAVEFTHISS RKRSNWILSH LETPTPFRYS
     HDQKIMIFDR LSWADSFERF LFTKFPNDKR FGLEGCEAMV PGMKALIDRS VDEGISNIVI
     GMAHRGRLNL LHNIVRKPAQ AIFSEFRGTQ DPDDEGSGDV KYHLGMNYQR PTPSGKRVSL
     SLVANPSHLE AEDPVVLGKV RAIQHYTSDE ASHEQSMGIL IHGDAAFAAQ GVVYETFGLH
     ALPGYSTGGT VHIVINNQIG FTTDPRFARS TPYCTDIAKS MEAPIFHVNG DDVEAVTFIC
     QLAADWRKAF KTDVVVDIVC YRRHGHNETD QPSFTQPRMY KAIAKHPPTF KIYTQQLLQE
     KTVSKAEVDA QEKRVWDILE SSFESSKNYK SDHREWLSNP WVGFASPKDL MTKILPSYPT
     GVNIDTLKQI GKALYTLPEG FDAHRNLKRI LNNRNKSISS GEGIDMPTAE ALAFGTLLEE
     GHHVRVSGQD VERGTFSQRH AVLHDQSSEN VYIPLNHLSP NQASFVIRNS SLSEYGVLGF
     EYGYSLSSPN ALVVWEAQFG DFANNAQCII DQFIAAGETK WLQRTGIVLS LPHGYDGQGP
     EHSSARMERY LQLCNEDPRE FPSEEKLQRQ HQDCNIQAIY VTKPSQYFHA LRRNIHRQFR
     KPLVIFFSKS LLRHPAARST IDEFDEKHGF KLILEEEEHG KSILPPEKIE KLIICSGQVW
     VALSKAREEN KIDNIAITRV EQLHPFGWKQ MAANISQYPN LKEIIWCQEE PLNAGAWTYM
     EPRIYTILKH LGRDLPVRYA GRPPSASVAA GNKQQHLAEQ EQFLNDALL
//