ID   ODO1_CAEBR              Reviewed;        1027 AA.
AC   Q623T0; A8WQY9;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
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-1; ORFNames=CBG01737;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(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) (By similarity).
CC       {ECO:0000250|UniProtKB:Q02218}.
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         Evidence={ECO:0000250|UniProtKB:Q02218};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:Q02218};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE601298; CAP22897.1; -; Genomic_DNA.
DR   RefSeq; XP_002634170.1; XM_002634124.1.
DR   AlphaFoldDB; Q623T0; -.
DR   SMR; Q623T0; -.
DR   STRING; 6238.Q623T0; -.
DR   EnsemblMetazoa; CBG01737.1; CBG01737.1; WBGene00024926.
DR   GeneID; 8576165; -.
DR   KEGG; cbr:CBG_01737; -.
DR   CTD; 8576165; -.
DR   WormBase; CBG01737; CBP00459; WBGene00024926; Cbr-ogdh-1.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_1_1; -.
DR   InParanoid; Q623T0; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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   Glycolysis; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..1027
FT                   /note="2-oxoglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000234099"
SQ   SEQUENCE   1027 AA;  115481 MW;  99584397C5540D7B CRC64;
     MHRASLICRL ASPSRINSIR SASSYGNNTI SATPLVQQRK QSVAASVKHE PFLNGSSSVY
     IEQMYETWLE NPSSVHTSWD AYFRNVEAGA GPGQAFQAPP SVAYAGSMGV PSAPITSAAP
     ATRLDTNASV QSISDHLKIQ LLIRSYQTRG HNIADLDPLG INSADLDDTI PPELELSFYG
     LGERDLDREF LLPPTTFISE KKSLTLREIL QRLKEIYCTS TGVEYMHLNN LEQQDWIRRR
     FEAPRVTELS HDQKKVLFKR LIRSTKFEEF LAKKWPSEKR FGLEGCEVLI PAIKQVIDSS
     STLGVDSFVI GMPHRGRLNV LANVCRQPLA TILSQFSTLE PADEGSGDVK YHLGVCIERL
     NRQSQKNVKI AVVANPSHLE AVDPVVMGKV RAEAFYAGDE KCDRTMAILL HGDAAFAGQG
     VVLETFNLDD LPSYTTHGAI HIVVNNQIGF TTDPRSSRSS PYCTDVGRVV GCPIFHVNVD
     DPEAVMHVCN VAADWRKTFK KDVIVDLVCY RRHGHNELDE PMFTQPLMYQ RIKQTKTALE
     KYQEKILNEG VANEQYVKEE LTKYGAILED AYENAQKVTY VRNRDWLDSP WDDFFKKRDP
     LKLPSTGIEQ ENIEHIIGKF GSYPEGFNLH RGLERTLKGR QQMLKDNSLD WACGEALAFG
     SLLKEGIHVR LSGQDVERGT FSHRHHVLHD QKVDQKIYNP LNDLADPQGE YTVCNSSLSE
     YAVLGFELGY SMVDPNSLVI WEAQFGDFSN TAQCIIDQFV SSGQSKWIRQ SGLVMLLPHG
     YEGMGPEHSS ARPERFLQMC NEDDEIDLDK IAFGGTFEAQ QLHDTNWIVA NCTTPANIYH
     LLRRQVTMPF RKPAVVFSPK SLLRHPMARS PVEDFQSGSN FQRIIPETGA PSQNPPNVQR
     LVFCTGKVYY DMVAARKHVG KENDVALVRV EQLSPFPYDL VQQECRKYQG AEIIWAQEEH
     KNMGAWSFVQ PRINSLLSID GRATKYAGRL PSSSPATGNK YTHMQEQKEM MSKVFGVPKS
     KLEGFKA
//