ID   ODO1_CAEEL              Reviewed;        1029 AA.
AC   O61199;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   27-MAR-2024, entry version 154.
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=T22B11.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 126-146; 297-317; 320-328; 372-391; 504-514; 548-565;
RP   622-633; 673-680; 910-918; 975-984 AND 992-1002, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (MAR-2006) to UniProtKB.
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}.
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DR   EMBL; FO081256; CCD70240.1; -; Genomic_DNA.
DR   PIR; T15098; T15098.
DR   RefSeq; NP_500617.1; NM_068216.4.
DR   AlphaFoldDB; O61199; -.
DR   SMR; O61199; -.
DR   BioGRID; 42364; 6.
DR   IntAct; O61199; 1.
DR   STRING; 6239.T22B11.5a.1; -.
DR   iPTMnet; O61199; -.
DR   EPD; O61199; -.
DR   PaxDb; 6239-T22B11-5a; -.
DR   PeptideAtlas; O61199; -.
DR   EnsemblMetazoa; T22B11.5a.1; T22B11.5a.1; WBGene00020679.
DR   GeneID; 177235; -.
DR   KEGG; cel:CELE_T22B11.5; -.
DR   UCSC; T22B11.5; c. elegans.
DR   AGR; WB:WBGene00020679; -.
DR   WormBase; T22B11.5a; CE28486; WBGene00020679; ogdh-1.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_1_1; -.
DR   InParanoid; O61199; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   PhylomeDB; O61199; -.
DR   Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-CEL-71064; Lysine catabolism.
DR   Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR   PRO; PR:O61199; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00020679; Expressed in larva and 4 other cell types or tissues.
DR   ExpressionAtlas; O61199; baseline and differential.
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; HDA:WormBase.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..1029
FT                   /note="2-oxoglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000234100"
SQ   SEQUENCE   1029 AA;  115661 MW;  71ECB0F4236135F4 CRC64;
     MHRASLICRL ASPSRINAIR NASSGKSHIS ASTLVQHRNQ SVAAAVKHEP FLNGSSSIYI
     EQMYEAWLQD PSSVHTSWDA YFRNVEAGAG PGQAFQAPPA TAYAGALGVS PAAAQVTTSS
     APATRLDTNA SVQSISDHLK IQLLIRSYQT RGHNIADLDP LGINSADLDD TIPPELELSF
     YGLGERDLDR EFLLPPTTFI SEKKSLTLRE ILQRLKDIYC TSTGVEYMHL NNLEQQDWIR
     RRFEAPRVTE LSHDQKKVLF KRLIRSTKFE EFLAKKWPSE KRFGLEGCEV LIPAMKQVID
     SSSTLGVDSF VIGMPHRGRL NVLANVCRQP LATILSQFST LEPADEGSGD VKYHLGVCIE
     RLNRQSQKNV KIAVVANPSH LEAVDPVVMG KVRAEAFYAG DEKCDRTMAI LLHGDAAFAG
     QGVVLETFNL DDLPSYTTHG AIHIVVNNQI GFTTDPRSSR SSPYCTDVGR VVGCPIFHVN
     VDDPEAVMHV CNVAADWRKT FKKDVIVDLV CYRRHGHNEL DEPMFTQPLM YQRIKQTKTA
     LEKYQEKILN EGVANEQYVK EELTKYGSIL EDAYENAQKV TYVRNRDWLD SPWDDFFKKR
     DPLKLPSTGI EQENIEQIIG KFSQYPEGFN LHRGLERTLK GRQQMLKDNS LDWACGEALA
     FGSLLKEGIH VRLSGQDVQR GTFSHRHHVL HDQKVDQKIY NPLNDLSEGQ GEYTVCNSSL
     SEYAVLGFEL GYSMVDPNSL VIWEAQFGDF SNTAQCIIDQ FISSGQSKWI RQSGLVMLLP
     HGYEGMGPEH SSARPERFLQ MCNEDDEIDL EKIAFEGTFE AQQLHDTNWI VANCTTPANI
     YHLLRRQVTM PFRKPAVVFS PKSLLRHPMA RSPVEDFQSG SNFQRVIPET GAPSQNPPDV
     KRVVFCTGKV YYDMVAARKH VGKENDVALV RVEQLSPFPY DLVQQECRKY QGAEILWAQE
     EHKNMGAWSF VQPRINSLLS IDGRATKYAG RLPSSSPATG NKFTHMQEQK EMMSKVFGVP
     KSKLEGFKA
//