ODO1_CAEBR
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 03-AUG-2022, entry version 93.
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=(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 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; HE601298; CAP22897.1; -; Genomic_DNA.
DR RefSeq; XP_002634170.1; XM_002634124.1.
DR AlphaFoldDB; Q623T0; -.
DR SMR; Q623T0; -.
DR STRING; 6238.CBG01737; -.
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; 134699at2759; -.
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 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..?
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
