ID   DHTK1_CAEEL             Reviewed;         911 AA.
AC   Q23629;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 4.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial;
DE            EC=1.2.4.2;
DE   Flags: Precursor;
GN   Name=ogdh-2 {ECO:0000312|WormBase:ZK836.2a};
GN   ORFNames=ZK836.2 {ECO:0000312|WormBase:ZK836.2a};
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).
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; Z78201; CAB01590.2; -; Genomic_DNA.
DR   EMBL; Z78019; CAB01590.2; JOINED; Genomic_DNA.
DR   PIR; T28034; T28034.
DR   RefSeq; NP_001256410.1; NM_001269481.1.
DR   AlphaFoldDB; Q23629; -.
DR   SMR; Q23629; -.
DR   STRING; 6239.ZK836.2a; -.
DR   EPD; Q23629; -.
DR   PaxDb; Q23629; -.
DR   PeptideAtlas; Q23629; -.
DR   EnsemblMetazoa; ZK836.2a.1; ZK836.2a.1; WBGene00014098.
DR   GeneID; 179674; -.
DR   KEGG; cel:CELE_ZK836.2; -.
DR   UCSC; ZK836.2.1; c. elegans.
DR   CTD; 179674; -.
DR   WormBase; ZK836.2a; CE35706; WBGene00014098; ogdh-2.
DR   eggNOG; KOG0451; Eukaryota.
DR   GeneTree; ENSGT00950000183125; -.
DR   InParanoid; Q23629; -.
DR   OMA; GMAIDNP; -.
DR   OrthoDB; 134699at2759; -.
DR   PhylomeDB; Q23629; -.
DR   Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:Q23629; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00014098; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q23629; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR   Gene3D; 3.40.50.11610; -; 1.
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; 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           ?..911
FT                   /note="Probable 2-oxoglutarate dehydrogenase E1 component
FT                   DHKTD1 homolog, mitochondrial"
FT                   /id="PRO_0000307942"
SQ   SEQUENCE   911 AA;  102731 MW;  D935381071E95A85 CRC64;
     MMLRSAGGSI RRAITQRQNQ HRFYRPGHGV FGHLPDPPKR VFENQGGLTP ENAQRVHLIN
     AFRRYGYLEA DLDPLGLRKV ESVAELDPAI YGLSLDENVK GNFSLHDLAE QLRHIYCGPT
     AIEFMHINNW EERQWISQNF ENCIAEELRK EELLRIGDLM LKCENFDKFL STKFPTLKRY
     GAEGAESMFA FFSELFEGAA EKQVEEIIIG IAHRGRLNLL TQLMDFPPVH MFRKIKGRAE
     FPESADAAGD VLSHLVSSFD YKGSEGNVHV TMLPNPSHLE AVNPVAMGKA RARAWSMNKG
     DYSPDERSAR AGDSVLNVLV HGDGAFTGQG VVWESIALSQ APHFRLGGTV HLVTNNQIAF
     TAESSVGRSS THCTDIAKAF EYPVIHVNGD HPEEVVKATR LALAYRERFR KDVFINLVCF
     RRWGHNELDD PTFTSPVMYK EVEARESVPR LFLDRLVEEG FTTEEAVKEQ LQKHTEQLNN
     ELKKVDSTVP IDISHRGRWE GFKQAPKAIE SWDTGVATDL LRFIGAGSVK VPEDFDTHKH
     LYKMHIDSRM QKMQTGEGID WATAEAMAFG SILLEGNDVR ISGQDVGRGT FCHRHAMMVD
     QSTDHIHIPL NELVEEQKNQ LEVANNLLSE EAILGFEWGF SSENPRRLCI WEAQFGDFFN
     GAQIIIDTFL ASAESKWLTS SGLTMLLPHG FDGAGPEHSS CRMERFLQLC DSREDQTPVD
     GENVNMRVAN PTTSAQYFHL LRRQVVPNYR KPLIVVGPKI LLRHPKAAST INEFGPGTTY
     QNVISEEHAT SSQKIKKVIF VSGKHWINVE KARDERGLKD SVAIVRVEML CPFPVVDLQA
     VLKKYPGAQD FVWSQEEPRN AGAWSFVRPR FENALGVRLK FAGRPELAWT ATAIGEHHTK
     EAEEVINQTF A