ID   Q6GPC8_XENLA            Unreviewed;      1018 AA.
AC   Q6GPC8;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040429};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041946};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
DE   AltName: Full=Thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00042799};
GN   Name=ogdh.L {ECO:0000313|RefSeq:NP_001085695.1,
GN   ECO:0000313|Xenbase:XB-GENE-17331499};
GN   Synonyms=akgdh {ECO:0000313|RefSeq:NP_001085695.1}, e1k
GN   {ECO:0000313|RefSeq:NP_001085695.1}, MGC80496
GN   {ECO:0000313|EMBL:AAH73213.1}, ogdc
GN   {ECO:0000313|RefSeq:NP_001085695.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH73213.1};
RN   [1] {ECO:0000313|RefSeq:NP_001085695.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH73213.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH73213.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001085695.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00043712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC         Evidence={ECO:0000256|ARBA:ARBA00043712};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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; BC073213; AAH73213.1; -; mRNA.
DR   RefSeq; NP_001085695.1; NM_001092226.1.
DR   DNASU; 444121; -.
DR   GeneID; 444121; -.
DR   KEGG; xla:444121; -.
DR   AGR; Xenbase:XB-GENE-17331499; -.
DR   CTD; 444121; -.
DR   Xenbase; XB-GENE-17331499; ogdh.L.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 444121; Expressed in intestine and 19 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF7; 2-OXOGLUTARATE DEHYDROGENASE COMPLEX COMPONENT E1; 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   2: Evidence at transcript level;
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          647..860
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1018 AA;  115016 MW;  2A3BCD093CD5FF01 CRC64;
     MFNLRTCASK LRPLTASQTV RSLTHKKPAA PRTFQQFRCL STPVAAEPFL SGTSSNYVEE
     MYYAWLENPK SVHKSWDIFF RNANAGASPG AAYQSPPPLG SSLSTLSQAQ SLVQARPNID
     KLVGDHLAVQ SLIRAYQVRG HHIAKLDPLG ISSVNFDGAP VIVGSPNVGF YGLEESDLDK
     VFHLPTTTFI GSNEMALPLR EIIRRLESAY CQHIGVEFMF INDLEQCQWI RQKFETPGIM
     QFNSEEKRTL LARLVRSTRF EEFLHRKWSS EKRFGLEGCE VLIPALKTII DKSSENGVDY
     VIMGMPHRGR LNVLANVIRK ELEQIFCQFD SKLEATDEGS GDVKYHLGMY HRRINRVTDR
     NITLSLMANP SHLEAADPVV QGKTKAEQFY CGDTEGKKVM SILLHGDAAF AGQGIVYETF
     HLSDLPSYTT HGTVHVVVNN QIGFTTDPRM ARSSPYPTDV ARVVNAPIFH VNADDPEAVM
     YVCNVAAEWR STFHKDVVVD LVCYRRNGHN EMDEPMFTQP LMYKQIRKQK TVLQKYAETL
     VSQGVVNQSE YEEEISKYDK ICEEAFARSK DEKILHIKHW LDSPWPGFFT LDGQPRSMTC
     PSTGLSEEEL THIGNVASSV PVEDFTIHGG LSRILKGRGE MVKNRTVDWA LAEYMSLGSL
     LKEGIHIRLS GQDVERGTFS HRHHVLHDQN VDKRTCIPMN HLWPNQAPYT VCNSSLSEYG
     VLGFELGFAM ASPNALVLWE AQFGDFHNTA QCIIDQFVCP GQAKWVRQNG IVLLLPHGME
     GMGPEHSSAR PERFLQMCND DSDVWPKASE DFAVRQLYDC NWIVVNCSTP ANFFHVIRRQ
     ILLPFRKPLI VFTPKSLLRH PEARSSFDDM LAGTHFERII PDAGPASQNP EGVKRLIFCA
     GKVYYDLTKE RSGRGMEGDV AITRVEQLSP FPFDLVEKEV QKYPNADLVW CQEEHKNQGY
     YDYVKPRLRT TIHRAKPVWY AGRDPAAAPA TGNKKTHLTE LKRLLDTSFN LDSFKGHS
//