ID   A0A137QBL6_9AGAR        Unreviewed;       830 AA.
AC   A0A137QBL6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN   ORFNames=AN958_12280 {ECO:0000313|EMBL:KXN84599.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN84599.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN84599.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN84599.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|ARBA:ARBA00037426}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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; KQ962581; KXN84599.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QBL6; -.
DR   STRING; 1714833.A0A137QBL6; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
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; 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; 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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          637..830
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   830 AA;  93049 MW;  258F0E8A4F81D499 CRC64;
     MLSRRVVGRL TPLVRAPRSL RPLPVPIRRE YALARGPSSN DPFANGTNAY YADEMYRLWK
     QDPKTVHPSW DVYFSGLDKG LPSYQAFQPP PTTHLPPPAD GAPALHAGGG AELDDHLKVQ
     LLVRAYQVRG HHMAELDPLG ILDTDLADVR PPELELSRYG FTERDLEKDI TLGPGILPHF
     ATEENRAMKL RDIIKVLKRI YCGAVGIQYV HIPDKEQCDW IRERVETPKP WNYTVEEKRM
     ILDRLIWSES FEKFIASKYP NEKRFGLEGC ESLIPGMKAL IDRSVDNGVK HITIGMPHRG
     RLNVLANVIR KPIEAILNEF SGDEDDNWPA GDVKYHLGAN YVRPTPSGKK VSLSLVANPS
     HLEAADPVVL GKTRAIQHFE NDESAHTTAM GVLLHGDAAF AGQGVVYETM GLHNLPEYGT
     GGTIHLLVNN QIGFTTDPRF SRSTPYPSDI AKSIDAPIFH VNGDNVEAVN FVCQLAADYR
     AKFKKDVVID IVCYRRYGHN ETDQPSFTQP RMYEAIKNQP TPLTKYTKFL VGRGTFTEKD
     IEEHKKWVWG MLDKATNAAK DYVPTSKEWL SAAWTGFPSP KQLAEQTLPT RSTGSDVDTL
     QRIGKAISSY PQGFMAHRNL ARILSARGKT VEEGKNIDWS TAEALAFGAL ALEKIHVRLS
     GQDVERGTFS QRHAVIHDQK NEQQYIPLND LGSNQARFVV CNSSLSEYGS LGFELGYSLV
     SPDSLTIWEA QFGDFANNAQ CIIDQFIAAG ERKWLQRTGL VVNLPHGYDG QGPEHSSGRM
     ERFLQLCDDH PHVYPSPEKI ERQHQDCNMQ VVYPTCVHLH VLSLVPLLTF
//