ID   A1CI95_ASPCL            Unreviewed;      1056 AA.
AC   A1CI95;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=ACLA_050720 {ECO:0000313|EMBL:EAW10600.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10600.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10600.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027054; EAW10600.1; -; Genomic_DNA.
DR   RefSeq; XP_001272026.1; XM_001272025.1.
DR   AlphaFoldDB; A1CI95; -.
DR   STRING; 344612.A1CI95; -.
DR   EnsemblFungi; EAW10600; EAW10600; ACLA_050720.
DR   GeneID; 4703814; -.
DR   KEGG; act:ACLA_050720; -.
DR   VEuPathDB; FungiDB:ACLA_050720; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IEA:EnsemblFungi.
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:0006103; P:2-oxoglutarate metabolic process; IEA:EnsemblFungi.
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: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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          680..890
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1056 AA;  118769 MW;  16681CBF24528FFF CRC64;
     MFRNTAVKAS SGMLRGSTSS TCRRSISLTA TARTTASHSS KFGLTSRRPL AVVDRMCNGK
     RFYAAGTSVG VDPNDNFLSG NTANYIDEMY LAWKKDPSSV HISWQTYFKN MEDGNMPISQ
     AFQPPPTLVP TPTLGVPQDM PGAGLGLSAG TDVTSHLKVQ LLVRAYQARG HHKAKIDPLG
     IRGEAEAFGY NKPKELELDH YGFTERDLDQ EFTLGPGILP RFATDSRKKM TLREIVATCE
     KIYCGSYGVE YIHIPDRKPC DWIRDRFEIP EPYKYSVDDK RRILDRLIWS HSFESFLATK
     FPNDKRFGLE GCETLVPGMK ALIDRSVEHG IKDIVIGMPH RGRLNVLSNV VRKPNESIFS
     EFSGSAEPSD EGSGDVKYHL GMNFERPTPS GKRVQLSLVA NPSHLEAEDP VVLGKARSIQ
     HYNNDETEFK TAMGVLLHGD AAFAAQGVVY ETMGFHSLPA YSTGGTIHLI VNNQIGFTTD
     PRFARSTPYC SDIAKSIDAP VFHVNADDVE ALNYVCQVAA DWRAEFKRDV VIDIVCYRKQ
     GHNETDQPSF TQPLMYKRIA EQKAQLDKYV EKLISEGTFT KEDIDEHKKW VWGMLNDSFD
     RSKDYQPTSK EWLTSAWNGF KTPKELATEV LPHLPTAAEP ALLSRIAEKI SGPPEGFTVH
     RNLKRILANR RKTVEEGTGI DWPTAEALAF GTLVDEGYHV RVSGQDVERG TFSQRHAVLH
     DQENEGTYTP LQDISDKQGS FVISNSSLSE FGALGFEYGY SLTSPNALVM WEAQFGDFAN
     NAQCIIDQFI ASGESKWLQR SGLVISLPHG YDGQGPEHSS GRMERWLQLC NEEPRVFPSQ
     DKLDRQHQDC NMQIACMTSP ANLFHILRRQ IHRQFRKPLV IFFSKSLLRH PIARSDLEEF
     TGESHFQWII RDPAHGSAID EPEKIERVIL CSGQVYAALV KHREANNIRN TAITRVEQLH
     PFPWAQLKEN LDSYPNAKDI VWAQEEPLNA GAWSFAQPRL ETLLNATEHH NRRHVLYAGR
     APSASVATGL KSVHIKEEQE FLEDAFTLHQ ERLKGE
//