ID   F2Q5D7_TRIEC            Unreviewed;      1050 AA.
AC   F2Q5D7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=TEQG_08331 {ECO:0000313|EMBL:EGE09355.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995802; EGE09355.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2Q5D7; -.
DR   VEuPathDB; FungiDB:TEQG_08331; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   Proteomes; UP000009169; 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; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          674..884
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1050 AA;  118607 MW;  55D03BE0A0C256D6 CRC64;
     MFRTTRAMTL KASGASSLLR QSYTRSICSG ARSNLQLTAR KPLGVVCARK AWEQTRGYAV
     ATGETSKGVD PNDSFLQGNT ANYIDEMYMA WKEDPQSVHV SWRTYFHNME EGKMPISQAF
     QPPPTIVPTP TGGVPQHMPG NAAGTNVSNH LKVQLLVRAY QARGHHKAKI DPLGIRGEAD
     SFGYSKPKEL ELSHYGFTEK DLDEEFALGP GILPRFETET RKKMTLREII DACEKIYCGS
     FGVEYIHIPD RVPCDWIRDR IEIPQPYKYS VDEKRRILDR LIWSSSFEAF LATKFPNDKR
     FGLEGCETLV PGMKALIDRS VDYGVKDIVI GMPHRGRLNV LSNVVRKPNE SIFSEFSGSA
     EPSDEGSGDV KYHLGMNFER PTPSGKRVQL SLVANPSHLE AEDPVVLGKT RSIQHYNNDE
     KEFNTAMGVL LHGDAAFAAQ GIVYETMGFH SLPAYSTGGT IHIVVNNQIG FTTDPRFARS
     TPYCSDIAKA IDAPVFHVNG DDVEALNHVC QLAADWRAQF KSDVVIDIVC YRKQGHNETD
     QPAFTQPLMY KRIASQQSQI DKYVEKLLKE KTFTKEDIDE HKKWVWGMLN DSFERSKDYT
     PTSREWLTSA WNGFKTPKEL ATEVLGHPPT GVEAETLQMI GAKLGSIPEN FTPHRNLKRI
     LANREKSIKE GQNIDWSTAE ALAFGTLCKE GHHVRVSGQD VERGTFSQRH AVLHDQENES
     TYTALQHISP DQGSFVISNS SLSEYGALGF EYGYSLTSPN ALVMWEAQFG DFANNAQCII
     DQFIASGESK WVQRSGLVMS LPHGYDGQGP EHSSGRLERY LQLCNEDPRV YPAADRIDRQ
     HQDCNMQIAY MTSPANLFHI LRRQINRQFR KPLIIFFSKS LLRHPSCRSS IEEFTGDSHF
     RWIIPDDQHG KQIDEPEKID RVIMCSGQVW AALTKHREAN GIRNTAITRI EQMHPFPWQQ
     LKENLDSYPN AKDIVFCQEE PLNAGSWSYM QPRIETLLNE TVHHNRRHVL YAGRNPSASV
     ATGLKSSHIK EEQDLLHDAF TVHQEKLKGE
//