ID   A6QVX8_AJECN            Unreviewed;      1054 AA.
AC   A6QVX8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=HCAG_01535 {ECO:0000313|EMBL:EDN03670.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN03670.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476655; EDN03670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6QVX8; -.
DR   STRING; 339724.A6QVX8; -.
DR   VEuPathDB; FungiDB:HCAG_01535; -.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000009297; 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   Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          677..887
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1054 AA;  118999 MW;  8691E502BF9FD1D6 CRC64;
     MLQTATVKAF SNAAFLRRSS SAYNIRTFSV ISSKPANTVS RSSSKLHLAL RRPLAVLSRQ
     QVWNQKRYYA VAAEESSKGV DPSDSFLQGN TANYIDEMYM AWKKDPTSVH VSWQTYFRNM
     EDGNMPISQA FQPPPTLVPI PTGGVPQHMP HAGTASVAGT EVSNHLKVQL LVRAYQARGH
     HKAKIDPLGI RGEAEAFGYN KPRELELDHY GFTESDLDQE FALGPGILPR FETETRKKMT
     LREIIAACEK IYCGSYGIEY IHIPDRGPCD WIRDRVEIPT PYKYSIDEKR RILDRLIWSS
     SFESFLATKF PNDKRFGLEG CETLVPGMKA LIDRSVDYGI KDIVIGMPHR GRLNVLSNVV
     RKPNESIFSE FSGTVEPSDE GSGDVKYHLG MNFERPTPSG KRVQLSLVAN PSHLEAEDPV
     VLGKTRAIQH YNNDEKEFNT AMGVLLHGDA AFAAQGVVYE TMGFHSLPAY STGGTIHIIV
     NNQIGFTTDP RFARSTPYCS DIAKAIDAPV FHVNGDDVEA LNYVCQMAAD WRATFKRDVV
     IDIVCYRKQG HNETDQPSFT QPLMYKRIAE QTNQLDNKAD IEEHKKWVWG MLNDSFDRSK
     DYQPSSKEWL TSAWNGFKTP KELATEVLPH PPTGVPTETL KRIGDVLGSI PENFTVHRNL
     KRILANRKKT VEEGENIDWS TAEALAFGSL CAEGHHVRIS GQDVERGTFS QRHAVLHDQE
     NETTYTSLQH ISPDQGKFVI SNSSLSEFGA LGFEYGYSLT SPDAFVMWEA QFGDFANNAQ
     CIIDQFIASG ESKWLQRSGL VMSLPHGYDG QGPEHSSARI ERYLQLCNED PRVFPAPDRI
     DRQHQDCNMQ IAYMTTPSNL FHVMRRQMNR QFRKPLIIFF SKSLLRHPLC RSPLSDFTGD
     SHFQWIIADP EHGSSSLNNH EDIERVILCS GQVYAALQKH RAAHGINNTA ITRIEQMHPF
     PWQQLKENLD SYPNAKDIVW CQEEPLNAGA WSYMQPRIET LLNETVHHNR RHVLYAGRNP
     SASVATGLKA SHVKEEQDLL QDAFSVHQDR LKGE
//