ID A0A397GRD7_9EURO Unreviewed; 1057 AA.
AC A0A397GRD7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
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 Name=KGD1 {ECO:0000313|EMBL:RHZ52114.1};
GN ORFNames=CDV56_100666 {ECO:0000313|EMBL:RHZ52114.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ52114.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ52114.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ52114.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ52114.1}.
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DR EMBL; NKHU02000139; RHZ52114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397GRD7; -.
DR STRING; 41047.A0A397GRD7; -.
DR VEuPathDB; FungiDB:CDV56_100666; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000215305; 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:UP000215305};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 681..891
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1057 AA; 118785 MW; F65BE18694437E89 CRC64;
MLRTTAVKAT SSGLLRGPAC SACRRSISLT STARATSSHS SKFGLTTRRP LAIVDRLSNG
RRHYAAAADA GVDPNDNFLS GNTANYIDEM YLAWKNDPSS VHISWQTYFK NMEDGNMPIS
QAFQPPPTLV PTPTGGVPQT MPGEGLGLAA GTDLTNHLKV QLLVRAYQAR GHHKAKIDPL
GIRGEAEAFG YNKPKELELD HYGFTERDLD QEFTLGPGIL PRFATESRKK MTLREIIATC
EKIYCGSYGV EYIHIPDRKP CDWIRDRFEI PEPYKYSVDD KRRILDRLIW SHSFESFLAT
KFPNDKRFGL EGCETLVPGM KALIDRSVEH GIKDIVIGMP HRGRLNVLSN VVRKPNESIF
SEFSGSAEPS DEGSGDVKYH LGMNFERPTP SGKRVQLSLV ANPSHLEAED PVVLGKTRSI
QHYNNDEKDF NSAMGVLLHG DAAFAGQGVV YETMGFHSLP AYSTGGTIHI IVNNQIGFTT
DPRYSRSTPY CSDIAKSIDA PVFHVNADDV EAVNYVCQIA ADWRAEFKRD VVIDIVCYRK
QGHNETDQPS FTQPLMYKRI AEQKAQLDKY VEKLIAEGTF TKEDIDEHKK WVWGMLNDSF
DRSKDYQPTG KEWLTSAWNG FKTPKELATE VLPHLPTAVD ASLLSHIADK ISGAPEGFTV
HRNLKRILAN RKKAVDEGKN IDWATAEALA FGSLVKEGYH VRVSGQDVER GTFSQRHAVL
HDQENEATYT PLKHIGEDQG SFVISNSSLS EFGALGFEYG YSLTSPNALV MWEAQFGDFA
NNAQCIIDQF IASGESKWLQ RSGLVVSLPH GYDGQGPEHS SGRMERWLQL CNEEPRQFPT
QDKLDRQHQD CNMQIAYMTS PANLFHILRR QIHRQFRKPL VIFFSKSLLR HPIARSDIEE
FTGDSHFQWI IPDPAHGTAI DEPEKIERVI LCSGQVYATL IKHREAKGIR NTAITRVEQL
HPFPWAQLKE NLDSYPNAKD IVWAQEEPLN AGAWSYTQPR IETLLNETEH HNRRHVLYAG
RAPSASVATG LKSVHAKEEQ DFLEEAFTVH QDRLKGE
//
