ID J5J9C7_BEAB2 Unreviewed; 1047 AA.
AC J5J9C7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, 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=BBA_08088 {ECO:0000313|EMBL:EJP62883.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP62883.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP62883.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP62883.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(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; JH725180; EJP62883.1; -; Genomic_DNA.
DR RefSeq; XP_008601407.1; XM_008603185.1.
DR AlphaFoldDB; J5J9C7; -.
DR STRING; 655819.J5J9C7; -.
DR GeneID; 19891100; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; J5J9C7; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000002762; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 669..879
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1047 AA; 118185 MW; A9C75E6B1CFA7946 CRC64;
MLRNSLCRAS SQLLRGARVS PVISSLSAAC ARPSSWNVTA ARRSLTLASR RTYATTDASH
SAPDPNDNFL TGSTANYIDE MYMQWKKDPK SVHVSWQIYF KNMESGDMPI SQAFQPPPNL
VPNMTGGVPR LGDGLVMEDG SDVTNHLMVQ LLVRAYQARG HHKANIDPLG IRNTAEGFGN
IKPKELTLDF YGFTEKDLDT EYTLGPGILP RFKREGREKM TLREIVAACE KIYSGSYGVE
FIHIPDREKC DWLRERLEVP QPFKFSIDEK RRILDRLIWS SSFESFLMTK YPNDKRFGLE
GCETLVPGMK ALIDRSVDYG VKDIVIGMPH RGRLNVLSNV VRKPNESIFS EFGGTDTAEE
GSGDVKYHLG MNFERPTPSG KRVQLSLVAN PSHLEAEDPV VLGKTRAIQH YNNDEKSHRT
AMSVLLHGDA AFAAQGIVYE CLGFHSLPAF STGGTIHLVV NNQIGFTTDP RFARSTAYCT
DIAKAIDAPV FHVNADDVEA VNFVCQLAAD WRAEFQHDVV IDLICYRKHG HNETDQPSFT
QPLMYKRINS QVPQIDVYVD KLLKEGTFTK EDIDEHKQWV WGMLEESFAK SKDYTATSKE
WTTSAWNGFK SPKELATEIL PHNPTNVDKK TIEHIGEVIG SAPEGFTVHR NLKRILNNRT
KSVVEGKNID FPTAEALAFG SLVTDGYHVR VSGQDVERGT FSQRHAVFHD QENEATYTPL
QHISKDQGKF VIANSSLSEF GALGFEYGYS LSSPNALVMW EAQFGDFANN AQCIIDQFVA
SGEVKWMQRS GIVMSLPHGY DGQGPEHSSA RIERYLQLSN EDPRVFPAKD KLARQHQDCN
MQIAYMTTPA NLFHVLRRQM ERQFRKPLII FFSKSLLRHP LARSSLEEFT AEDAGFQWII
PDPEHQTGAI KSPEEIDRVI LCTGQVWAAL HKYRADNKID NVAFTRIEQL NPFPWQQLKE
NLDMYPNAKT IVWAQEEPLN AGAWSFTQPR IETLLNQTKY HDRKHVMYAG RSPSASVATG
LKHVHSKEEK ELLEMAFTVK QDKLKGE
//
