ID A0A166YJJ3_9HYPO Unreviewed; 1047 AA.
AC A0A166YJJ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BBO_07951 {ECO:0000313|EMBL:OAA36976.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA36976.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA36976.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA36976.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA36976.1}.
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DR EMBL; AZHA01000033; OAA36976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166YJJ3; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000076863; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
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; 118216 MW; 18C0705A717342A3 CRC64;
MLRNSLCRAS SQLLRGARVS PAISSLSTAC 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 AQCIIDQFIA
SGEVKWMQRS GIVMSLPHGY DGQGPEHSSA RIERYLQLSN EDPRVFPAED KLARQHQDCN
MQIAYMTTPA NLFHVLRRQM ERQFRKPLII FFSKSLLRHP LARSSLEEFT AEDAGFQWII
PDPEHQTGAI KSPEEIDRVI LCTGQVWAAL HKYRADNKID NVAFTRIEQL NPFPWQQLKE
NLDMYPNAKT IVWAQEEPLN AGAWSFTQPR IETLLNQTKY HDRKHVMYAG RSPSASVATG
LKHIHSKEEK ELLEMAFTVK QDKLKGE
//
