ID A0A0A2VY65_BEABA Unreviewed; 935 AA.
AC A0A0A2VY65;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BBAD15_g2971 {ECO:0000313|EMBL:KGQ11317.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ11317.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ11317.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ11317.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ11317.1}.
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DR EMBL; ANFO01000227; KGQ11317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VY65; -.
DR STRING; 1245745.A0A0A2VY65; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR Proteomes; UP000030106; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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:UP000030106};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 593..786
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 935 AA; 105020 MW; 0A09B644609542AC CRC64;
MQNGAMKPWL DSSWLAGANQ SYIEQLYEDF LTDPDSVDAH WRTMFQQLPG TGARPDQFHS
KTRDYFRRLA KDASRYSTAI TDPDTDVKQV KVLQLINAWR FRGHQAANLD PLGLWKQESV
PDLDPAFHNL TDEDLQQSFN VGSFAGGKET MKLADLIDAL QQTYGGSIGA EYMHITNTEE
KRWIQQRIES VVGQSTFTPE EKKRFLSELT AAEGLERYLG AKFPGAKRFS LEGGDALVPM
LKEMIRHAGK SGTREVVLGM AHRGRLNVLI NVLGKKPQDL FDEFAGKHKE HLGTGDVKYH
MGFSSDVETE GGLVHLALAF NPSHLEIVSP VVIGSVRARL DRLDKPGSNQ VLPITIHGDA
AVAGQGVVQE TLNMSKARGY EVGGTVRIVI NNQIGFTTSN PLDARSTPYC TDIGKMVMAP
IFHVNADDPE AVAFVTRLAL DFRNTFKRDV FIDLVCYRRH GHNEADEPSA TQPVMYQKIK
KHPTPRKIYA DKLEQDKLAT LEDATEMVNL YRDALDAGEC VVNEWRPMNM HSFTWSPYLN
HEWDESYPNK VEMKRVQELA KRISTVPEAV EMQSRVAKIY SDRQEMANGN KLFDWGAAEN
LAYATLVDEG VSVRLSGEDA GRGTFFHRHA VIHNQTNGST YTPLAHVHNS QGIFKVWDSV
LSEEAVLAFE YGYATAEPRT LTIWEAQFGD FANGAQVVID QFISSGEQKW GRMCGLVMLL
PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLVVMSP
KSLLRHPLAV SSLDELANGA FQPAIGEIDE LDPKGVKRVV LCSGKVYYDL LEQRRKNDQK
DVAIVRIEQL YPFPHQAVQE ALKPFAHVHD FVWCQEEPLN QGAWYCSQHH FREVIPFGSA
LRYAGRPASA SPAVGYMSVH QKQQQDLVND ALNVE
//