ID A0A0D1ZZ94_9PEZI Unreviewed; 1053 AA.
AC A0A0D1ZZ94;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=PV09_08934 {ECO:0000313|EMBL:KIV99389.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99389.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIV99389.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99389.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847578; KIV99389.1; -; Genomic_DNA.
DR RefSeq; XP_016209259.1; XM_016362910.1.
DR AlphaFoldDB; A0A0D1ZZ94; -.
DR STRING; 253628.A0A0D1ZZ94; -.
DR GeneID; 27316907; -.
DR VEuPathDB; FungiDB:PV09_08934; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; A0A0D1ZZ94; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000053259; 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:UP000053259};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 676..886
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 118727 MW; B0448B9F0A4892F2 CRC64;
MWRASLSRCG GGVKACSRAS LSSLSRASHN ASVASRRRAM AVVCRSHQTR SYASSAEEPK
GSIGEGVNPN DAFLQGNTAN YIDEMYMQWK NDPSSVHISW QIYFRNMEDG DMPIEQAFQA
PPTILPPPHG GLPDFKPGMG MEIGAGSDTM NHLKVQLLVR AYQARGHHKA KIDPLGIRGS
DYEPWYSKPK ELELSHYNFT EKDLDQEFTL GPGILPRFKT ETRQKMTLRE IIDTCERLYC
GSYGVEYIHI PDREQCDWIR ERVEIPQPFK YSVDEKRRIL DRLIWGTSFE AFLATKYPND
KRFGLEGGEA LIPGMKALID RSVDYGVKDI VIGMPHRGRL NVLSNVVRKP NESIFSEFSG
TADPADEGSG DVKYHLGMNF ERPTPSGKRV QLSLVANPSH LEAEDPVVLG KTRAILHYNG
DEKEANTAMG VLLHGDAAFA GQGVVYETLG FYNLPGYQTG GTIHIIVNNQ IGFTTDPRFA
RSTPYCSDIA KAIDAPVFHV NGDDVEALNF ICQLAADWRA KFKKDVVIDM VCYRKQGHNE
TDQPFFTQPL MYKKIAEQKP ALDKYVDRLL ADGTFTKEDI DEHKKWVWGM LEESFTRSKD
YQPTAKEWLT SAWNGFKSPK ELATEVLPHL PTAVDRETLV KIGNAIGSAP EGFNVHRNLK
RILAQRTKTV SEGKGIDMST AEALAFGSLC LDGHHVRVSG QDVERGTFSQ RHAVLHDQEN
EATWTPLANL SKDQATFVIS NSSLSEYGVL GFEYGYSLSS PNALVMWEAQ FGDFANNAQC
IIDQFIASGE VKWLQRTGIV LSLPHGYDGQ GPEHSSGRIE RYLQLCNEDP RVFPSPDKLD
RQHQDCNMQV AYVTKPSNYF HLLRRQMNRQ FRKPLILFFS KSLLRHPMAR SSIEEFTGDS
HFQWVIPDPA HEDGTIEGRD QIKRVIMCTG QVYTALVKHR EELGDKTTAI TRLEQLHPFP
WQQLKDNLDS YPNAETLVWA QEEPLNAGGW SFTQPRIETL LNETQHHNRK HVMYAGRAPS
ASVATGLKSV HKKEEKELLE MAWSVRQDKL KGE
//
