ID A0A166WB70_9PEZI Unreviewed; 923 AA.
AC A0A166WB70;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CT0861_05040 {ECO:0000313|EMBL:KZL75512.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL75512.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL75512.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL75512.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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}.
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:KZL75512.1}.
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DR EMBL; LFIV01000022; KZL75512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166WB70; -.
DR STRING; 708197.A0A166WB70; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000076552; 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:UP000076552};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 576..774
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 923 AA; 101674 MW; 921B72B43FB43A93 CRC64;
MYAAWKANPA NVHVSWHTYF RKMEDPSVHS TRAFQPPPGL LPERHTPALT SATTAAPSDR
VNYLKAQSVV RAFQQHGHTA AKINPLGDLA NATVQPHADI PSASNLSKYG FSAADLDCEI
PLGPEILPHL ARSRESMKLR DIIEACEEIY CGPLGIEYHH ISDAAKREWV RERIEAYHGS
TLSVEEKKRV LDTLIWATSL ERFLAAKFPN EKRFGLDGAE GLAPGLAALI DRCAEVHGVQ
DIVMGSCHRG RMNLMSTVYG KDFETLFRQF AGTEKFDTEG GQTGDVKYHF GMDGQRTTAG
GRTVGISMLP NPSHLEAVDP VAQGKAKAVQ HVNNDADQSK VMFMALHGDA AFSGQGPVYE
TLNLSALKGY EVGGTVRIMV NNQIGFTTDS PDSRSTPYCT DLAKYIGAPI IHVNADDPEA
VVYACKLAAD WRAKFRSDIV VDVNCYRRFG HNEIDQASFT QPEMYKRIAE KKALMELYIE
KLVREGTTSA EVVEQQKAWV WEQLEEKLAK SKQPAEQSEE VTSRNSVVPT TATAVEESTL
ATVAQAITSV PEGFNLHRNL QRILVAKKQA FDAGVLDWST AEALAFGSLV MEGKPVRISG
QDVERGTFSQ RHSVLHDQNT HAEHTPLNHL QESQAAYTAV NSPLSEFGVL GFDYGYSLAA
KNALVMWEAQ FGDFVNNAQV IIDQFIASGE AKWLLKSGLV MSLPHGYDGQ GPEHSSARLG
RFLELGSEDP RSWPADLAAA KRECNVRIVC MTTPANLFHA LRRQVHSPEK KLQDLTGTST
FQPVLADPEH GASILPKDEI RRVILCSGQV YAALHKHREA KGIKDVAITR LEELHPFPWA
EVKENLESYP GAETVVWAQE EPYNGGAWQY MRDRLETVAR ESEVLGGKRT VYAGRGTGAA
AATGSKKVHQ QEEEKLLADA FGI
//
