ID M2THP6_COCSN Unreviewed; 1044 AA.
AC M2THP6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=COCSADRAFT_178113 {ECO:0000313|EMBL:EMD68237.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD68237.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD68237.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445638; EMD68237.1; -; Genomic_DNA.
DR RefSeq; XP_007695899.1; XM_007697709.1.
DR AlphaFoldDB; M2THP6; -.
DR STRING; 665912.M2THP6; -.
DR GeneID; 19133122; -.
DR KEGG; bsc:COCSADRAFT_178113; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000016934; 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:UP000016934};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 667..877
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 118371 MW; 81696F6715A2CCD4 CRC64;
MLRNTLRQCS RKLPGSAPTR ASFTTFAQPS RTAISTCRRP LALTHRRPYA VSAEETSKGV
DPNDSFLQGN TANYIDAMYM QWKHDPESVH YSWQVYFHNM ESGDMPVSQA FQPPPTIMSS
PQGATARPGM GMANVEGTDI MNHLKVQLLV RAYQARGHHK AKIDPLGIRS EAESFGYNKP
RELELSHYNF TDKDLEQEIE LGPGILPRFR TESRKKMKLK EIIDACERLY CGSYGIEYIH
IPDREQCDWL RERIEVPTPF KYSVDEKRRI LDRLIWGTNF EAFLATKYPN DKRFGLEGGE
SLIPGMKALI DRSVDYGVKD IVIGMPHRGR LNVLSNVVRK PNESIFSEFA GTAEANEEGS
GDVKYHLGMN FERPTPSGKR VQLSLVANPS HLEAEDPVVL GKTRAILHYN NDEKEAVSAM
GVLLHGDAAF AAQGVVYETM GFHQLPSYHT GGTIHIVVNN QIGFTTDPRF SRSTPYCSDI
AKAIDAPVFH VNGDDVEAVN FVCQLAADFR AEFKKDVVID MVCYRKQGHN ETDQPFFTQP
LMYKKISQQP QTLDIYTKKL LEEKTFTKED IDEHKAWVWG MLDESFNRSK DYVSNSREWL
TSAWNGFKTP KELATEVLPH LPTAIEEPQL KHIAKVIGEA PEDFNVHKNL KRILAGRTKT
VMDGQNIDMA TAEALAFGSL CMEGHHVRVS GQDVERGTFS QRHAVLHDQE TEKTYTPLQN
LSQDQATFTI SNSSLSEYGV LGFEYGYSLS SPNALVMWEA QFGDFANTAQ VIIDQFIASG
EVKWLQRSGL VMSLPHGYDG QGPEHSSGRI ERYLQLCNED PRIFPSPEKL DRQHQDCNMQ
IAYTTKPSNL FHLLRRQMNR QFRKPLILFF SKSLLRHPIA RSSIDEFTGD SHFQWIIEDP
AHASGEIESH EGINRVILCT GQVYAALVKE REARGEKDVA ITRIEQLNPF PWQQLKDNLD
SYPNAQNIIW CQEEPLNAGA WSFTQPRIET LLNQTEHHNR RHVMYAGRNP SASVATGLKV
SHKNEEKALL DMAFTVKQDK LKSE
//
