ID E5A9P5_LEPMJ Unreviewed; 1045 AA.
AC E5A9P5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=LEMA_P015160.1 {ECO:0000313|EMBL:CBY00386.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929138; CBY00386.1; -; Genomic_DNA.
DR RefSeq; XP_003843865.1; XM_003843817.1.
DR AlphaFoldDB; E5A9P5; -.
DR STRING; 985895.E5A9P5; -.
DR EnsemblFungi; CBY00386; CBY00386; LEMA_P015160.1.
DR GeneID; 13292491; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; E5A9P5; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000002668; Genome.
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: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:UP000002668};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 668..878
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1045 AA; 118217 MW; 4C9DBD799BA0A2B0 CRC64;
MLRNTMRQCS RKLQSYPARS LSTLAAAPSR TAITSCRRPL ALAPRRHYAI AAEDTNKGVD
PNDSFLQGNT ANYVDAMYMQ WKHDPSSVHI SWQVYFRNME SGDMPVSQAF QPPPTIVPTP
EGGAPDFKPG MGMASAEGSD VMNHLKVQLL VRAYQARGHH KAKIDPLGIR SEAEQFGYSK
PRELELSHYN FTEKDLDHEI ELGPGILPRF KTESRKKMTL REIIDACERL YCGSYGIEYI
HIPDREQCDW LRERIEVPTP FKYSVDEKRR ILDRLIWGTN FEAFLATKYP NDKRFGLEGG
ESLIPGMKAL IDRSVDYGVK DIVIGMPHRG RLNVLSNVVR KPNESIFSEF AGTAEAGDEG
SGDVKYHLGM NFERPTPSGK RVQLSLVANP SHLEAEDPVV LGKTRAILHY NNDEKEAVSA
MGVLLHGDAA FAGQGIVYET MGFHQLPQYH TGGTIHIIVN NQIGFTTDPR FSRSTPYCSD
IAKAIDAPVF HVNGDDVEAL NFVCQLAADF RAQFKKDVVI DMVCYRKQGH NETDQPFFTQ
PLMYKKIAQQ PQTLDIYTQK LLEEKTFTKE DIDEHKAWVW GMLDESFNRS KDYTPTAKEW
LTSAWNGFKS PKELATEVLP HLPTAIEESQ LKHIAEKIGS APEGFNVHKN LKRILAGRTK
TVVEGQNIDM ATAEALAFGS LCMEGHHVRV SGQDVERGTF SQRHAVLHDQ ENEQTYTPLQ
NLTEDQATFT ISNSSLSEYG VLGFEYGYSL SSPNALVMWE AQFGDFANTA QVIIDQFIAS
GEVKWLQRSG LVMSLPHGYD GQGPEHSSAR MERYLQLVNE DPRIFPSADK LDRQHQDCNI
QIAYTTKPSN LFHLLRRQMN RQFRKPLILF FSKSLLRHPI ARSNLEEFTG DSHFQWIIED
PAHASGEIES HEGINRVILC TGQVYAALVK EREARGLKDV AITRLEQLNP FPWQQLKENL
DSYPNAQNII WCQEEPLNAG AWSFTQPRIE TLLNETEYHN RRHVMFAGRN PSASVATGLK
NSHKKEEKDL LEMAFSVKQD KLKGE
//
