ID A0A2H3TLA0_FUSOX Unreviewed; 1051 AA.
AC A0A2H3TLA0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BFJ68_g11615 {ECO:0000313|EMBL:RKL03335.1}, BFJ69_g12288
GN {ECO:0000313|EMBL:RKK69952.1}, FOXYS1_10386
GN {ECO:0000313|EMBL:KAF5259014.1}, FRV6_13590
GN {ECO:0000313|EMBL:SCO89462.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO89462.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SCO89462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|EMBL:SCO89462.1};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000285084, ECO:0000313|Proteomes:UP000285860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo_A13 {ECO:0000313|EMBL:RKK69952.1,
RC ECO:0000313|Proteomes:UP000285084}, and Fo_A28
RC {ECO:0000313|EMBL:RKL03335.1, ECO:0000313|Proteomes:UP000285860};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
RN [4] {ECO:0000313|EMBL:KAF5259014.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 39464 {ECO:0000313|EMBL:KAF5259014.1};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (FEB-2020) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAAFOW010001844; KAF5259014.1; -; Genomic_DNA.
DR EMBL; MRCX01000144; RKK69952.1; -; Genomic_DNA.
DR EMBL; MRCY01000069; RKL03335.1; -; Genomic_DNA.
DR EMBL; FMJY01000008; SCO89462.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10007338; -.
DR VEuPathDB; FungiDB:FOC4_g10005991; -.
DR VEuPathDB; FungiDB:FOIG_04378; -.
DR VEuPathDB; FungiDB:FOMG_10350; -.
DR VEuPathDB; FungiDB:FOXG_13932; -.
DR VEuPathDB; FungiDB:FOZG_11374; -.
DR VEuPathDB; FungiDB:HZS61_016382; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR Proteomes; UP000285084; Unassembled WGS sequence.
DR Proteomes; UP000285860; Unassembled WGS sequence.
DR Proteomes; UP000558688; 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:UP000558688};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 673..883
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1051 AA; 118484 MW; 7B9D0517782D4999 CRC64;
MLRNSLCRAS SQLLRGARCS AASSTASIST LSARTSSWKL AASRRPLAVA ARRNYATSAT
SAPPDPNDNF LSGSTASYID EMYMQWRQDP ESVHVSWQIY FKNMESGEMP ISQAFQPPPN
LVPNMTGGVP RLAGNLAMED GSDVTNHLKV QLLVRAYQSR GHHTAKIDPL GIRGTNDAKG
FSNIKPKELT LEHYGFTEKD MDTEYTLGPG ILPRFKRDGR EKMTLREIVD ACERIYCGSF
GVEFIHIPDR DKCDWLRERL EVPTPFKYSV DEKRRVLDRL IWSSSFESFL ATKYPNDKRF
GLEGCETLVP GMKALIDRSV DYGVKDIVIG MPHRGRLNVL SNVVRKPNES IFSEFAGTNG
AEDEGSGDVK YHLGMNFERP TPSGKRVQLS LVANPSHLEA EDPVVLGKTR AIQHYNNDEK
THRTAMSVLL HGDAAFAAQG IVYECLGFHS LPAFSTGGTI HLVVNNQIGF TTDPRFARST
AYCTDIAKAI DAPVFHVNAD DVEAVNFVCQ LAADWRAEFQ HDVVIDLNCY RKYGHNETDQ
PSFTQPLMYK RITEKEPQID IYVNKLIEEG SFSKADVDEH KQWVWGMLEE SFTKSKDYTP
TSKEWTTSAW NGFKSPKELA TEVLATNETS VKSTTLEHIG TVIGSTPEGF HVHRNLKRIL
ANRTKSVVEG KNIDFPTAEA LAFGSLVTEG YHVRVSGQDV ERGTFSQRHA VFHDQETEDT
YTPLQHLSQD QGKFVISNSS LSEFGALGFE YGYSLSSPHA LVMWEAQFGD FANNAQCIID
QFIASGEVKW MQRTGLVMSL PHGYDGQGPE HSSGRLERYL QLSNEDPRDF PTGEKLVRQH
QDCNMQIAYM TSPANLFHIL RRQMHRQYRK PLVIFFSKSL LRHPLARSNI EEFTGENAGF
QWIIPDPEHE TGAIKAPEEI ERVILCSGQV WAALHKHRSE NNLDNVAITR IEQLNPFPWQ
QLKENLDQYP NAKTIVWCQE EPLNAGAWSF TQPRIETLLN NTEHHTRKHV MYAGRNPSAS
VATGLKQVHM KEERELLEMA FTVKQDKLKG E
//
