ID L8WWJ8_THACA Unreviewed; 1099 AA.
AC L8WWJ8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AG1IA_03630 {ECO:0000313|EMBL:ELU42340.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU42340.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU42340.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(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}.
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:ELU42340.1}.
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DR EMBL; AFRT01000856; ELU42340.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WWJ8; -.
DR STRING; 983506.L8WWJ8; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR OMA; RDSYCRT; -.
DR Proteomes; UP000011668; 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:UP000011668};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 731..943
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 123815 MW; 48BC916847CB4534 CRC64;
MSAFETIKRS TLTRSAKSAG TREPEMLEEF KRGAHDSLVY PRAFRAHEFQ WILQSSHIQS
MTVPCNRPEL NQAAQAGSMV TRTLSRSTRS DKSHDCATFY PVTMRSLLRH RAIARASRPL
VRCYATAAPP SPNDAFATST NAYYVEEMYK HWKRDPSSVH ASWQAYFSGL DKGLSSPNAF
QPPPDYTGVP MAADGAPSLH VGSGALTDHL KVQLLVRAYQ VRGHHVADLD PLGVLDADLH
NIVPAELELS HYGWTERDLD KKFKLGPGIL PHYARDGTQE MTLRDIIRTC EKIYCSSIGF
QYIHIPDKDQ CDWIRERVEI SKPYNYTTDE KRMILDRLMW SEMFEKFIAS KFPSEKRFGL
EGCESLIPGM KALIDRSVDH GVKSIVMGMP HRGRLNVLAN VVRKPIEAIL NEFIGTEDAN
DLASGDVKYH LGANYVRPTP SGKRVSLSLV ANPSHLEAED PVVLGKTRAL QHFENDEQAH
NTAMGVLLHG DAAFAGQGVV YETMGMAGLP SYGTGGTIHL IVNNQIGFTT DPRFSRSTPY
CSDIAKSIDA PIFHVNGDDA EAVTFVCQLA ADWRAKYKKD VVVDIVCYRR YGHNETDQPA
FTQPKMYKAI EKQPTPLTQY TQALIKEGTF TEQDIEEHRK WVWGMLEKAA AASKEYKPSP
KEWLSSSWDG FPSPKELAEQ NLPHRPTGVD EEIHRTIGNT ISNVPQGFTP HRNLARILSA
RGKSVEQGSG IDWATAEALA FGSLVLEKYH VRISGQDVER GTFSQRHAVI HDQENEAQYV
PLNNLGHDQA VFKVCNSSLS EFGTLGFELG YSLVSPRNLT MWEAQFGDFA NNAQCIIDQF
IAAGERKWVQ RSGLVMSLPH GYDGQGPEHS SGRIERFLQL VDDHPDIFPS PEKMERMHQD
CNMQIVYPTT PANYFHVLRR QVHRDFRKPI QLILFFSKSL LRHPLVKSDL SEMTGETHFQ
RYLPEPHPED VLVAPEQIKR HILCSGQVYY TLLKAREDRG VKDVAISRLE QLSPFPYDLL
TPHLDKYPNA ELMYCQEEPL NCGGWTYVAP RIRTASNETQ HHKGTYPKYA GRDPTSSVAT
GSKHKHKKEI EQYLDAAFA
//
