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Database: UniProt
Entry: A0A2J8C0R2_VERDA
LinkDB: A0A2J8C0R2_VERDA
Original site: A0A2J8C0R2_VERDA 
ID   A0A2J8C0R2_VERDA        Unreviewed;      1047 AA.
AC   A0A2J8C0R2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-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=BJF96_g6253 {ECO:0000313|EMBL:PNH30614.1};
OS   Verticillium dahliae (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=27337 {ECO:0000313|EMBL:PNH30614.1, ECO:0000313|Proteomes:UP000236305};
RN   [1] {ECO:0000313|EMBL:PNH30614.1, ECO:0000313|Proteomes:UP000236305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12008 {ECO:0000313|EMBL:PNH30614.1,
RC   ECO:0000313|Proteomes:UP000236305};
RA   Fan R., Armitage A.D., Cascant-Lopez E., Sobczyk M., Cockerton H.M.,
RA   Harrison R.J.;
RT   "Comparative genomics yields insights into virulence evolution of
RT   Verticillium dahliae.";
RL   Submitted (DEC-2017) 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:PNH30614.1}.
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DR   EMBL; MPSH01000020; PNH30614.1; -; Genomic_DNA.
DR   Proteomes; UP000236305; Unassembled WGS sequence.
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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
SQ   SEQUENCE   1047 AA;  118367 MW;  3883182A2273EFC1 CRC64;
     MLRSSLSKAS TRVLQSSRCA APSSRRFSTL PTTPRTAATQ TLAASRRPLS LTARRHYASA
     TDNAPDPNDN FLSGNTANYI DEMYMQWKED PKSVHVSWQV YFRNMESGDM PISQAFTPPP
     SLVPGATGGV PRLAAGSAEG TEVANHLKVQ LLVRAYQARG HNKANIDPLG IRNEQKGFGN
     IKPKELTLEH YQFTEKDLDT EYSLGPGILP RFKREGREKM TLREIIDACE RIYCGSYGIE
     FIHIPDREKC DWLRERLEVP QPFKYSIDEK RRILDRLIWS SSFESFLSTK YPNDKRFGLE
     GCETLVPGMK ALIDRSVDYG VKDIVIGMPH RGRLNVLSNV VRKPNESIFS EFAGTAGAED
     EGSGDVKYHL GMNFERPTPS GKRVQLSLVA NPSHLEAEDP VVLGKTRAIQ HYNNDEKAHR
     TAMGVLLHGD AAFAAQGVVY ECLGFHSLPA FSTGGTIHLV VNNQIGFTTD PRFARSTAYC
     TDIAKAIDAP VFHVNADDVE AVNFVCQMAA DWRAEFQQDV IVDLVCYRKH GHNETDQPSF
     TQPLMYKRIQ SHKSQIAIYV DKLIKDGTFT KEDVEEHKQW VWGMLEESFT KSKEYQPTSK
     EWTTSAWNGF KSPKELATEV LPHNTTSVDK KTLEHIGEVI GSTSEGFNVH RNLKRILSNR
     TKSVVEGKNI DFPTAEALAF GSLVTEGHHV RVSGQDVERG TFSQRHAVFH DQETEDTYTP
     LQNISKDQGK FVIANSSLSE FGALGFEYGY SLSSPNALVM WEAQFGDFAN NAQCIIDQFI
     ASGEVKWMQR TGLVMSLPHG YDGQGPEHSS GRLERYLQLC NEDPRVFPSP EKLERQHQDC
     NMQIAYFTTP ANLFHALRRQ MHRQFRKPLI IFFSKSLLRH PLARSNIEEF VDESHFQWII
     PDPEHEAGTI KKPEEIKRVV LCTGQVWAAL HKYRADNKID DTAFTRIEQL NPFPWQQLKE
     NLDQYPNAET IVWAQEEPLN AGAWSFTQPR IETLLNQTEH HNRKHVMYAG RNPSASVAAG
     TKGLHTKEEQ EFLEMAFTVK QDKLKGE
//
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