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}.
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; 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
//