ID   V9EAE6_PHYPR            Unreviewed;       955 AA.
AC   V9EAE6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component, variant 2 {ECO:0000313|EMBL:ETI35227.1};
GN   ORFNames=F443_18367 {ECO:0000313|EMBL:ETI35227.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI35227.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI35227.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI35227.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:ETI35227.1}.
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DR   EMBL; ANIZ01003168; ETI35227.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9EAE6; -.
DR   EnsemblProtists; ETI35227; ETI35227; F443_18367.
DR   OrthoDB; 89567at2759; -.
DR   Proteomes; UP000018721; 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; 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; 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:UP000018721};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          570..800
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   955 AA;  108313 MW;  709DF26B41B36606 CRC64;
     MLRVLRKGGA VRARPVAVVL RRWKSEKLTP PVQKLSDDIR RSQEETRRVL LLIRTFKQYG
     HYVAQIDPLQ KREKLPELER WINGDRDLDR EFFIGQDLSI GPVATLREIV TELRELFCGH
     IGLEYQHLRN RDAALWIRER LEKYKENQFS NEEKVDMLRQ MVQAELFERF LGRRFSGAKR
     FSIEGCESLI PGLCELLESA SEHGVEVVQM GMAHRGRLNV LANVLQRPLR SIISQFQPYL
     PDEPDYPNNS DDVRYHLGTS SVIEMRNGKN LEVTLAANPS HLEAVNPVVL GQARACQTQL
     GDDGSRVMPI LIHGDASMFQ GSVREALGFS SLEDFRTGGT IHVIINNQIG FTTLPKNADS
     AVYCTDVAKV SRSPIFHVNA DDPEAVAKVM RIAVEFRQKF QCDVTIDLVC YRRHGHNEQD
     SPEITAPIMY HFINKHPTVI KLYSQKLTSE GALSPKEYVK MCSTFEDHLV SEYHHSREIH
     SGWDDPGDTS WKTEWYADSK IPNSETPANT SNVCDNNDKQ IYDRSTGVDQ NFLEKVGSQL
     FRIPQGFSAH RKVEAIMNNR LRAVETGARV DWATAEMLAF GSLLVEGVDV RLSGQDCERG
     TFNQRHAVLY DQFEALSGRN SSYTPLNNLD VEGIRSTLQM TGLESARRGR FDVVNSPLSE
     EGVLGFEYGY SLQTPMGLTI WEAQFGDFAN GAQTMIDTFI TTGEQKWQRQ SGIVLNLPHG
     FEGQGPEHSS ARLERFLQLV NEDSDEFTGE QDVNAAITRT NIQVVIPSTP AQYFHALRRQ
     VSSSYRKPLI MFTPKSLLHH RPCNSDLADL VVGTSFQRVL PPHPDDQVTM VNDDEIRKLV
     LCCGKIYFPV RHGMRSRGIR DIATARIEQL APFPFHEVAD YIARYPNAEI VWVQEEPKNM
     GAYSHVLPRL LTVLKYLDDP RKFSYIGRPP SASPATGQYE IHLQEMKTIV DEALA
//