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Database: UniProt
Entry: W2PNA2_PHYPN
LinkDB: W2PNA2_PHYPN
Original site: W2PNA2_PHYPN 
ID   W2PNA2_PHYPN            Unreviewed;       986 AA.
AC   W2PNA2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:ETN01729.1};
GN   ORFNames=PPTG_17143 {ECO:0000313|EMBL:ETN01729.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN01729.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN01729.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN01729.1,
RC   ECO:0000313|Proteomes:UP000018817};
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 INRA-310.";
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}.
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DR   EMBL; KI669623; ETN01729.1; -; Genomic_DNA.
DR   RefSeq; XP_008913044.1; XM_008914796.1.
DR   AlphaFoldDB; W2PNA2; -.
DR   STRING; 761204.W2PNA2; -.
DR   EnsemblProtists; ETN01729; ETN01729; PPTG_17143.
DR   GeneID; 20186167; -.
DR   VEuPathDB; FungiDB:PPTG_17143; -.
DR   OrthoDB; 89567at2759; -.
DR   Proteomes; UP000018817; 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:UP000018817};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          601..831
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   986 AA;  111853 MW;  A6FDBA408D9B7273 CRC64;
     MLRVLRKGGA VRARPVAVVL RRWKSEKLTP PVQKLSDDIR RSQEETRRVL LLIRTFKQYG
     HYVAQIDPLQ KREKLPELER WINGDRWVET PFFDDFNLRS LASKNLLELT THGFTASDLD
     REFFIGQDLS IGPVATLREI VTELRELFCG HIGLEYQHLR NRDAALWIRE RLEKYKENQF
     SNEEKVDMLR QMVQAELFER FLGRRFSGAK RFSIEGCESL IPGLCELLES ASEHGVEVVQ
     MGMAHRGRLN VLANVLQRPL RSIISQFQPY LPDEPDYPNN SDDVRYHLGT SSVIEMRNGK
     NLEVTLAANP SHLEAVNPVV LGQARACQTQ LGDDGSRVMP ILIHGDASMF QGSVREALGF
     SSLEDFRTGG TIHVIINNQI GFTTLPKNAD SAVYCTDVAK VSRSPIFHVN ADDPEAVAKV
     MRIAVEFRQK FQCDVTIDLV CYRRHGHNEQ DSPEITAPIM YHFINKHPTV IKLYSQKLTS
     EGALSPKEYV KMCSTFEDHL VSEYHHSREI HSGWDDPGDT SWKTEWYADS KIPNSETPAN
     TSNVCDNNDK QIYDRSTGVD QNFLEKVGSQ LFRIPQGFSA HRKVEAIMNN RLRAVETGAR
     VDWATAEMLA FGSLLVEGVD VRLSGQDCER GTFNQRHAVL YDQFEALSGR NSSYTPLNNL
     DVEGIRSTLQ MTGLESARRG RFDVVNSPLS EEGVLGFEYG YSLQTPMGLT IWEAQFGDFA
     NGAQTMIDTF ITTGEQKWQR QSGIVLNLPH GFEGQGPEHS SARLERFLQL VNEDSDEFTG
     EQDVNAAITR TNIQVVIPST PAQYFHALRR QVSSSYRKPL IMFTPKSLLH HRPCNSDLAD
     LVVGTSFQRV LPPHPDDQVT MVNDDEIRKL VLCCGKIYFP VRHGMRSRGI RDIATARIEQ
     LAPFPFHEVA DYIARYPNAE IVWVQEEPKN MGAYSHVLPR LLTVLKYLDD PRKFSYIGRP
     PSASPATGQY EIHLQEMKTI VDEALA
//
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