ID H3G7C9_PHYRM Unreviewed; 874 AA.
AC H3G7C9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra50827, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra50827}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra50827};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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; DS566053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3G7C9; -.
DR STRING; 164328.H3G7C9; -.
DR EnsemblProtists; Phyra50827; Phyra50827; Phyra50827.
DR VEuPathDB; FungiDB:PSURA_50827; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; H3G7C9; -.
DR OMA; LFEINWI; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 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:UP000005238};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 490..720
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 874 AA; 98138 MW; 1EF8CBB49CBA6F81 CRC64;
GFTASDLDRE FFIGQDLSIG PVATLREIVT ELRELFCGHI GLEYQHLRNR DAALWIRERL
EKYKDEPHSK EEKVDMLRQM VQAELFERFL GRRFSGAKRF SIEGCESLIP GLCELLENAS
DHGVEVVQMG MAHRGRLNVL ANVLQRPLRS IISQFQPYLP DEPDYPNNSD DVRYHLGTSS
MLKMRNGKQL EVNLAANPSH LEAVNPVVLG QARACQTQLG DNGSRVMPIL IHGDAAMFQG
SVREALGFSS LEDFRTGGTI HVIINNQIGF TTLPKNADSA VYCTDVAKVS RSPIFHVNAD
DPEAVAKVMK IAVEFRQTFH CDVTVDLVCY RRHGHNEQDS PEITAPVMYH FINKHPTIIK
LYSQKLASEG TLPPKDYAKM CSTFEDHLVS EYHHSRENHS GWDNPGDTSW KTEWYADTKS
DISKSFPGDL SNACELTDKP IYDRSTGVDK SFLEKVGGQL FRIPQGFSAH RKVEAIMNNR
LRAVETGDRV DWATAEMLAF GCLLVEGVDV RLSGQDCERG TFNQRHAVLY DQFEALSGRN
SSYTPLNDLD VDGVRSSLQM TGLENAPCGR FDVVNSPLSE EGVLGFEYGY SIQTPMGLTI
WEAQFGDFAN GAQTMIDTFI TSGEQKWQRQ SGIVLNLPHG FEGQGPEHSS ARIERFLQLV
NEDGDEFTAE EGIDAAMTRT NVQVVIPSTP AQYFHALRRQ ISSSYRKPLI MFTPKSLLHH
RPCNSDLADL TLGTSFQRVL PPHPDDQVTM VNDDEIRKLV LCCGKIYFPV RHGLRSRGIR
NIATARIEQL APFPFHEVAD CIARYPKAEI VWVQEEPKNM GAYGHILPRL LTVLEHLGDS
REFSYIGRPP SASPATGQYE IHVHEMKTIV DEAL
//
