ID   W6L9D6_9TRYP            Unreviewed;      1026 AA.
AC   W6L9D6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=GSHART1_T00001494001 {ECO:0000313|EMBL:CCW71100.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW71100.1, ECO:0000313|Proteomes:UP000053358};
RN   [1] {ECO:0000313|EMBL:CCW71100.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW71100.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW71100.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW71100.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
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; HF955209; CCW71100.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6L9D6; -.
DR   EnsemblProtists; CCW71100; CCW71100; GSHART1_T00001494001.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000053358; 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   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; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
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; 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:UP000053358};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          631..847
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          894..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  115176 MW;  D224EE777F887E40 CRC64;
     MRRLFHPRRL TRAVFLRCYT DAQTIREPNP YEQILASDNQ EYMENLLTQY EKDRSSVDAS
     WFPVLEAIRT GNLELPVVTA FSRPIDVKSL SVKQRLDNMR LAWMIKEYES KGHHVARVDP
     FNGAFVSSRS LNDLHLDPSA FGFTEADLEK VFLVTFGSNH KATFVSGGTG MTLSQIVQEL
     QKMYCGTIGF DFAFSGPDAL CQWFRNEVYN TLKPLPVEEK REILNDVVKA TKLEKFLYTK
     YPLHKRFGLE GSEALVLALK AAILEASNHG VEHCMFGMPW RGRLNVLANV CGKPLKDIFY
     EFRDDIAPDG ETSDDLFLNL GFNNAINLSN GKQVGIEVLP TSAHAEAATA MVLGKAHARQ
     IYTNDIARIH TMPILIHNDG SMSGEGVCYE LMGMCNLTNY KVGGTFHIVI NNQISFTTDP
     RDSRGNFYCS ELGKMNRTPT MRVNGDDVEA CVRAARIAVR FRQQYQRDVI LELVCYRSYG
     HDVGDIPDLT HPNMYRMIQE HPRLIEIYSK SLIDEGVITA PDFKAKESDC EEAMQNAFER
     ALTSQVFPRT IPLFHPESEN IAEDLPSEVV KAVETLLNAP PPAVITGENY DILKSVGLHI
     ATIPKAMKKP HPVVERTFAN RKKGIENGNA VEWCQAELMA LGTLSLKGTH VRFTGEDVER
     GTFTQRHACI TDMETNEKYT PVATISPNQA LFVMGNSSLS ELGVCGFELG YNMANPRNMV
     IWEAQFGDFA NGAQVVIDDF LSAGERRWGW QASLVLSLPH GYSGAGPEHS SARIERFLQL
     SDALDVVPTT FRKLPNDQML EARIRNRNWQ VCYPSTPASY FHLLRRQGLR DFAKPLVIFF
     SKARLRAPNL SRLEEFAGET SFRAVLDTGA PRGRGRGRAD GEAAPAALLH RPNRKYRRRG
     SRRRAGQDAE PTRRFDPHHA RAARALPLGA GRGCDREVHR AEPRGGVGVA AGGAEEYGHV
     VFYAAADEFP HAAPRRPPAA DSVHRPQELR LPVHRLRLRP RRGGAPDRSG MFRLETNLER
     QGFYRI
//