ID   W6KUJ5_9TRYP            Unreviewed;      1005 AA.
AC   W6KUJ5;
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=GSEM1_T00004499001 {ECO:0000313|EMBL:CCW60986.1};
OS   Phytomonas sp. EM1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW60986.1, ECO:0000313|Proteomes:UP000027080};
RN   [1] {ECO:0000313|EMBL:CCW60986.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW60986.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW60986.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW60986.1};
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; HF955063; CCW60986.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6KUJ5; -.
DR   EnsemblProtists; CCW60986; CCW60986; GSEM1_T00004499001.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000027080; 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; 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:UP000027080};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          631..847
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1005 AA;  113205 MW;  A1DE69EE368BEAF4 CRC64;
     MRRLFQERLL ASAAFLRSYT DARTVREPYP YDQIVAAENQ EYIENLLKLY EKDRASVDVS
     WLPVLEAIRS GSVEMPVVTA FSRPIDVKTL SEKQRLDNMR LAWMIKEYES KGHHVAKVDP
     FNGAFTSSRS LNDLHLDPAA FGFSQEDLEQ VFHVTFGSNQ KATFVSGGTA MTLEQIVKQL
     QQMYCGSIGF DFTSSGPTAL RNWFRHEILG SLKAFSLEDK KRILSDVVKT TKLERFLYSK
     YPMQTRFGLE GSEALVLALK AAINEASSNS VEHCIVGMAW RGRLNVIANV CGKPLKDLFY
     EFINDAPPDG ADKDDIFLNF GYRNSVHLPN GKQMGIEVMP TSIHSEAATS LVLGKTHARQ
     MYTSDIGQTH TMPILIHGDA SLSGQGACYE LMGLCNLKNY KVGGTLHIVI NNQIGFTTDP
     RDSRGSAYCS DIGKINRSPI IRVNGDDAEA CVRAARIATR FRQHYQRDVI LELVCYRSYG
     HDVRDTPDFT HPNMYRMIQE HPRLIEIYSK TLIDENLITP EEFNAEVNEY EKTMQNEFER
     AITAQVFPKT VLLFHPESEN TSEDLSSEKV KAAKSLLNAP PPAIITGENA ELLKTVGLHV
     ATIPREMKKA HPVVERTFAN RNKGIQNGDA IEWCQAELMA LGTLSLKGIH VRFTGEDVER
     GTFTQRHATI TDMLTNMKYT PVATLSPDQA PFVISNSSLS ELGVCGFELG YNLENPKSVV
     IWEAQFGDFA NGAQVIFDHV LSVVEQRWGM RSSLVLSLPH GYSGAGPEHS SARIERYLQL
     SDDVDALPNT FRKLPSDQML EARIRDRNWQ VCYPSTPASY FHMLRRQGLR DFAKPLVFFF
     SKARLRAPNL SRLEDLAGDT TFRAVLDTGA AKTKPRKLLF CSGQIESIVA EARAAIQAKE
     PHKHDDLILI TLEQLAPFPW EQVADVIEKY VALNPEVELV WLQEEPKNMG MWSFMRPRMN
     SLMRHLGVRQ PRITYIGREN SASPATGYGS IHVEEERQII HECFA
//