ID   A0A0G0LKF9_9BACT        Unreviewed;       647 AA.
AC   A0A0G0LKF9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000313|EMBL:KKQ92398.1};
GN   ORFNames=UT17_C0002G0061 {ECO:0000313|EMBL:KKQ92398.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWB1_39_10.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618572 {ECO:0000313|EMBL:KKQ92398.1, ECO:0000313|Proteomes:UP000034774};
RN   [1] {ECO:0000313|EMBL:KKQ92398.1, ECO:0000313|Proteomes:UP000034774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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:KKQ92398.1}.
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DR   EMBL; LBVU01000002; KKQ92398.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LKF9; -.
DR   STRING; 1618572.UT17_C0002G0061; -.
DR   Proteomes; UP000034774; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF4; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          335..504
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   647 AA;  72025 MW;  221189E397B6BD64 CRC64;
     MERLSPPVKQ YDKDILNNLA LEIRKSVFET IINANSGHLG GNSSCIELLT CLYFGGVLKF
     DPANPQDKNR DRVLILGHKG PVRYKIFSLM GLFSEDELKT YRQFGSRLQG HEDMHTTPGV
     DITPSGSLGM ILSYGVGDAI VAKEKGSNHK TFVFLGDGEE QEGNISEAAR HAANLGLDNL
     ICILDKNDKQ LSRPTNESDS GSDVRRIWEG YGWNVLEISD GHNVEEIMEV YSKFEDIQKP
     TFVIAHTIKG RGISGAEENF CGYHTLSVTP KDLARQALEL SAKEIKSRND EVQQAKLLAN
     GLVTRPEKLD QSLESKVEFP NVNIAVNPDD ETNLDNSQGF YFKELRSIIE ADNRIKMYVI
     TPDFIRKDLV EMANFERFTK FIDTGIREQH AVAMAHGISI SDPLARIFIN FGDAFIYRAM
     DQLNAVAQGG SKMIIVGEHS GLTQERNGKT HQTSGQPGAL INMPGLNIKE PADVQDLFNV
     LNWAFTNNPG VVYARLHRKN ISPLYRQIDD LKNIRHYITH DPGKKPGLVI VSSGFTTHNS
     VKAAEILESK YNIPTRVVNV ISPGELGKDF LNLLENDTPV LTVYNGFHKV LQSVVSMAVM
     EFTSIRPSVI AGHGFDFGTT GSIVDLERYY QIDELGIVRK AKSLLDK
//