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Database: UniProt
Entry: A0A1F6R8Q1_9BACT
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ID   A0A1F6R8Q1_9BACT        Unreviewed;       313 AA.
AC   A0A1F6R8Q1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000313|EMBL:OGI16905.1};
GN   ORFNames=A2255_07080 {ECO:0000313|EMBL:OGI16905.1};
OS   Candidatus Melainabacteria bacterium RIFOXYA2_FULL_32_9.
OC   Bacteria; Candidatus Melainabacteria.
OX   NCBI_TaxID=1801611 {ECO:0000313|EMBL:OGI16905.1, ECO:0000313|Proteomes:UP000198209};
RN   [1] {ECO:0000313|EMBL:OGI16905.1, ECO:0000313|Proteomes:UP000198209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGI16905.1}.
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DR   EMBL; MFRQ01000162; OGI16905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6R8Q1; -.
DR   STRING; 1801611.A2255_07080; -.
DR   Proteomes; UP000198209; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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   PANTHER; PTHR43825:SF5; HYPOTHETICAL TRANSKETOLASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          1..163
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   313 AA;  34637 MW;  B75AC6947FF802EC CRC64;
     MRDAFTRNLK ELFHKDENMF FITSDTGYKV LDEFQETFPD RYLNIGISEA NMIGVAAGLA
     LSGKKVFTYA IAPFITLRCF EQIRVNLCFQ NLPVFLVGIG GGLTYGAGGA THHTIEDIAV
     LNSLPNMTII CPGDPVEVEL AMQKMSEVQG PVYLRLGKSG EKVIHQQSPK FEIGKGIKVL
     QGNDVAIITT GNMLETGYTV CEMLTHQGLN PGLISMHTVK PIDKNLIEET AKQYKLIVTI
     EEHNVIGGLG SSVSDVITER DLNVRFKKFG IPDRYVDVVG SQEFLRAQFG LKPEQISADI
     LNYLKGKVYE KAN
//
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