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Database: UniProt
Entry: A0A1F5SH79_9BACT
LinkDB: A0A1F5SH79_9BACT
Original site: A0A1F5SH79_9BACT 
ID   A0A1F5SH79_9BACT        Unreviewed;       293 AA.
AC   A0A1F5SH79;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 10.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=A2227_02570 {ECO:0000313|EMBL:OGF26078.1};
OS   Candidatus Falkowbacteria bacterium RIFOXYA2_FULL_47_19.
OC   Bacteria; Candidatus Falkowbacteria.
OX   NCBI_TaxID=1797994 {ECO:0000313|EMBL:OGF26078.1, ECO:0000313|Proteomes:UP000178367};
RN   [1] {ECO:0000313|EMBL:OGF26078.1, ECO:0000313|Proteomes:UP000178367}
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:OGF26078.1}.
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DR   EMBL; MFGB01000017; OGF26078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5SH79; -.
DR   STRING; 1797994.A2227_02570; -.
DR   Proteomes; UP000178367; 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..167
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   293 AA;  32165 MW;  6DE21203F06A5507 CRC64;
     MRKQFVNTIE NILTTDERLV LLLGDIGVWG FNKALALYPE RVYNIGILEQ STVGLAAGLA
     MSGFIPVIHT IAPFLVERSY EQLKLDFCYQ KMGGNFLSIG GSYDYAALGC THHCPGDVGI
     LKNLPGMEII LPGTAQEFDT LFRDTYANGH PTYFRLSDRP NKNSYNVKFG KAEILQRGNL
     ATIVAVGPTL NHVLEACTGM DVTILYYTTV TPFDSETLKN NSASGKILLC EPYYKGGLTA
     EIAEALSLRP IVIDSIGVPK RFLSNYGSAD EHDLNIGLSA ININKKLKKL IYG
//
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