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Database: UniProt
Entry: A0A0G1YYN1_9BACT
LinkDB: A0A0G1YYN1_9BACT
Original site: A0A0G1YYN1_9BACT 
ID   A0A0G1YYN1_9BACT        Unreviewed;       334 AA.
AC   A0A0G1YYN1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=UY99_C0003G0015 {ECO:0000313|EMBL:KKW48391.1};
OS   Parcubacteria group bacterium GW2011_GWA1_59_11.
OC   Bacteria.
OX   NCBI_TaxID=1618804 {ECO:0000313|EMBL:KKW48391.1, ECO:0000313|Proteomes:UP000033896};
RN   [1] {ECO:0000313|EMBL:KKW48391.1, ECO:0000313|Proteomes:UP000033896}
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   -!- 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:KKW48391.1}.
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DR   EMBL; LCSE01000003; KKW48391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1YYN1; -.
DR   PATRIC; fig|1618804.3.peg.86; -.
DR   Proteomes; UP000033896; 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; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   4: Predicted;
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          21..186
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   334 AA;  35663 MW;  87EFA9F752C5E286 CRC64;
     MPLDPKAKLN AAVFEGDVAQ RPIRDGYGEG LARAGETNRN VVALSADLAE STRNEDFARL
     FPDRFFEIGV AEQNMAAIAA GLGVSGKIPF ISSYAVFSPG RNWEQIRTTI AYNDSNVKIA
     GHHAGVSVGP DGATHQALED IAAMRAMPNM KVIVPCDAIE ARKATEAAAR IWGPVYLRFA
     REKSPVLTTE STPFRPGKAE VFWQPSGALK AQAAIVACGP LLHQALLAAR ELEKNKIGVL
     VLNSHTVKPL DEEAIIGAAR RTGAVVTVEE HQIAGGLGGA VAELLARRCP APVEFVGIGD
     SFGESGTPEE LWRKFGLTAK DIRAAVKRAL RRKA
//
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