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Database: UniProt
Entry: A0A0G0QPL2_9BACT
LinkDB: A0A0G0QPL2_9BACT
Original site: A0A0G0QPL2_9BACT 
ID   A0A0G0QPL2_9BACT        Unreviewed;       332 AA.
AC   A0A0G0QPL2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, 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=UT41_C0002G0114 {ECO:0000313|EMBL:KKR12340.1};
OS   Candidatus Wolfebacteria bacterium GW2011_GWC2_39_22.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1619013 {ECO:0000313|EMBL:KKR12340.1, ECO:0000313|Proteomes:UP000034665};
RN   [1] {ECO:0000313|EMBL:KKR12340.1, ECO:0000313|Proteomes:UP000034665}
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:KKR12340.1}.
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DR   EMBL; LBWR01000002; KKR12340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0QPL2; -.
DR   STRING; 1619013.UT41_C0002G0114; -.
DR   PATRIC; fig|1619013.3.peg.765; -.
DR   Proteomes; UP000034665; 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          22..187
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   332 AA;  36127 MW;  046DBEF0B1BF83E6 CRC64;
     MHMLSVENFI SEKTFESDVE QKATRDGFGT GLVQLGETNP DVVVLSADLK ESTRCEAFAT
     KYPKRFFECG VAEQNMITLA AGFGVSNKIP FAASYAVFSP GRNWEQIRTT IAYNDANVKI
     AGHHAGISTG PDGATHQAIE DIATMRSMPN MRVIVPVDAL EAHKATVAAS QIWGPIYLRF
     TREKSPLVTT QETPFIPDKA YTLWESKKPQ VVIIGCGPLL HQALLAAQEL EKEKIGTLVL
     NSHTVKPLDE KKIVALAKKY GAVVTVEEHS VLGGLGGAVA ECLAKHQPTP IEFIGMQDTF
     GESGTSAELF KKYKLDKNAI ADAVKKVIAR KK
//
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