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Database: UniProt
Entry: A0A0G0ZTZ3_9BACT
LinkDB: A0A0G0ZTZ3_9BACT
Original site: A0A0G0ZTZ3_9BACT 
ID   A0A0G0ZTZ3_9BACT        Unreviewed;       330 AA.
AC   A0A0G0ZTZ3;
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=UU85_C0003G0039 {ECO:0000313|EMBL:KKS25466.1};
OS   Candidatus Wolfebacteria bacterium GW2011_GWA2_42_10.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1619004 {ECO:0000313|EMBL:KKS25466.1, ECO:0000313|Proteomes:UP000034256};
RN   [1] {ECO:0000313|EMBL:KKS25466.1, ECO:0000313|Proteomes:UP000034256}
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:KKS25466.1}.
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DR   EMBL; LCCF01000003; KKS25466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0ZTZ3; -.
DR   PATRIC; fig|1619004.3.peg.222; -.
DR   Proteomes; UP000034256; 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          20..185
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   330 AA;  35774 MW;  0D525972DE697B32 CRC64;
     MISENAKLNP KIFSEDIEQK PTRDGYGEGL LIAGEENPGV VVLCADLKES TRSLPFAQKF
     PERYIEMGVA EQNMATVAAG LGVSNKIPFI SSYAVFSPGR NWEQIRTTIA YNDSNVKICG
     AHAGVSVGPD GATHQAIEDI ATMRAMSNMK VFVPVDAFEA KKATIAAAKI WGPVYLRFTR
     EKTPVFTSED TPFVPGKAEI FYESKKPQVV IVGCGPILYN ALLAAKELEK ENIGVIVLNN
     HTIKPIDEKK IIELAKKCGA VVTVEEHSVI GGLGGSVAEV LAKNYPTPME FVGMKDIFGE
     SGPPEKLIEK YGMGAKDVIS AVKKVIKRKK
//
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