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Database: UniProt
Entry: A0A0G0UV20_9BACT
LinkDB: A0A0G0UV20_9BACT
Original site: A0A0G0UV20_9BACT 
ID   A0A0G0UV20_9BACT        Unreviewed;       332 AA.
AC   A0A0G0UV20;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=UT90_C0001G0045 {ECO:0000313|EMBL:KKR54172.1};
OS   Parcubacteria group bacterium GW2011_GWA1_40_21.
OC   Bacteria.
OX   NCBI_TaxID=1618784 {ECO:0000313|EMBL:KKR54172.1, ECO:0000313|Proteomes:UP000034712};
RN   [1] {ECO:0000313|EMBL:KKR54172.1, ECO:0000313|Proteomes:UP000034712}
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:KKR54172.1}.
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DR   EMBL; LBYO01000001; KKR54172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0UV20; -.
DR   STRING; 1618784.UT90_C0001G0045; -.
DR   PATRIC; fig|1618784.3.peg.56; -.
DR   Proteomes; UP000034712; 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   332 AA;  36058 MW;  11D05DC39DEE56AF CRC64;
     MINPNLKLNP KLFKEDIEQV PTRFGYGEGL VIAGKENPNV VALCADLTDS TRTSVFKKEF
     PDRFVEVGIG EQNMASLASG MAAVGKVPFI SSYAMFSPGR NWEQIRTTIC YNNQNVKIAG
     AHSGVSVGPD GATHQAIEDM AITRVVPNMI VIAPCDAIEA KKATIAAARH KGPVYIRFTR
     EKTPVMTTEE TPFEIGKAEI YREGKDVSII ACGPLLYEAL KAAEELAKEG IEAEVINNHT
     VKPMDKETIL QSVKKTGCVV TIEEHQAAGG MGSAVSEILS QNHPAPMEII GVKDRFGESG
     EPHQLLEKFG LTAPFIKEAV LKVIKRKIKL KG
//
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