ID A0A0G1XQV2_9BACT Unreviewed; 389 AA.
AC A0A0G1XQV2;
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=UY77_C0002G0003 {ECO:0000313|EMBL:KKW33255.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWA2_53_10.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618980 {ECO:0000313|EMBL:KKW33255.1, ECO:0000313|Proteomes:UP000034711};
RN [1] {ECO:0000313|EMBL:KKW33255.1, ECO:0000313|Proteomes:UP000034711}
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:KKW33255.1}.
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DR EMBL; LCRI01000002; KKW33255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XQV2; -.
DR PATRIC; fig|1618980.3.peg.44; -.
DR Proteomes; UP000034711; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 28..193
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 368..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 340..367
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 389 AA; 42013 MW; 676F9EC67EA7E133 CRC64;
MARTKPQKGL NRDAYLVRGI FHANVEQLPT RDGYGRGLVE AGKNDPNIVV LCADLSESTR
SLWFKQAFPD RFVQLGVSEQ SMASIAAGMA LAGKVPFISS YAGFSPGRNW EQIRTAVALN
NTNVKIAGAH AGVSVGPDGA THQMMEDIAI MRVMPNMRVI VPCDSIETRK ATIAAAQLNG
PAYLRFTREK SPVFTTEKTP FKLGRAETFR FGSDLTILAC GPLVYEALKA AEQLSKQGIE
ARVLNIHTIK PLDEKAIVRA VKETGAIVTV EEAQGAGGLG GAVAEVLGLT APTPLEIIGM
PDRFGESGEP LELLEAFGLT APSITLAALR VLKRKQEKSV PEQKESVVAA QKRLMQLQKE
IMEEALARAP RKWGGSKPDT SLKSRKRSP
//
