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Database: UniProt
Entry: A0A0G1JDZ0_9BACT
LinkDB: A0A0G1JDZ0_9BACT
Original site: A0A0G1JDZ0_9BACT 
ID   A0A0G1JDZ0_9BACT        Unreviewed;       346 AA.
AC   A0A0G1JDZ0;
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=UW28_C0003G0003 {ECO:0000313|EMBL:KKT42222.1};
OS   Parcubacteria group bacterium GW2011_GWA2_44_13.
OC   Bacteria.
OX   NCBI_TaxID=1618830 {ECO:0000313|EMBL:KKT42222.1, ECO:0000313|Proteomes:UP000034666};
RN   [1] {ECO:0000313|EMBL:KKT42222.1, ECO:0000313|Proteomes:UP000034666}
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:KKT42222.1}.
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DR   EMBL; LCHS01000003; KKT42222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1JDZ0; -.
DR   PATRIC; fig|1618830.3.peg.76; -.
DR   Proteomes; UP000034666; 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   346 AA;  37320 MW;  BB64F505C30697D0 CRC64;
     MPINPNAKLV SNLLDLKTIE QAPTRKGYGE GLLEAGEKNE KVVALCADLT ESTQMHLFAK
     KFPERFIEIG VAEQNMATVA SGLANYGKIP FISSYAMFSP GRNWEQIRTT ICYNNVPVKI
     AGSHVGVSVG PDGATHQAIE DIAITRPIPN ITVINPCDMH EAKKATLAAV SIDGPIYLRF
     HREKTPVFTT PDTPFQIGRA EVVWDPEKGS PSSDDSGRLS LLDVAIIACG PLVHNAILAA
     AELEKAGIKV RVINNHTIKP MDEKTIIQAA KDADAIVTVE EHQVQGGMGS AVAEVLARNY
     PVPIEFIGVQ NRFGESGAPN ELIEHFGMGV SHIIGAVKKV LARKHV
//
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