ID   A0A0G0XJY2_9BACT        Unreviewed;       638 AA.
AC   A0A0G0XJY2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:KKS24742.1};
GN   ORFNames=UU83_C0020G0004 {ECO:0000313|EMBL:KKS24742.1};
OS   Candidatus Jorgensenbacteria bacterium GW2011_GWF2_41_8.
OC   Bacteria; Candidatus Jorgensenbacteria.
OX   NCBI_TaxID=1618667 {ECO:0000313|EMBL:KKS24742.1, ECO:0000313|Proteomes:UP000033856};
RN   [1] {ECO:0000313|EMBL:KKS24742.1, ECO:0000313|Proteomes:UP000033856}
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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:KKS24742.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LCCD01000020; KKS24742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0XJY2; -.
DR   PATRIC; fig|1618667.3.peg.357; -.
DR   Proteomes; UP000033856; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
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   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          329..492
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   638 AA;  70405 MW;  729654801EE402CB CRC64;
     MLEKDKLYFV PLYELEELRN KIITSGSDCQ VYLNILATIL RINILYMIKN AGSGHIGTSF
     SSLEMMLWLW MMEMRGANDS SIPNSDTFFS SKGHDAPALY AVMVALGKIC FNNIHQLRKM
     GGLPGHPDIH TPFVAANTGS LGMGISKARG MAIANRLRGS KGRIFIIIGD GELQEGQIWE
     SLQPAANGNF SEITVLADLN QIQSDREVSK TSHLGPLVEK FKGFGWNVSC CNGNDFSSLK
     YALDSRSKEK PNIILAKTKK GFGVSFMECL DENGFYKYHS GAPSDEDYYR ALEELTITAD
     RALMASGMDC LLLVCNKKPE VAGVGLRVEK LIQAYGEELC ELGKIRTDMV VLNADLVVDC
     GLVGFKNEFP ERFVECGIAE QDMVSAAGGL ALKGVLPIVH SFGCFLSTRP NEQIYNNATE
     KTKIIYTAPL AGLLPAGPGH SHQSVRDISL VGAIPGVTIF EPCNEIETKL ALRWAVNENP
     ESTYIRLVII PVEITYKLPA GYQLNKGQGI RLYTPSRVGS KTAILAYGPV MLGQAINAAR
     EIGADLYNFP WLNFIDEDWF YGKLARYKNL VVVDDHYTKF GLGTLIGAVV AKSRLDIHFS
     QLGLEEIPVC GQTKEVLRHH QLDDFSIAER ITDEFKNI
//