GenomeNet

Database: UniProt
Entry: A0A0G1WJ46_9BACT
LinkDB: A0A0G1WJ46_9BACT
Original site: A0A0G1WJ46_9BACT 
ID   A0A0G1WJ46_9BACT        Unreviewed;       640 AA.
AC   A0A0G1WJ46;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:KKW18868.1};
GN   ORFNames=UY60_C0002G0045 {ECO:0000313|EMBL:KKW18868.1};
OS   Parcubacteria group bacterium GW2011_GWB1_50_9.
OC   Bacteria.
OX   NCBI_TaxID=1618884 {ECO:0000313|EMBL:KKW18868.1, ECO:0000313|Proteomes:UP000034442};
RN   [1] {ECO:0000313|EMBL:KKW18868.1, ECO:0000313|Proteomes:UP000034442}
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   -!- 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:KKW18868.1}.
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; LCQP01000002; KKW18868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WJ46; -.
DR   PATRIC; fig|1618884.3.peg.93; -.
DR   Proteomes; UP000034442; 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   CDD; cd02012; TPP_TK; 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; TRANSKET_PYR 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   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          333..499
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   640 AA;  70699 MW;  444B276DBD03C398 CRC64;
     MSELTSAALS EKTLYYVPLS EIQRIRKSIS DPFLLAWVLS DVFRINALYM IRSTNSGHIG
     SSFSSIDIAT WLWTQELRNP NESGKDPSDI YFSSKGHDVP ALYSILIGLE KLDFEMIHKL
     RRLGGLPGHP DTGTPYIAAN TGSLGMGISK ARGMAKAKRL QGKSGRVYVL TGDGELQEGQ
     IWESLQPTVN GKYSEITAIV DHNKIQSDSW VSDLNDVSAI EQRFRDFGWE VLRCDGHDFY
     ALKKAFDRAK TVGDRPQMLI ADTIKGKGVS FMERMDADGT YKFHSGAPAY EQYVAAFEEI
     RDRANSNLKS TGLDVLQFES AMMPATTMPG TVERLIPAYG DELLKIGRER KDVVVLDADL
     IPDTGVLAFK NEFPDRFVEC GIAEQDMVSM AGGIALQGML PIAHSFAAFV STRPNEHIYN
     NATEKKRIIY VGTLAGLLPG MPGHSHQSVR DISALGGIPG LVAIEPANER EARMAIRWAV
     EKNPESTYIR FVSVASEAPY RLPEKYELEI GKGALLVQGT DVLIMAYGPV MMTEAVKAVE
     LLRGKGISTA VMNFPWLNRV DSAWLSKALN GYPLVVTIDD HYVSLGQGMQ IRSALAPHMK
     GQRILSLGVE EIPACGHNSE VLQYHKLDFE SIAERIEKET
//
DBGET integrated database retrieval system