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}.
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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
//