ID A0A1Q3SEK5_9CHLR Unreviewed; 313 AA.
AC A0A1Q3SEK5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:OJV86868.1};
GN ORFNames=BGO39_13670 {ECO:0000313|EMBL:OJV86868.1};
OS Chloroflexi bacterium 54-19.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV86868.1, ECO:0000313|Proteomes:UP000186384};
RN [1] {ECO:0000313|EMBL:OJV86868.1, ECO:0000313|Proteomes:UP000186384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54-19 {ECO:0000313|EMBL:OJV86868.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJV86868.1}.
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; MKTJ01000092; OJV86868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3SEK5; -.
DR STRING; 1895928.BGO39_13670; -.
DR Proteomes; UP000186384; 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; 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.
PE 4: Predicted;
FT DOMAIN 5..170
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 313 AA; 33001 MW; E957AE6F2B945033 CRC64;
MTQLFDCRDA FNEKLLELAH LDTRIVTVVN DSVGSSKLTQ FRAEFANRLI NVGIAEQNMV
GVGAGLANGG LIPFVCGASP FLTGRALEQI KADVAYSNTN VKLCGMSSGM AYGELGPTHH
SIEDLAWLRA IANMTIIVPA DPVETSQAVA AAASITGPMF LRISRVGVPV VHPADYKFEI
GKAARLREGR DITLIANGVL VHKALEAAEQ LASEGIEARV LNMATVKPLD EEAVLAAAAE
TGAIVTVEEH TIYGGLGSAV AEVVVTHQPV PMRILGVPGV FAPTGSAEWL LDHFGLNAAG
IYNAARELVK PTK
//