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Database: UniProt
Entry: A0A1Q3SEK5_9CHLR
LinkDB: A0A1Q3SEK5_9CHLR
Original site: A0A1Q3SEK5_9CHLR 
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}.
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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
//
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