ID   THIK_ECOL6              Reviewed;         274 AA.
AC   Q8FIN3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Thiamine kinase {ECO:0000255|HAMAP-Rule:MF_01604};
DE            EC=2.7.1.89 {ECO:0000255|HAMAP-Rule:MF_01604};
GN   Name=thiK {ECO:0000255|HAMAP-Rule:MF_01604}; OrderedLocusNames=c1379;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_01604}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thiamine = ADP + H(+) + thiamine phosphate;
CC         Xref=Rhea:RHEA:12012, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37575, ChEBI:CHEBI:456216;
CC         EC=2.7.1.89; Evidence={ECO:0000255|HAMAP-Rule:MF_01604};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine phosphate from thiamine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01604}.
CC   -!- SIMILARITY: Belongs to the thiamine kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01604}.
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DR   EMBL; AE014075; AAN79849.1; -; Genomic_DNA.
DR   RefSeq; WP_001116601.1; NC_004431.1.
DR   AlphaFoldDB; Q8FIN3; -.
DR   SMR; Q8FIN3; -.
DR   STRING; 199310.c1379; -.
DR   EnsemblBacteria; AAN79849; AAN79849; c1379.
DR   KEGG; ecc:c1379; -.
DR   eggNOG; COG0510; Bacteria.
DR   HOGENOM; CLU_055115_2_1_6; -.
DR   OMA; DVHAGNI; -.
DR   BioCyc; ECOL199310:C1379-MON; -.
DR   UniPathway; UPA00060; UER00596.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019165; F:thiamine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR   HAMAP; MF_01604; Thiamine_kinase; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR014093; Thiamine_kinase.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR02721; ycfN_thiK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..274
FT                   /note="Thiamine kinase"
FT                   /id="PRO_0000218058"
SQ   SEQUENCE   274 AA;  32441 MW;  ED7FB1F418F7BC65 CRC64;
     MPFRSNNPLT RDELLSRFFP QFHPVTTFNS GLSGGSFLIE HQGQRFVVRQ PHDPDAPQSA
     FLRQYRALSQ LPACIAPKPH LYLRDWMVVD YLPGEVKTYL PDTNELAGLL YYLHQQPRFG
     WRITLLPLLE LYWQQSDPAR RTVGWLRMLK RLRKAREPRL LRLSPLHMDV HAGNLVHSAS
     GLKLIDWEYA GDGDIALELA AVWVENTDQH RQLVNDYATR AKIYPAQLWR QVRRWFPWLL
     MLKAGWFEYR WRQTGDQQFI RLADDTWRQL LIKQ