ID   THIK_ECO27              Reviewed;         274 AA.
AC   B7UPC2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=E2348C_1198;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS08746.1; -; Genomic_DNA.
DR   RefSeq; WP_001116587.1; NC_011601.1.
DR   AlphaFoldDB; B7UPC2; -.
DR   SMR; B7UPC2; -.
DR   EnsemblBacteria; CAS08746; CAS08746; E2348C_1198.
DR   KEGG; ecg:E2348C_1198; -.
DR   HOGENOM; CLU_055115_2_1_6; -.
DR   OMA; DVHAGNI; -.
DR   UniPathway; UPA00060; UER00596.
DR   Proteomes; UP000008205; 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_1000185831"
SQ   SEQUENCE   274 AA;  32538 MW;  C7B98BF9F2EB8BFB CRC64;
     MPFRSNNPIT RDELLSRFFP QFHPVTTFNS GLSGGSFLIE HQGQRFVVRQ PHDPDAPRFA
     FLRQYRALSQ LPACIAPKPH LYLRDWMVVD YLPGEVKTYL PDTNELAGLL YYLHQQPRFG
     WRITLLPLLE LYWQQSDPAR RTVGWLRRLK RLRKAREPRP LRLSPLHMDV HAGNLVHSAS
     GLKLIDWEYA GDGDIALELA AVWVENTDQH RQLVNDYATR AKIYPAQLWR QVRRWFPWLL
     MLKAGWFEYR WRQTGDQQFI RLADDTWRQL LIKQ