ID   THIK_ECOLI              Reviewed;         274 AA.
AC   P75948;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Thiamine kinase;
DE            EC=2.7.1.89;
GN   Name=thiK; Synonyms=ycfN; OrderedLocusNames=b1106, JW1092;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=15150256; DOI=10.1128/jb.186.11.3660-3662.2004;
RA   Melnick J., Lis E., Park J.-H., Kinsland C., Mori H., Baba T., Perkins J.,
RA   Schyns G., Vassieva O., Osterman A., Begley T.P.;
RT   "Identification of the two missing bacterial genes involved in thiamine
RT   salvage: thiamine pyrophosphokinase and thiamine kinase.";
RL   J. Bacteriol. 186:3660-3662(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC       phosphate.
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;
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine phosphate from thiamine: step 1/1.
CC   -!- SIMILARITY: Belongs to the thiamine kinase family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74190.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35913.1; -; Genomic_DNA.
DR   PIR; G64854; G64854.
DR   RefSeq; NP_415624.1; NC_000913.3.
DR   RefSeq; WP_001116592.1; NZ_SSZK01000019.1.
DR   AlphaFoldDB; P75948; -.
DR   SMR; P75948; -.
DR   BioGRID; 4260073; 122.
DR   IntAct; P75948; 5.
DR   STRING; 511145.b1106; -.
DR   PaxDb; P75948; -.
DR   PRIDE; P75948; -.
DR   EnsemblBacteria; AAC74190; AAC74190; b1106.
DR   EnsemblBacteria; BAA35913; BAA35913; BAA35913.
DR   GeneID; 948525; -.
DR   KEGG; ecj:JW1092; -.
DR   KEGG; eco:b1106; -.
DR   PATRIC; fig|1411691.4.peg.1161; -.
DR   EchoBASE; EB3206; -.
DR   eggNOG; COG0510; Bacteria.
DR   HOGENOM; CLU_055115_2_1_6; -.
DR   OMA; DVHAGNI; -.
DR   PhylomeDB; P75948; -.
DR   BioCyc; EcoCyc:THIKIN-MON; -.
DR   BioCyc; MetaCyc:THIKIN-MON; -.
DR   BRENDA; 2.7.1.89; 2026.
DR   UniPathway; UPA00060; UER00596.
DR   PRO; PR:P75948; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019165; F:thiamine kinase activity; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..274
FT                   /note="Thiamine kinase"
FT                   /id="PRO_0000218057"
SQ   SEQUENCE   274 AA;  32397 MW;  0F4DBC46F43944CC CRC64;
     MPFRSNNPIT RDELLSRFFP QYHPVTTFNS GLSGGSFLIE HQGQRFVVRQ PHDPDAPQSA
     FLRQYRALSQ LPACIAPKPH LYLRDWMVVD YLPGAVKTYL PDTNELAGLL YYLHQQPRFG
     WRITLLPLLE LYWQQSDPAR RTVGWLRMLK RLRKAREPRP LRLSPLHMDV HAGNLVHSAS
     GLKLIDWEYA GDGDIALELA AVWVENTEQH RQLVNDYATR AKIYPAQLWR QVRRWFPWLL
     MLKAGWFEYR WRQTGDQQFI RLADDTWRQL LIKQ