ID   THIK_SHISS              Reviewed;         274 AA.
AC   Q3Z311;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SSON_1126;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87851.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3Z311; -.
DR   SMR; Q3Z311; -.
DR   EnsemblBacteria; AAZ87851; AAZ87851; SSON_1126.
DR   KEGG; ssn:SSON_1126; -.
DR   HOGENOM; CLU_055115_2_1_6; -.
DR   OMA; DVHAGNI; -.
DR   UniPathway; UPA00060; UER00596.
DR   Proteomes; UP000002529; 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_0000291002"
SQ   SEQUENCE   274 AA;  32377 MW;  7B8DE5BC58B324D8 CRC64;
     MPFRSNNPIT RDELLSRFFP QFHPVTTFNS GLSGGSFLIE HQGQRFVVRQ PHDPDAPQSA
     FLRQYRALSQ LPASIAPKPH LYLRDWMVVD YLPGAVKTYL PDTNELAGLL YYLHQQPRFG
     WRITLLPLLE LYWQQSDPAR RTVGWLRMLK RLRKAREPRP LRLSPLHMDV HAGNLVHSAS
     GLKLIDWEYA GDGDIALELA AVWVENTEQH RQLVNDYATR AKIYPAQLWR QVRRWFPWLL
     MLKAGWFEYR WRQIGDQQFI RLADDTWRQL LIKQ