ID   THIK_SALTY              Reviewed;         274 AA.
AC   Q8ZQ07;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=STM1208;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006468; AAL20137.1; -; Genomic_DNA.
DR   RefSeq; NP_460178.1; NC_003197.2.
DR   RefSeq; WP_001257342.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZQ07; -.
DR   SMR; Q8ZQ07; -.
DR   STRING; 99287.STM1208; -.
DR   PaxDb; Q8ZQ07; -.
DR   DNASU; 1252726; -.
DR   EnsemblBacteria; AAL20137; AAL20137; STM1208.
DR   GeneID; 1252726; -.
DR   KEGG; stm:STM1208; -.
DR   PATRIC; fig|99287.12.peg.1277; -.
DR   HOGENOM; CLU_055115_2_1_6; -.
DR   OMA; DVHAGNI; -.
DR   PhylomeDB; Q8ZQ07; -.
DR   BioCyc; SENT99287:STM1208-MON; -.
DR   UniPathway; UPA00060; UER00596.
DR   Proteomes; UP000001014; 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; Reference proteome; Transferase.
FT   CHAIN           1..274
FT                   /note="Thiamine kinase"
FT                   /id="PRO_0000218062"
SQ   SEQUENCE   274 AA;  31941 MW;  AE29F8621639A575 CRC64;
     MRSNNNNPLT RDEILSRYFP QYRPAVATSQ GLSGGSCIIA HDTHRVVLRR HHDPDAPPAH
     FLRHYRALSQ LPASLAPRAL FYTPGWMAVE YLHGVVNSAL PDADELAALL YHLHQQPRFG
     WRIALSPLLA QYWSCCDPAR RTPFWLRRLK QLQKNGEPRP LRLAPLHMDV HGDNIVLTSA
     GLRLIDWEYA GDGDIALELA AVWVEDERQH RQLADAYAAR ARIDARQLWR QIRLWHPWVI
     MLKAGWFEYR WRQTGEQQFI RLADETWRQL RMKG