ID   THIK_SALPC              Reviewed;         274 AA.
AC   C0Q785;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=SPC_2538;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(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; CP000857; ACN46643.1; -; Genomic_DNA.
DR   RefSeq; WP_001257334.1; NC_012125.1.
DR   AlphaFoldDB; C0Q785; -.
DR   SMR; C0Q785; -.
DR   EnsemblBacteria; ACN46643; ACN46643; SPC_2538.
DR   KEGG; sei:SPC_2538; -.
DR   HOGENOM; CLU_055115_2_1_6; -.
DR   OMA; DVHAGNI; -.
DR   UniPathway; UPA00060; UER00596.
DR   Proteomes; UP000001599; 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_1000185832"
SQ   SEQUENCE   274 AA;  31857 MW;  1E38E0181C39B40E CRC64;
     MRSNNNNPLT RDEILSRYFP QYRPAVAASQ GLSGGSCIIA HDTHRVVLRR HHDPDAPPAH
     FLRHYRALSQ LPASLAPRAL FYTPGWMAVE YLHGVVNSAL PDADELAALL YHLHQQPRFG
     WRIALSPLLA QYWSCCDPAR RTPFWLRRLK QLQKNGEPRP LRLAPLHMDV HGDNIVLTSA
     GLRLIDWEYA GDGDIALELA AVWVEDERQH RQLANAYAAC ARIDARQLWR QIRLWHPWVI
     MLKAGWFEYR WRQTGEQQFI RLADETWRQL RMKG