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 27-MAR-2024, entry version 96.
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; Pseudomonadota; 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}.
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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; 99287-STM1208; -.
DR DNASU; 1252726; -.
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-MONOMER; -.
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 Gene3D; 3.90.1200.10; -; 1.
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 NCBIfam; TIGR02721; ycfN_thiK; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
