ID E8XEX6_SALT4 Unreviewed; 274 AA.
AC E8XEX6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Thiamine kinase {ECO:0000256|HAMAP-Rule:MF_01604};
DE EC=2.7.1.89 {ECO:0000256|HAMAP-Rule:MF_01604};
GN Name=thiK {ECO:0000256|HAMAP-Rule:MF_01604,
GN ECO:0000313|EMBL:ADX16907.1};
GN OrderedLocusNames=STM474_1205 {ECO:0000313|EMBL:ADX16907.1};
OS Salmonella typhimurium (strain 4/74).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX16907.1, ECO:0000313|Proteomes:UP000008978};
RN [1] {ECO:0000313|EMBL:ADX16907.1, ECO:0000313|Proteomes:UP000008978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX PubMed=21478351; DOI=10.1128/JB.00394-11;
RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT animals.";
RL J. Bacteriol. 193:3162-3163(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC phosphate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01604};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from thiamine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01604}.
CC -!- SIMILARITY: Belongs to the thiamine kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_01604}.
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DR EMBL; CP002487; ADX16907.1; -; Genomic_DNA.
DR RefSeq; WP_001257342.1; NC_016857.1.
DR AlphaFoldDB; E8XEX6; -.
DR SMR; E8XEX6; -.
DR KEGG; seb:STM474_1205; -.
DR PATRIC; fig|909946.3.peg.1234; -.
DR HOGENOM; CLU_055115_2_1_6; -.
DR UniPathway; UPA00060; UER00596.
DR Proteomes; UP000008978; 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 {ECO:0000256|HAMAP-Rule:MF_01604};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01604, ECO:0000313|EMBL:ADX16907.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01604};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01604}.
FT DOMAIN 43..235
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
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
//
