ID   B7LG39_ECO55            Unreviewed;       274 AA.
AC   B7LG39;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=ycfN {ECO:0000313|EMBL:CAU97077.1};
GN   Synonyms=thiK {ECO:0000256|HAMAP-Rule:MF_01604};
GN   OrderedLocusNames=EC55989_1218 {ECO:0000313|EMBL:CAU97077.1};
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055 {ECO:0000313|EMBL:CAU97077.1, ECO:0000313|Proteomes:UP000000746};
RN   [1] {ECO:0000313|Proteomes:UP000000746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAU97077.1; -; Genomic_DNA.
DR   RefSeq; WP_001116554.1; NC_011748.1.
DR   AlphaFoldDB; B7LG39; -.
DR   KEGG; eck:EC55989_1218; -.
DR   HOGENOM; CLU_055115_2_1_6; -.
DR   UniPathway; UPA00060; UER00596.
DR   Proteomes; UP000000746; 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};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01604};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000746};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01604, ECO:0000313|EMBL:CAU97077.1}.
FT   DOMAIN          25..233
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   274 AA;  32423 MW;  4C366CBC40F4E4D6 CRC64;
     MPFRSNNPIM RDELLSRFFP QFHPVTTFNS GLSGGSFLIE HQGQRFVVRQ PHDPDAPQSA
     FLRQYRALSQ LPASIAPKPH LYLRDWMVVD YLPGAVKTYL PDTNELAGLL YYLHQQPRFG
     WRITLLPLLE LYWQQSDPAR RTVGWLRMLK RLRKVREPRP LRLSPLHMDV HAGNLVHSAS
     GLKLIDWEYA GDGDIALELA AVWVENTEQH RQLVNDYATR AKIYPAQLWR QVRRWFPWLL
     MLKAGWFEYR WRQTGDQQFI RLADDTWRQL LIKQ
//