THIK_ECO57
ID THIK_ECO57 Reviewed; 274 AA.
AC Q8X8G6; Q7AF80;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=Z1745, ECs1484;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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; AE005174; AAG55852.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34907.1; -; Genomic_DNA.
DR PIR; D90814; D90814.
DR PIR; H85673; H85673.
DR RefSeq; NP_309511.1; NC_002695.1.
DR RefSeq; WP_001116570.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X8G6; -.
DR SMR; Q8X8G6; -.
DR STRING; 155864.EDL933_1684; -.
DR DNASU; 913746; -.
DR EnsemblBacteria; AAG55852; AAG55852; Z1745.
DR EnsemblBacteria; BAB34907; BAB34907; ECs_1484.
DR GeneID; 913746; -.
DR KEGG; ece:Z1745; -.
DR KEGG; ecs:ECs_1484; -.
DR PATRIC; fig|386585.9.peg.1585; -.
DR eggNOG; COG0510; Bacteria.
DR HOGENOM; CLU_055115_2_1_6; -.
DR OMA; DVHAGNI; -.
DR UniPathway; UPA00060; UER00596.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000218059"
SQ SEQUENCE 274 AA; 32439 MW; F17EB845E8F4EA65 CRC64;
MPFRSNNPIT RDELLSRFFP QFHPVTTFNS GLSGGSFLIE HQGQRFVVRQ PHDPDAPQSA
FLRQYRALSQ LPACIAPKPH LYLRDWMVVD YLPGEVKTYL PDTNELAGLL YYLHQQPRFG
WRITLLPLLE LYWQQSDPAR RTVGWLRMLK RLRKAREPRP LRLSPLHMDV HAGNLVHSAS
GLKLIDWEYA GDGDIALELA AVWVENTEQH RQLVNDYATR AKIYPAQLWR QVRRWFPWLL
MLKAGWFEYR WRQTGDQQFI RLADDTWRQL LIKQ
