ID THIM1_STRPJ Reviewed; 260 AA. AC B8ZN14; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 05-JUL-2017, entry version 56. DE RecName: Full=Hydroxyethylthiazole kinase 1 {ECO:0000255|HAMAP-Rule:MF_00228}; DE EC=2.7.1.50 {ECO:0000255|HAMAP-Rule:MF_00228}; DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase 1 {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=TH kinase 1 {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=Thz kinase 1 {ECO:0000255|HAMAP-Rule:MF_00228}; GN Name=thiM1 {ECO:0000255|HAMAP-Rule:MF_00228}; GN OrderedLocusNames=SPN23F06420; OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=561276; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700669 / Spain 23F-1; RX PubMed=19114491; DOI=10.1128/JB.01343-08; RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., RA Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., RA Bentley S.D., Mitchell T.J.; RT "Role of conjugative elements in the evolution of the multidrug- RT resistant pandemic clone Streptococcus pneumoniae Spain23F ST81."; RL J. Bacteriol. 191:1480-1489(2009). CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of CC 4-methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|HAMAP- CC Rule:MF_00228}. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC {ECO:0000255|HAMAP-Rule:MF_00228}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00228}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00228}. CC -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00228}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FM211187; CAR68489.1; -; Genomic_DNA. DR ProteinModelPortal; B8ZN14; -. DR SMR; B8ZN14; -. DR EnsemblBacteria; CAR68489; CAR68489; SPN23F06420. DR KEGG; sne:SPN23F06420; -. DR KO; K00878; -. DR OMA; KRPLVHN; -. DR UniPathway; UPA00060; UER00139. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01170; THZ_kinase; 1. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF02110; HK; 1. DR PIRSF; PIRSF000513; Thz_kinase; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 260 Hydroxyethylthiazole kinase 1. FT /FTId=PRO_1000198131. FT BINDING 39 39 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00228}. FT BINDING 115 115 ATP. {ECO:0000255|HAMAP-Rule:MF_00228}. FT BINDING 160 160 ATP. {ECO:0000255|HAMAP-Rule:MF_00228}. FT BINDING 187 187 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00228}. SQ SEQUENCE 260 AA; 27635 MW; B1846DA024C97404 CRC64; MTSLKLLKEK APLVICITND VVKNFTANGL VALGASPAMS EFPADLEDLL KYAGGLLINI GTLTDENWKL YQAALKIAEK YNVPVVLDPV ACGAGEYRKK VADDLINNYK LAAIRGNAGE IASLVGIDVA SKGVDSAGVD NIDEIALAAN EKFNIPIVVT GEVDAIAVNG EVVTIHNGSA MMPKVIGTGC LLGAVVASFI GLEKGQELKS LETAMLVYNI AGEMAEKRPN GHLPGTFKVE FINALYEITD EDVKEFKRVK //