ID THIM1_CLOBL Reviewed; 263 AA. AC A7GAL1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 83. 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=CLI_0535; OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441772; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Langeland / NCTC 10281 / Type F; RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D., RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4- CC methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|HAMAP- CC Rule:MF_00228}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2- CC phosphooxyethyl)-thiazole + ADP + H(+); Xref=Rhea:RHEA:24212, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17957, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:58296, ChEBI:CHEBI:456216; EC=2.7.1.50; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00228}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00228}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4- CC 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; CP000728; ABS41348.1; -; Genomic_DNA. DR RefSeq; WP_011987460.1; NC_009699.1. DR AlphaFoldDB; A7GAL1; -. DR SMR; A7GAL1; -. DR KEGG; cbf:CLI_0535; -. DR HOGENOM; CLU_019943_0_0_9; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000002410; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; 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 NCBIfam; TIGR00694; thiM; 1. DR Pfam; PF02110; HK; 1. DR PIRSF; PIRSF000513; Thz_kinase; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF53613; Ribokinase-like; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. FT CHAIN 1..263 FT /note="Hydroxyethylthiazole kinase 1" FT /id="PRO_0000336549" FT BINDING 42 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 164 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" SQ SEQUENCE 263 AA; 28464 MW; 8F3C24E8D5D034BE CRC64; MKNKNVIQKM REKIPLIHCI TNYVTINDCA NILLSFGASP AMCEAYDEVY DFVSISSALY INLGTLTKEQ ETAAVLASIS AKNHNVPVVI DPVGCPAIKR KVEVINRIAE VGRIDIIKGN IGEIKFLAGM DSETRGVDSL DNGENALNAC TQLAKKYNCI VAATGQKDFV SDGKRGSVIK NGTEMLTKVT GAGCMLGALC AATCANFEDK LVSTTAAILS MNIAGEKAYE KAQLPGSFRI ALIDNIYMIS DEEIWERGNV EWK //