ID THIM_SALPC Reviewed; 265 AA. AC C0Q0Y8; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 64. DE RecName: Full=Hydroxyethylthiazole kinase {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 {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=TH kinase {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=Thz kinase {ECO:0000255|HAMAP-Rule:MF_00228}; GN Name=thiM {ECO:0000255|HAMAP-Rule:MF_00228}; GN OrderedLocusNames=SPC_1556; OS Salmonella paratyphi C (strain RKS4594). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=476213; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RKS4594; RX PubMed=19229335; DOI=10.1371/journal.pone.0004510; RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H., RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.; RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis RT and pathogenic convergence with Salmonella typhi."; RL PLoS ONE 4:E4510-E4510(2009). 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; CP000857; ACN45707.1; -; Genomic_DNA. DR RefSeq; WP_001182162.1; NC_012125.1. DR AlphaFoldDB; C0Q0Y8; -. DR SMR; C0Q0Y8; -. DR KEGG; sei:SPC_1556; -. DR HOGENOM; CLU_019943_0_1_6; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000001599; 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..265 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_1000198129" FT BINDING 50 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 125 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 171 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" SQ SEQUENCE 265 AA; 27574 MW; 9DBF3D1B04335B5C CRC64; MQPDLHCRTL AAHTLKHFRA LSPLTHCMTN DVVQTFTANT LLALGASPAM VIDPVEARPF AAIANALLVN VGTLTASRAD AMRAAVESAY DAKTPWTLDP VAVGALEFRR RFCLDLLSLR PAAIRGNASE ILALSGMALG GRGVDTTEAA LAALPAAQAL AHQIDCIVVV TREIDYVTNG QRTLSIPGGD PLMTRIVGTG CALSAVVAAS CALPGAALDN VASACCWMKL AGQAAAERSE GPGSFIPAFL DALYHLDVEA ANEEN //