ID THIM_PSYIN Reviewed; 267 AA. AC A1SX95; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 89. 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=Ping_2373; OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17664 / CCUG 51855 / 37; RX PubMed=18460197; DOI=10.1186/1471-2164-9-210; RA Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J., RA Land M.L., Thompson L.S.; RT "Genomics of an extreme psychrophile, Psychromonas ingrahamii."; RL BMC Genomics 9:210-210(2008). 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; CP000510; ABM04110.1; -; Genomic_DNA. DR RefSeq; WP_011770670.1; NC_008709.1. DR AlphaFoldDB; A1SX95; -. DR SMR; A1SX95; -. DR STRING; 357804.Ping_2373; -. DR KEGG; pin:Ping_2373; -. DR eggNOG; COG2145; Bacteria. DR HOGENOM; CLU_019943_0_1_6; -. DR OrthoDB; 8909021at2; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000000639; 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 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 Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1..267 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_0000383888" FT BINDING 51 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 127 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 173 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 200 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" SQ SEQUENCE 267 AA; 27860 MW; 3B067CEB9D73602E CRC64; MKKNIDSNIK TIVSALKTLR EQKPLVVNIS NYVAMNNTAN ALLALGASPI MAHSRDEMAE MLSFSGALVV NIGTLDSLWI PRMLFAVEQA NIHKKTVVLD PVGCGASSLR TATSWQIAEA ANKLIIRGNA SEIIALAGEK GQSKGVDSLD SSEAALGAAR YLRDTYQCAV VISGATDFIV TAGGQIQLNN GHAMMPYVTA MGCTLSALTG AFAAVGEETG LAAAAVLGVA GEIAAEQSKG PGSLQLNLLD ALYQLDEATL IQRLKLS //