ID THIM_CHLAA Reviewed; 269 AA. AC A9WDL9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 78. 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=Caur_0375; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl; RX PubMed=21714912; DOI=10.1186/1471-2164-12-334; RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.; RT "Complete genome sequence of the filamentous anoxygenic phototrophic RT bacterium Chloroflexus aurantiacus."; RL BMC Genomics 12:334-334(2011). 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; CP000909; ABY33625.1; -; Genomic_DNA. DR RefSeq; WP_012256281.1; NC_010175.1. DR RefSeq; YP_001634014.1; NC_010175.1. DR AlphaFoldDB; A9WDL9; -. DR SMR; A9WDL9; -. DR STRING; 324602.Caur_0375; -. DR EnsemblBacteria; ABY33625; ABY33625; Caur_0375. DR KEGG; cau:Caur_0375; -. DR PATRIC; fig|324602.8.peg.427; -. DR eggNOG; COG2145; Bacteria. DR HOGENOM; CLU_019943_0_1_0; -. DR InParanoid; A9WDL9; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000002008; 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 PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1. DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 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 Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1..269 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_1000078215" FT BINDING 46 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 122 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 168 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 195 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" SQ SEQUENCE 269 AA; 28199 MW; 33C10B1319BA9EA5 CRC64; MTLNERIAEL RERVRQQRPL IHHITNFVVM NDTANVTLHI GGLPVMAHDR AEVAEMVTAA GALVLNVGTL SPDWIEAMLI AGRRANELGI PIVLDPVGAG ATSLRTASNR RLLEELQIAV VRGNSGEIGA LAGMGGVVKG VETVVEVDDP TAAAKALAQQ YRTVVAVTGR QDVVTDGKRV FLVDNGHEWL KTLTGTGCSA TTVIAAFAAV EREYPFAAAA ALACFGLAAE LAAPAARGPA SFKVAFYDAI YHLSADQIRA GARVTAVAG //