ID THIM_STAA2 Reviewed; 263 AA. AC A6U3H8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 80. 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=SaurJH1_2167; OS Staphylococcus aureus (strain JH1). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=359787; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JH1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.; RT "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus RT JH1."; 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; CP000736; ABR52996.1; -; Genomic_DNA. DR AlphaFoldDB; A6U3H8; -. DR SMR; A6U3H8; -. DR KEGG; sah:SaurJH1_2167; -. DR HOGENOM; CLU_019943_0_2_9; -. DR UniPathway; UPA00060; UER00139. 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 Thiamine biosynthesis; Transferase. FT CHAIN 1..263 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_1000078218" FT BINDING 39 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 115 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 160 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" SQ SEQUENCE 263 AA; 28067 MW; B7D8DD02F2D8E98E CRC64; MNYLNKIRIE NPLTICYTND VVKNFTANGL LSIGASPAMS EAPEEAEEFY KVAQALLINI GTLTAQNEQD IIAIAQTANE AGLPIVFDPV AVGASTYRKQ FCKLLLKSAK VSVIKGNASE ILALIDDTAT MKGTDSDANL DAVAIAKKAY AIYKTAIVIT GKEDVIVQDN KAIVLANGSP LLARVTGAGC LLGGVIAGFL FRETEPDIEA LIEAVSVFNI AAEVAAENEN CGGPGTFSPL LLDTLYHLNE TTYQQRIRIQ EVE //