ID THIM_STAAR Reviewed; 263 AA. AC Q6GEY3; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 99. 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=SAR2181; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSA252; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence RT for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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; BX571856; CAG41161.1; -; Genomic_DNA. DR RefSeq; WP_001108496.1; NC_002952.2. DR PDB; 5CGA; X-ray; 1.87 A; A/B/C/E/F/H=1-263. DR PDB; 5CGE; X-ray; 1.62 A; A/B/C/D/E/F=1-263. DR PDB; 5CM5; X-ray; 2.09 A; A/B/C/D/E/F=1-263. DR PDB; 5COJ; X-ray; 1.90 A; A/B/C/E/F/H=1-263. DR PDBsum; 5CGA; -. DR PDBsum; 5CGE; -. DR PDBsum; 5CM5; -. DR PDBsum; 5COJ; -. DR AlphaFoldDB; Q6GEY3; -. DR SMR; Q6GEY3; -. DR KEGG; sar:SAR2181; -. DR HOGENOM; CLU_019943_0_2_9; -. DR BRENDA; 2.7.1.50; 3352. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000000596; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. FT CHAIN 1..263 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_0000156955" 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" FT HELIX 2..10 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:5CGE" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 43..52 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 65..81 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 85..88 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 96..108 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 118..125 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:5CM5" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 142..153 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 155..168 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 188..198 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 208..227 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 234..247 FT /evidence="ECO:0007829|PDB:5CGE" FT HELIX 250..256 FT /evidence="ECO:0007829|PDB:5CGE" FT STRAND 259..263 FT /evidence="ECO:0007829|PDB:5CGE" SQ SEQUENCE 263 AA; 28040 MW; 6072DA60FF96F1AA CRC64; MNYLNNIRIE NPLTICYTND VVKNFTANGL LSIGASPAMS EAPEEAEEFY KVAQALLINI GTLTAQNEQD IIAIAQTANE AGLPIVFDPV AVGASTYRKQ FCKLLLKSAK VSVIKGNASE ILALIDDTAT MKGTDSDANL DAVTIAKKAY AIYKTAIVIT GKEDVIVQGD KAIVLANGSP LLARVTGAGC LLGGIIAGFL FRETEPDIEA LIEAVSVFNI AAEVAAENEN CGGPGTFSPL LLDTLYHLNE TTYQQRIRIQ EVE //