ID THIM_ENTFA Reviewed; 272 AA. AC Q830K4; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 103. 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=EF_2777; OS Enterococcus faecalis (strain ATCC 700802 / V583). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=226185; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700802 / V583; RX PubMed=12663927; DOI=10.1126/science.1080613; RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C., RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.; RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus RT faecalis."; RL Science 299:2071-2074(2003). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS). RC STRAIN=ATCC 700802 / V583; RG Joint center for structural genomics (JCSG); RT "Crystal structure of 4-methyl-5-(beta-hydroxyethyl)thiazole kinase RT (np_816404.1) from Enterococcus faecalis V583 at 2.57 A resolution."; RL Submitted (FEB-2009) to the PDB data bank. 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; AE016830; AAO82474.1; -; Genomic_DNA. DR RefSeq; NP_816404.1; NC_004668.1. DR RefSeq; WP_002387209.1; NZ_KE136528.1. DR PDB; 3DZV; X-ray; 2.57 A; A/B=1-272. DR PDBsum; 3DZV; -. DR AlphaFoldDB; Q830K4; -. DR SMR; Q830K4; -. DR STRING; 226185.EF_2777; -. DR DNASU; 1201627; -. DR EnsemblBacteria; AAO82474; AAO82474; EF_2777. DR KEGG; efa:EF2777; -. DR PATRIC; fig|226185.45.peg.793; -. DR eggNOG; COG2145; Bacteria. DR HOGENOM; CLU_019943_0_0_9; -. DR UniPathway; UPA00060; UER00139. DR EvolutionaryTrace; Q830K4; -. DR Proteomes; UP000001415; 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; Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1..272 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_0000383858" FT BINDING 44 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 199 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 18..22 FT /evidence="ECO:0007829|PDB:3DZV" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 28..37 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 51..55 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 70..85 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:3DZV" FT TURN 95..98 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 101..112 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 122..128 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 147..163 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 168..179 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 184..187 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 200..214 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 218..239 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 243..256 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:3DZV" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:3DZV" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:3DZV" SQ SEQUENCE 272 AA; 29719 MW; 87AD9F1B009874F2 CRC64; MKTSVKFETI FPLTTAPLIQ CITNEITCES MANALLYIDA KPIMADDPRE FPQMFQQTSA LVLNLGHLSQ EREQSLLAAS DYARQVNKLT VVDLVGYGAS DIRNEVGEKL VHNQPTVVKG NLSEMRTFCQ LVSHGRGVDG SPLDQSEEAI EELIQALRQQ TQKFPQTVFL ATGIQDVLVS QEQVIVLQNG VPELDCFTGT GDLVGALVAA LLGEGNAPMT AAVAAVSYFN LCGEKAKTKS QGLADFRQNT LNQLSLLMKE KDWFEAVKGR VL //