ID THIM_SOLM1 Reviewed; 266 AA. AC C4XIJ3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 72. 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=DMR_30770; OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1) OS (Desulfovibrio magneticus). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Solidesulfovibrio. OX NCBI_TaxID=573370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700980 / DSM 13731 / RS-1; RX PubMed=19675025; DOI=10.1101/gr.088906.108; RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N., RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H., RA Matsunaga T.; RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed RT common gene clusters in magnetotactic bacteria."; RL Genome Res. 19:1801-1808(2009). 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; AP010904; BAH76568.1; -; Genomic_DNA. DR RefSeq; WP_015861727.1; NC_012796.1. DR AlphaFoldDB; C4XIJ3; -. DR SMR; C4XIJ3; -. DR STRING; 573370.DMR_30770; -. DR KEGG; dma:DMR_30770; -. DR eggNOG; COG2145; Bacteria. DR HOGENOM; CLU_019943_0_1_7; -. DR OrthoDB; 8909021at2; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000009071; 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 Thiamine biosynthesis; Transferase. FT CHAIN 1..266 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_1000204358" 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 266 AA; 26257 MW; 2807B3B4BB398CDC CRC64; MPFAAAVFAD LARIRQNAPL VVNITNNVVT NATANALLAL GASPAMTHHP ADAAELAALA GALVCNMGTP GGENIEAMLA AGGAANAGGV PVVFDPVAAG VTSRRREVAG RMLETVRLAA VRGNASEILA LAGEAALSKG ADSQHASREA APAAVALARS LGCTVCVSGE VDVVTDGERV VELAGGHAMM TRVTGLGCTA TAFVGAFLAV NPDYFAATCH AMAVMAAAGR LAAAGVAGPG SLAVRFLDVV YSLTEAEIAA GARVSA //