ID THIM_SYNAS Reviewed; 270 AA. AC Q2LWX9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 89. 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=SYNAS_27070; ORFNames=SYN_00303; OS Syntrophus aciditrophicus (strain SB). OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae; OC Syntrophus. OX NCBI_TaxID=56780; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB; RX PubMed=17442750; DOI=10.1073/pnas.0610456104; RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S., RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A., RA Campbell J.W., Gunsalus R.P.; RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit RT of microbial growth."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007). 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; CP000252; ABC78586.1; -; Genomic_DNA. DR RefSeq; WP_011418605.1; NC_007759.1. DR AlphaFoldDB; Q2LWX9; -. DR SMR; Q2LWX9; -. DR STRING; 56780.SYN_00303; -. DR KEGG; sat:SYN_00303; -. DR eggNOG; COG2145; Bacteria. DR HOGENOM; CLU_019943_0_1_7; -. DR InParanoid; Q2LWX9; -. DR OrthoDB; 8909021at2; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000001933; 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 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..270 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_0000336574" FT BINDING 47 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 170 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 197 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" SQ SEQUENCE 270 AA; 28368 MW; 5A105140C331DA2F CRC64; MQITPENTWA AVKAIRSRAP LIHNITNYVV MNSTANALLA LGASPVMAHA QEEVEEMVGI AQALVVNIGT LSPSWVRAMA SAALKAADRG IPIILDPVGA GATAYRTRTA FQLLETVSPT IIRGNASEIL AFESVETMET RGVDSTELSQ NAVDAGRRLN DSYGSTVCIS GETDFIIGDR AILGIRNGHP LMTRVTGLGC TASALCGAFA AVNSSFTLAA AQAMAVMGIA GEMAAEISPG PGSLQLHFLD ILYRLTEEDI ARRLRIVAGE //