ID THIM2_CLOBJ Reviewed; 265 AA. AC C1FR28; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Hydroxyethylthiazole kinase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=TH kinase 2 {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=Thz kinase 2 {ECO:0000255|HAMAP-Rule:MF_00228}; GN Name=thiM2 {ECO:0000255|HAMAP-Rule:MF_00228}; GN OrderedLocusNames=CLM_2460; OS Clostridium botulinum (strain Kyoto / Type A2). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyoto / Type A2; RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.; RT "Genome sequence of Clostridium botulinum A2 Kyoto."; RL Submitted (OCT-2008) 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; CP001581; ACO83484.1; -; Genomic_DNA. DR RefSeq; WP_003358296.1; NC_012563.1. DR AlphaFoldDB; C1FR28; -. DR SMR; C1FR28; -. DR KEGG; cby:CLM_2460; -. DR eggNOG; COG2145; Bacteria. DR HOGENOM; CLU_019943_0_0_9; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000001374; 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..265 FT /note="Hydroxyethylthiazole kinase 2" FT /id="PRO_0000383844" 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 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 265 AA; 28737 MW; 29FA7E43C251753A CRC64; MQIRQSVKFK KPLIHYITNP ISINDCANMI LAVGAKPIMA EHPLEVSEIT SISESLGINL GNITDNKMKS MLISGKISYE KKIPQVIDLV GVGCSKLRLD YAKKFILECH PNVIKGNMSE MKAIYGIKSS AKGIDVGACD IITEQNFDEN IEMIKRLSME TGSVVAATGV VDIISNGTYT YIISNGCEML SMITGTGCML TGIIASYISS GNILEGTALA IVLMGICGEL SQHVKGTGSF RNELIDNIFS ISDDIIIKKI RINSY //