ID THIM_PYRHO Reviewed; 265 AA. AC O58877; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 137. 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}; OrderedLocusNames=PH1157; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC OS 100139 / OT-3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=70601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RG RIKEN structural genomics initiative (RSGI); RT "Structure of hydroxyethylthiazole kinase protein from Pyrococcus RT horikoshii OT3."; RL Submitted (JUN-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; BA000001; BAA30257.1; -; Genomic_DNA. DR PIR; G71057; G71057. DR RefSeq; WP_010885242.1; NC_000961.1. DR PDB; 3HPD; X-ray; 1.85 A; A=1-265. DR PDBsum; 3HPD; -. DR AlphaFoldDB; O58877; -. DR SMR; O58877; -. DR STRING; 70601.gene:9378118; -. DR EnsemblBacteria; BAA30257; BAA30257; BAA30257. DR GeneID; 1443477; -. DR KEGG; pho:PH1157; -. DR eggNOG; arCOG00019; Archaea. DR OrthoDB; 214286at2157; -. DR BRENDA; 2.7.1.50; 7183. DR UniPathway; UPA00060; UER00139. DR EvolutionaryTrace; O58877; -. DR Proteomes; UP000000752; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. FT CHAIN 1..265 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_0000156972" FT BINDING 43 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 165 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT HELIX 2..14 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 17..21 FT /evidence="ECO:0007829|PDB:3HPD" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 27..37 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:3HPD" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 50..56 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 69..85 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 100..112 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 115..120 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 121..131 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 144..157 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 160..172 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 185..189 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 193..205 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 210..231 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 235..248 FT /evidence="ECO:0007829|PDB:3HPD" FT HELIX 251..257 FT /evidence="ECO:0007829|PDB:3HPD" FT STRAND 260..263 FT /evidence="ECO:0007829|PDB:3HPD" SQ SEQUENCE 265 AA; 28954 MW; 5D38EB1846CA02BA CRC64; MKFIIEALKR VRERRPLVHN ITNFVVMNTT ANALLALGAS PVMAHAEEEL EEMIRLADAV VINIGTLDSG WRRSMVKATE IANELGKPIV LDPVGAGATK FRTRVSLEIL SRGVDVLKGN FGEISALLGE EGKTRGVDSL EYGEEEAKKL TMNAAREFNT TVAVTGAVDY VSDGRRTFAV YNGHELLGRV TGTGCMVAAL TGAFVAVTEP LKATTSALVT FGIAAEKAYE EAKYPGSFHV KLYDWLYRIN ENVIRTYAKV REVEL //