ID THIM_KLEP7 Reviewed; 257 AA. AC A6TBJ8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 84. 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=KPN78578_25080; ORFNames=KPN_02551; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=272620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578; RG The Klebsiella pneumonia Genome Sequencing Project; RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; RL Submitted (SEP-2006) 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; CP000647; ABR77969.1; -; Genomic_DNA. DR RefSeq; WP_015875043.1; NC_009648.1. DR PDB; 6JYY; X-ray; 2.00 A; A/B/C=1-257. DR PDBsum; 6JYY; -. DR AlphaFoldDB; A6TBJ8; -. DR SMR; A6TBJ8; -. DR STRING; 272620.KPN_02551; -. DR jPOST; A6TBJ8; -. DR PaxDb; 272620-KPN_02551; -. DR EnsemblBacteria; ABR77969; ABR77969; KPN_02551. DR KEGG; kpn:KPN_02551; -. DR HOGENOM; CLU_019943_0_1_6; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000000265; 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..257 FT /note="Hydroxyethylthiazole kinase" FT /id="PRO_0000336562" FT BINDING 49 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228" FT BINDING 124 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" FT HELIX 10..20 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 23..27 FT /evidence="ECO:0007829|PDB:6JYY" FT TURN 30..32 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 33..42 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 53..60 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 75..91 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:6JYY" FT TURN 100..104 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 106..116 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 127..134 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 171..180 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 190..194 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 198..210 FT /evidence="ECO:0007829|PDB:6JYY" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 216..235 FT /evidence="ECO:0007829|PDB:6JYY" FT HELIX 240..251 FT /evidence="ECO:0007829|PDB:6JYY" SQ SEQUENCE 257 AA; 26117 MW; 5C7582B4D9F9A382 CRC64; MPELLNPAPV AHLRHLLRAH SPLVHCMTND VVQTFTANVL LAVGASPAMV IDPREAAQFA AIADALLINV GTLTEDRAVA MRAAVEHARQ AGKPWTLDPV AVGALTVRTA FCHELLALQP AAIRGNASEI LALAGMSAGG RGVDTTDTAA AALPAAQALA RRLATVVAVT GEVDYVTDGE RVLSVAGGNP LMTRVVGTGC ALSAVVAASA ALPGDRLENV AAACGLMKQA GAIAARQGGP GSFIPAFLDA LYQEVQG //