ID THIM_HAES1 Reviewed; 266 AA. AC Q0I129; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Hydroxyethylthiazole kinase; DE EC=2.7.1.50; DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase; DE Short=Thz kinase; DE Short=TH kinase; GN Name=thiM; OrderedLocusNames=HS_0092; OS Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=205914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17172329; DOI=10.1128/JB.01422-06; RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., RA Xie G., Inzana T.J.; RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) RT strain 129Pt and comparison to Haemophilus ducreyi 35000HP and RT Haemophilus influenzae Rd."; RL J. Bacteriol. 189:1890-1898(2007). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- PATHWAY: Cofactor biosynthesis; thiamine pyrophosphate CC biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 4-methyl- CC 5-(2-hydroxyethyl)-thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the Thz kinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000436; ABI24373.1; -; Genomic_DNA. DR RefSeq; YP_718299.1; -. DR GeneID; 4239601; -. DR GenomeReviews; CP000436_GR; HS_0092. DR KEGG; hso:HS_0092; -. DR NMPDR; fig|205914.1.peg.1251; -. DR HOGENOM; Q0I129; -. DR OMA; Q0I129; ASPVMAH. DR BioCyc; HSOM205914:HS_0092-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:HAMAP. DR GO; GO:0009228; P:thiamin biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00228; -; 1. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR011144; Hyethyz_kinsmonf. DR PANTHER; PTHR20857:SF14; Hyethyz_kinase; 1. DR Pfam; PF02110; HK; 1. DR PIRSF; PIRSF000513; Thz_kinase; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 266 Hydroxyethylthiazole kinase. FT /FTId=PRO_0000336560. FT BINDING 41 41 Substrate; via amide nitrogen (By FT similarity). FT BINDING 117 117 ATP (By similarity). FT BINDING 163 163 ATP (By similarity). FT BINDING 190 190 Substrate; via amide nitrogen (By FT similarity). SQ SEQUENCE 266 AA; 28152 MW; CE24FC71334828B8 CRC64; MNSQFLTKLR QRNPLIHNIT NIVAANFSAN GLLAIGASPI MSACIEEMEE MAKLSQSLVI NIGTLTGKDV EAMLLAGKTA NQVGIPVVLD PVGVGATTFR QKTTALLLEQ VQFSAIRGNA GELAYIAGVQ WSTKGVDAGK GMADIAEIAH LVARKYQCIA VISGETDYIS DGKRLAKLNN GTPLFPKITA SGCLLSAVCS AFLAVAEQKD YFDALVEGCS AYAIAGEIAA QSLSSTQFGQ FTLGLLDQLA SLTPEQINQY ARISYE //