ID THIM_BACLD Reviewed; 269 AA. AC Q65DJ9; Q62P19; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 16-JUN-2009, entry version 35. 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=BLi04052, BL03865; OS Bacillus licheniformis (strain DSM 13 / ATCC 14580). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., RA Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., RA Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an RT organism with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., RA Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., RA Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., RA Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004). 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; CP000002; AAU25492.1; -; Genomic_DNA. DR EMBL; AE017333; AAU42865.1; -; Genomic_DNA. DR RefSeq; YP_081130.1; -. DR RefSeq; YP_093558.1; -. DR GeneID; 3030181; -. DR GeneID; 3099156; -. DR GenomeReviews; AE017333_GR; BLi04052. DR GenomeReviews; CP000002_GR; BL03865. DR KEGG; bld:BLi04052; -. DR KEGG; bli:BL03865; -. DR NMPDR; fig|279010.5.peg.3173; -. DR HOGENOM; Q65DJ9; -. DR OMA; Q65DJ9; ASPVMAH. DR BioCyc; BLIC279010:BL03865-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 1 269 Hydroxyethylthiazole kinase. FT /FTId=PRO_1000021501. FT BINDING 45 45 Substrate; via amide nitrogen (By FT similarity). FT BINDING 121 121 ATP (By similarity). FT BINDING 167 167 ATP (By similarity). FT BINDING 194 194 Substrate; via amide nitrogen (By FT similarity). SQ SEQUENCE 269 AA; 28240 MW; DB464AB32443BCE7 CRC64; MNMEDAARGI ELVRKQKPLV HNMTNNVVTN FTANGLLALG ASPVMAYARE EAADMAKIAG ALVLNIGTLS RESVEAMIIA GKSANEHGVP VIFDPVGAGA TPFRTESAQA IMRKVKVSAV RGNAAEIANT LGEDWLIKGV DAGEESGDRT ELAKKAAKLW DTAVIITGAE DVITDGTKTY TVGNGHQLLT KVTGTGCLFT SVIGAFCAVE KDVCRAAVSA AAFYGTAAEL AAAKTESRGP GSFQIEFLNQ LAAVEAMDIK ERGRIREVE //