ID THIM_METMA Reviewed; 261 AA. AC Q8PS50; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 51. 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=MM_3234; OS Methanosarcina mazei (Methanosarcina frisia). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=2209; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88; RX MEDLINE=22120827; PubMed=12125824; RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., RA Fritz H.-J., Gottschalk G.; RT "The genome of Methanosarcina mazei: evidence for lateral gene RT transfer between Bacteria and Archaea."; RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002). CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity). 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; AE008384; AAM32930.1; -; Genomic_DNA. DR RefSeq; NP_635258.1; -. DR HSSP; P39593; 1EKQ. DR GeneID; 1481576; -. DR GenomeReviews; AE008384_GR; MM_3234. DR KEGG; mma:MM_3234; -. DR NMPDR; fig|192952.1.peg.3234; -. DR HOGENOM; Q8PS50; -. DR OMA; Q8PS50; ASPVMAH. DR BioCyc; MMAZ192952:MM3234-MON; -. DR BRENDA; 2.7.1.50; 261165. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. 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; Magnesium; Metal-binding; KW Nucleotide-binding; Thiamine biosynthesis; Transferase. FT CHAIN 1 261 Hydroxyethylthiazole kinase. FT /FTId=PRO_0000156969. FT METAL 89 89 Magnesium 1 (By similarity). FT METAL 121 121 Magnesium 1 (By similarity). FT BINDING 40 40 Substrate; via amide nitrogen (By FT similarity). FT BINDING 116 116 ATP (By similarity). FT BINDING 162 162 ATP (By similarity). FT BINDING 189 189 Substrate; via amide nitrogen (By FT similarity). SQ SEQUENCE 261 AA; 27555 MW; 5D5128BAEECBC3EC CRC64; MKNPLKTIRE TKPLVHHITN WVTIYDCANI TRAFGALPVM AHAPEECADM TGISSALVLN IGTLTSEIID SMLLSAAAAN KKKIPVVLDA VGVGATRFRD EMAAKILGSV RVDIIKGNYS EIAKLAGENA ETKGVESTSI SADPQKVAKE FAKSSSSVVV MTGKEDVISD GNRTFVVKNG HELMGSIVGT GCMAASIIGS FASVNPDYCD AAKDALCYFG AAGELAAKNS AGPGSFKVNL YDEVFNLSDE KVQAMMKVEE L //