ID   THIM_LEPBJ              Reviewed;         264 AA.
AC   Q04V49;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 16.
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=LBJ_0526;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A.,
RA   Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P.,
RA   Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ75221.1; -; Genomic_DNA.
DR   RefSeq; YP_799979.1; -.
DR   GeneID; 4409425; -.
DR   GenomeReviews; CP000350_GR; LBJ_0526.
DR   KEGG; lbj:LBJ_0526; -.
DR   OMA; Q04V49; ASPVMAH.
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    264       Hydroxyethylthiazole kinase.
FT                                /FTId=PRO_1000021516.
FT   BINDING      55     55       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     130    130       ATP (By similarity).
FT   BINDING     176    176       ATP (By similarity).
FT   BINDING     203    203       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   264 AA;  27495 MW;  FB4EEF5732113255 CRC64;
     MPKHSALERA WPAKEIVEDL LELRKRSPLT HIMTNIVVTN WTANVLLAVG ASPAMVIAEE
     EAGEFVKIAN GLLINVGTIT SNDAKAMKIA ATVAHQTNTP WVLDPVAVGA LGFRTETTKK
     LLDLKPTVIR GNASEILTLA GIAGKGKGVD STVNSKDALP YAQELSGKTG AVVAVSGEVD
     YVTNGKETIE IYGGDPIMTK VTGVGCSLGA LIASFLGIQK DPLRASASAS AVFAIAGSRS
     AKKSNGPGSF AINFIDQLSQ LSIE
//