ID   THIM_CLOPS              Reviewed;         265 AA.
AC   Q0STA0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=CPR_1337;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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.
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DR   EMBL; CP000312; ABG86073.1; -; Genomic_DNA.
DR   RefSeq; YP_698657.1; -.
DR   GeneID; 4205487; -.
DR   GenomeReviews; CP000312_GR; CPR_1337.
DR   KEGG; cpr:CPR_1337; -.
DR   TIGR; CPR_1337; -.
DR   HOGENOM; Q0STA0; -.
DR   OMA; Q0STA0; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN         1    265       Hydroxyethylthiazole kinase.
FT                                /FTId=PRO_1000021506.
FT   BINDING      36     36       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     112    112       ATP (By similarity).
FT   BINDING     160    160       ATP (By similarity).
FT   BINDING     187    187       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   265 AA;  29595 MW;  C60CCC5533A51D02 CRC64;
     MEVLKRENPL IHMITNYVTV NDLAQVTINY GGLPLMATHH DELKVITKMA NGLLVNIGTL
     EPYQMESSMI SMKIAKEKGI PSVLDSVCVQ VSKLRRDFAK KIILEGEPSL IKGNLAEIKT
     LIGETSNSIG IDSFEDSLSE NTKNKIKEYA KERNLIVVVS GVVDFITNGE ESASVKNGTY
     KMSKITGTGC MLGALLTLAL SFYDHKDLRF KEVVKAVSTW GICGELAEER LREKEGLMTF
     KYNLLDELSI INDEIIKERE KVIYE
//