ID   THIM_MOOTA              Reviewed;         267 AA.
AC   Q2RGX6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=Moth_2017;
OS   Moorella thermoacetica (strain ATCC 39073).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteriaceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f.
RT   Clostridium thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC20313.1; -; Genomic_DNA.
DR   RefSeq; YP_430856.1; -.
DR   GeneID; 3831971; -.
DR   GenomeReviews; CP000232_GR; Moth_2017.
DR   KEGG; mta:Moth_2017; -.
DR   NMPDR; fig|264732.9.peg.2034; -.
DR   HOGENOM; Q2RGX6; -.
DR   OMA; Q2RGX6; ASPVMAH.
DR   BioCyc; MTHE264732:MOTH_2017-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    267       Hydroxyethylthiazole kinase.
FT                                /FTId=PRO_1000021523.
FT   BINDING      46     46       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     122    122       ATP (By similarity).
FT   BINDING     168    168       ATP (By similarity).
FT   BINDING     195    195       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   267 AA;  27779 MW;  FDAEF4164D4F0BBD CRC64;
     MNWGEQVASR RQRVHEQRPL VHHITNLVVT NLTANVTLAI GASPVMAYAR EEVADMARLA
     QAVVLNMGTL TGDVVEAMLL AGKAANNAGI PVVFDPVGAG ATPFRTRTAQ KIIKELHIDI
     LRGNASEIAS IGGFGGHTKG VDAAGAPARV AEMVKQVARD LNTVVAVTGA TDYISDGERL
     IAVDNGHPLL TFVTGTGCSA TSIIAAFRAV EEDGVTASTA ALAYYGLAAE RAAAVSQGPA
     SFQVALLDTL YNLAGEELAR GVKIRLL
//