ID   THIM_DESPS              Reviewed;         273 AA.
AC   Q6AQZ6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE            EC=2.7.1.50 {ECO:0000255|HAMAP-Rule:MF_00228};
DE   AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE            Short=TH kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE            Short=Thz kinase {ECO:0000255|HAMAP-Rule:MF_00228};
GN   Name=thiM {ECO:0000255|HAMAP-Rule:MF_00228}; OrderedLocusNames=DP0499;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC       methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|HAMAP-
CC       Rule:MF_00228}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-
CC         phosphooxyethyl)-thiazole + ADP + H(+); Xref=Rhea:RHEA:24212,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17957, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58296, ChEBI:CHEBI:456216; EC=2.7.1.50;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00228};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00228};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC       methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-
CC       methylthiazole: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00228}.
CC   -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00228}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG35228.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR522870; CAG35228.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041277537.1; NC_006138.1.
DR   AlphaFoldDB; Q6AQZ6; -.
DR   SMR; Q6AQZ6; -.
DR   STRING; 177439.DP0499; -.
DR   KEGG; dps:DP0499; -.
DR   eggNOG; COG2145; Bacteria.
DR   HOGENOM; CLU_019943_0_1_7; -.
DR   OrthoDB; 8909021at2; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000000602; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01170; THZ_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_00228; Thz_kinase; 1.
DR   InterPro; IPR000417; Hyethyz_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR00694; thiM; 1.
DR   Pfam; PF02110; HK; 1.
DR   PIRSF; PIRSF000513; Thz_kinase; 1.
DR   PRINTS; PR01099; HYETHTZKNASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..273
FT                   /note="Hydroxyethylthiazole kinase"
FT                   /id="PRO_0000383853"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   273 AA;  28652 MW;  DCF61E401D81E147 CRC64;
     MSNISLTAAE NLQQIRENKP LIHNITNFVV MNYTANVLLA TGASPVMAHA QNEVEEMVAF
     AGSLVLNIGT LSESWVSSML MASQRANTLK TPIILDPVGS GATAFRTASA KRIIAEAKVS
     VIRGNASEIL SLGSEQSNTR GVDTSQSVSD AAQTASLLAR ELDTILAITG PTDLVTDGRR
     VFNVDNGHPL MPYVTGTGCS ATAVVGAFAA VDRDYLRAAT TALAFFGLAG EMAGKAATGP
     GSFMIHLLDA LYNMSPEQLE KGCRIKESSA TRS
//