ID   THIM_LEPCP              Reviewed;         278 AA.
AC   B1Y3E4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 69.
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=Lcho_2206;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000255|HAMAP-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=ACB34472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001013; ACB34472.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043704194.1; NC_010524.1.
DR   AlphaFoldDB; B1Y3E4; -.
DR   SMR; B1Y3E4; -.
DR   STRING; 395495.Lcho_2206; -.
DR   EnsemblBacteria; ACB34472; ACB34472; Lcho_2206.
DR   KEGG; lch:Lcho_2206; -.
DR   eggNOG; COG2145; Bacteria.
DR   HOGENOM; CLU_019943_0_1_4; -.
DR   OrthoDB; 1717689at2; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000001693; 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   Pfam; PF02110; HK; 1.
DR   PIRSF; PIRSF000513; Thz_kinase; 1.
DR   PRINTS; PR01099; HYETHTZKNASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00694; thiM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..278
FT                   /note="Hydroxyethylthiazole kinase"
FT                   /id="PRO_0000383879"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   278 AA;  28439 MW;  E5462D3D455E51D1 CRC64;
     MSLAAPLTAA DLWADVLAVR AQSPLVHSIT NFVVMNFNAN VLLALGAAPV MAHAHDEVAD
     MAGIAQALVL NIGTLEPAWV ESMHKARRAA RARGIPVVLD PVGAGATAYR NRALSGLLAA
     GAPTVIRGNG SEVLSVAGLG APTRGVDSTL SSNDAVAAAQ TLSRRIGSVV CVSGADDHVV
     DALGRWATLS NGHPWMTRIT GVGCSATAMI GAFAAVQPDA WRATTAAMAY LGVVGEWAAE
     QVIAAGNGVG SLQVKLLDGL QLLDDATFRA RLKMTVHG