ID   THIM1_STRPI             Reviewed;         260 AA.
AC   B1IAN9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Hydroxyethylthiazole kinase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00228};
DE            Short=TH kinase 1 {ECO:0000255|HAMAP-Rule:MF_00228};
DE            Short=Thz kinase 1 {ECO:0000255|HAMAP-Rule:MF_00228};
GN   Name=thiM1 {ECO:0000255|HAMAP-Rule:MF_00228}; OrderedLocusNames=SPH_0804;
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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}.
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DR   EMBL; CP000936; ACA36964.1; -; Genomic_DNA.
DR   RefSeq; WP_000202454.1; NC_010380.1.
DR   AlphaFoldDB; B1IAN9; -.
DR   SMR; B1IAN9; -.
DR   EnsemblBacteria; ACA36964; ACA36964; SPH_0804.
DR   GeneID; 66805858; -.
DR   KEGG; spv:SPH_0804; -.
DR   HOGENOM; CLU_019943_0_2_9; -.
DR   OMA; KRPLVHN; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000002163; 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   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..260
FT                   /note="Hydroxyethylthiazole kinase 1"
FT                   /id="PRO_1000100428"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   260 AA;  27570 MW;  D883CEB1E02C2378 CRC64;
     MTSLKLLKEK APLVICITND VVKNFTANGL VALGASPAMS EFPADLEDLL KYAGGLLINI
     GTLTDENWKL YQAALKIAEK YNVPAVLDPV ACGAGEYRKK VADDLINNYK LAAIRGNAGE
     IASLVGIDVA SKGVDSAGVD NIDEIALAAN EKFNIPIVVT GEVDAIAVNG EVVTIHNGSA
     MMPKVIGTGC LLGAVVASFI GLEKGQELKS LETAMLVYNI AGEIAEKHPN GHLPGTFKVE
     FINALYEITD EDVKEFKRVK