ID   THIM1_STRPS             Reviewed;         260 AA.
AC   B2IN99;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 71.
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=SPCG_0666;
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14;
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(2009).
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=ACB89918.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001033; ACB89918.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000202464.1; NC_010582.1.
DR   AlphaFoldDB; B2IN99; -.
DR   SMR; B2IN99; -.
DR   EnsemblBacteria; ACB89918; ACB89918; SPCG_0666.
DR   KEGG; spw:SPCG_0666; -.
DR   HOGENOM; CLU_019943_0_2_9; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000001682; 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_0000383900"
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;  27635 MW;  B1846DA024C97404 CRC64;
     MTSLKLLKEK APLVICITND VVKNFTANGL VALGASPAMS EFPADLEDLL KYAGGLLINI
     GTLTDENWKL YQAALKIAEK YNVPVVLDPV ACGAGEYRKK VADDLINNYK LAAIRGNAGE
     IASLVGIDVA SKGVDSAGVD NIDEIALAAN EKFNIPIVVT GEVDAIAVNG EVVTIHNGSA
     MMPKVIGTGC LLGAVVASFI GLEKGQELKS LETAMLVYNI AGEMAEKRPN GHLPGTFKVE
     FINALYEITD EDVKEFKRVK