ID   THIM2_STRPI             Reviewed;         267 AA.
AC   B1IAP6;
DT   22-SEP-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 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00228};
DE            Short=TH kinase 2 {ECO:0000255|HAMAP-Rule:MF_00228};
DE            Short=Thz kinase 2 {ECO:0000255|HAMAP-Rule:MF_00228};
GN   Name=thiM2 {ECO:0000255|HAMAP-Rule:MF_00228}; OrderedLocusNames=SPH_0811;
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; ACA36432.1; -; Genomic_DNA.
DR   RefSeq; WP_001155198.1; NC_010380.1.
DR   AlphaFoldDB; B1IAP6; -.
DR   SMR; B1IAP6; -.
DR   EnsemblBacteria; ACA36432; ACA36432; SPH_0811.
DR   GeneID; 66805865; -.
DR   KEGG; spv:SPH_0811; -.
DR   HOGENOM; CLU_019943_0_0_9; -.
DR   OMA; KPIMAEH; -.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..267
FT                   /note="Hydroxyethylthiazole kinase 2"
FT                   /id="PRO_0000383902"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   267 AA;  29186 MW;  7A0741B88C4B3AE9 CRC64;
     MQEFTNPFPI GSSSLIHCMT NEISCEMLAN GILALGCKPV MADDSREVLD FTKQSQALFI
     NLGHLSAEKE KAIRMAASYA NQSSLPMVVD AVGVTTSSIR KSLVKDLLDY RPTVLKGNMS
     EIRSLVGLKH HGVGVDASAK DQETEDLLQV LKDWCQTYPG MSFLVTGPKD LIVSKNQVAV
     LENGCTELDW ITGTGDLVGA LTAVFLSQGK TGFEASCLAV SYLNIAAEKI VVQGMGLEEF
     RYQVLNQLSL LRRDENWLDT IKGEVYE