THIM2_STRPN
ID THIM2_STRPN Reviewed; 267 AA.
AC Q97RR9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SP_0724;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; AE005672; AAK74865.1; -; Genomic_DNA.
DR PIR; D97951; D97951.
DR PIR; H95083; H95083.
DR RefSeq; WP_001155185.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97RR9; -.
DR SMR; Q97RR9; -.
DR STRING; 170187.SP_0724; -.
DR EnsemblBacteria; AAK74865; AAK74865; SP_0724.
DR GeneID; 60232532; -.
DR KEGG; spn:SP_0724; -.
DR eggNOG; COG2145; Bacteria.
DR OMA; KPIMAEH; -.
DR PhylomeDB; Q97RR9; -.
DR BioCyc; SPNE170187:G1FZB-743-MON; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000000585; 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_0000383896"
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; 29081 MW; 70B2FBA10D231FA1 CRC64;
MQEFTNPFPI GSSSLIHCIT NEISCEMLAN GILALGCKPV MADDSREVLD FTKQSQALFI
NLGHLSAEKE KAIRMAASYA NQSSLPMVVD AVGVTTSSIR KSLVKDLLDY RPTVLKGNMS
EIRSLVGLKH HGVGVDASAK DQETEDLLQV LKDWCQTYPG MSFLVTGPKD LVVSKNQVAV
LGNGCTELDW ITGTGDLVGA LTAVFLSQGK TGFEASCLAV SYLNIAAEKI VVQGMGLEEF
RYQVLNQLSL LRRDENWLDT IKGEVYE
