THIM_STAAR
ID THIM_STAAR Reviewed; 263 AA.
AC Q6GEY3;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=SAR2181;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG41161.1; -; Genomic_DNA.
DR RefSeq; WP_001108496.1; NC_002952.2.
DR PDB; 5CGA; X-ray; 1.87 A; A/B/C/E/F/H=1-263.
DR PDB; 5CGE; X-ray; 1.62 A; A/B/C/D/E/F=1-263.
DR PDB; 5CM5; X-ray; 2.09 A; A/B/C/D/E/F=1-263.
DR PDB; 5COJ; X-ray; 1.90 A; A/B/C/E/F/H=1-263.
DR PDBsum; 5CGA; -.
DR PDBsum; 5CGE; -.
DR PDBsum; 5CM5; -.
DR PDBsum; 5COJ; -.
DR AlphaFoldDB; Q6GEY3; -.
DR SMR; Q6GEY3; -.
DR KEGG; sar:SAR2181; -.
DR HOGENOM; CLU_019943_0_2_9; -.
DR OMA; KRPLVHN; -.
DR OrthoDB; 1717689at2; -.
DR BRENDA; 2.7.1.50; 3352.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000000596; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Thiamine biosynthesis; Transferase.
FT CHAIN 1..263
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000156955"
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"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5CGE"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5CM5"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 155..168
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 208..227
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:5CGE"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:5CGE"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:5CGE"
SQ SEQUENCE 263 AA; 28040 MW; 6072DA60FF96F1AA CRC64;
MNYLNNIRIE NPLTICYTND VVKNFTANGL LSIGASPAMS EAPEEAEEFY KVAQALLINI
GTLTAQNEQD IIAIAQTANE AGLPIVFDPV AVGASTYRKQ FCKLLLKSAK VSVIKGNASE
ILALIDDTAT MKGTDSDANL DAVTIAKKAY AIYKTAIVIT GKEDVIVQGD KAIVLANGSP
LLARVTGAGC LLGGIIAGFL FRETEPDIEA LIEAVSVFNI AAEVAAENEN CGGPGTFSPL
LLDTLYHLNE TTYQQRIRIQ EVE
