THIM_ENTFA
ID THIM_ENTFA Reviewed; 272 AA.
AC Q830K4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=EF_2777;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS).
RC STRAIN=ATCC 700802 / V583;
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of 4-methyl-5-(beta-hydroxyethyl)thiazole kinase
RT (np_816404.1) from Enterococcus faecalis V583 at 2.57 A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
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; AE016830; AAO82474.1; -; Genomic_DNA.
DR RefSeq; NP_816404.1; NC_004668.1.
DR RefSeq; WP_002387209.1; NZ_KE136528.1.
DR PDB; 3DZV; X-ray; 2.57 A; A/B=1-272.
DR PDBsum; 3DZV; -.
DR AlphaFoldDB; Q830K4; -.
DR SMR; Q830K4; -.
DR STRING; 226185.EF_2777; -.
DR PRIDE; Q830K4; -.
DR DNASU; 1201627; -.
DR EnsemblBacteria; AAO82474; AAO82474; EF_2777.
DR KEGG; efa:EF2777; -.
DR PATRIC; fig|226185.45.peg.793; -.
DR eggNOG; COG2145; Bacteria.
DR HOGENOM; CLU_019943_0_0_9; -.
DR OMA; KPIMAEH; -.
DR UniPathway; UPA00060; UER00139.
DR EvolutionaryTrace; Q830K4; -.
DR Proteomes; UP000001415; 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; Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..272
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000383858"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3DZV"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3DZV"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 147..163
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 200..214
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 218..239
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3DZV"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:3DZV"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3DZV"
SQ SEQUENCE 272 AA; 29719 MW; 87AD9F1B009874F2 CRC64;
MKTSVKFETI FPLTTAPLIQ CITNEITCES MANALLYIDA KPIMADDPRE FPQMFQQTSA
LVLNLGHLSQ EREQSLLAAS DYARQVNKLT VVDLVGYGAS DIRNEVGEKL VHNQPTVVKG
NLSEMRTFCQ LVSHGRGVDG SPLDQSEEAI EELIQALRQQ TQKFPQTVFL ATGIQDVLVS
QEQVIVLQNG VPELDCFTGT GDLVGALVAA LLGEGNAPMT AAVAAVSYFN LCGEKAKTKS
QGLADFRQNT LNQLSLLMKE KDWFEAVKGR VL
