ID   THIM_LARHH              Reviewed;         267 AA.
AC   C1DCM4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=LHK_02662;
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Laribacter.
OX   NCBI_TaxID=557598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9;
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA   Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA   Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(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}.
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DR   EMBL; CP001154; ACO75643.1; -; Genomic_DNA.
DR   RefSeq; WP_012698107.1; NC_012559.1.
DR   AlphaFoldDB; C1DCM4; -.
DR   SMR; C1DCM4; -.
DR   STRING; 557598.LHK_02662; -.
DR   EnsemblBacteria; ACO75643; ACO75643; LHK_02662.
DR   KEGG; lhk:LHK_02662; -.
DR   eggNOG; COG2145; Bacteria.
DR   HOGENOM; CLU_019943_0_1_4; -.
DR   OMA; KRPLVHN; -.
DR   OrthoDB; 1717689at2; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000002010; 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   Reference proteome; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..267
FT                   /note="Hydroxyethylthiazole kinase"
FT                   /id="PRO_0000383876"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   267 AA;  27119 MW;  F63780CB69EA3879 CRC64;
     MSDLLPLPPA AIRLPDLVRQ HPPLVHCLTN QVVSQFTANV LLAAGAAPAM VIAREEAGDF
     ARMASAVLVN VGTLTPVQAD AMRVAVAAAL EAGTPWTLDP VAVGALAFRT QFCRELLSQR
     PTAIRGNPAE ILALAGEASR GRGVDSLDDS TVALAAARRL ADATGAVVAV TGATDFITDG
     ERVIALAGGH PLLQQVTGTG CSLSALVAAM TAMTDDPLSG AAVACALMKL AGERAADKAA
     GPGSFAVHLL DEIAALTPAD LAQRWPA