ID   THIM_PYRAB              Reviewed;         265 AA.
AC   Q9UZQ4; G8ZJP5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   24-JAN-2024, entry version 130.
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};
GN   OrderedLocusNames=PYRAB10910; ORFNames=PAB2432;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; Evidence={ECO:0000255|HAMAP-
CC         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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB50002.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248286; CAB50002.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE70504.1; -; Genomic_DNA.
DR   PIR; E75087; E75087.
DR   RefSeq; WP_048146833.1; NC_000868.1.
DR   AlphaFoldDB; Q9UZQ4; -.
DR   SMR; Q9UZQ4; -.
DR   STRING; 272844.PAB2432; -.
DR   GeneID; 1496449; -.
DR   KEGG; pab:PAB2432; -.
DR   PATRIC; fig|272844.11.peg.1147; -.
DR   eggNOG; arCOG00019; Archaea.
DR   HOGENOM; CLU_019943_0_1_2; -.
DR   OrthoDB; 214286at2157; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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   NCBIfam; TIGR00694; thiM; 1.
DR   Pfam; PF02110; HK; 1.
DR   PIRSF; PIRSF000513; Thz_kinase; 1.
DR   PRINTS; PR01099; HYETHTZKNASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..265
FT                   /note="Hydroxyethylthiazole kinase"
FT                   /id="PRO_0000156970"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   265 AA;  28705 MW;  5E7C4084BA3C5A18 CRC64;
     MNFIVEALNE VRKRKPLVHN ITNFVVMNTT ANALLALGAS PVMAHAEEEL EEMIGLADAV
     VINIGTLDSW WRKSMIKAVE IANEMKKPIV LDPVGAGATK LRTKVALEIL DRGVTVLKGN
     FGEISSLLGE FGKTRGVDSS EYDEEKAKVL ALSAAKEFNT TVAVTGAVDY VSDGGKVFAI
     YNGHKLLERV TGTGCIVTAI TGAFVAVTEP LRAAISSLVV FGIAAEKAYE EAKYPGSFHV
     KLYDWLYRID GEVIRKYAKV REVGV
//