THIM_ANOFW
ID THIM_ANOFW Reviewed; 264 AA.
AC B7GKQ7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=Aflv_1345;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ33713.1; -; Genomic_DNA.
DR AlphaFoldDB; B7GKQ7; -.
DR SMR; B7GKQ7; -.
DR STRING; 491915.Aflv_1345; -.
DR EnsemblBacteria; ACJ33713; ACJ33713; Aflv_1345.
DR KEGG; afl:Aflv_1345; -.
DR eggNOG; COG2145; Bacteria.
DR HOGENOM; CLU_019943_0_1_9; -.
DR OMA; KRPLVHN; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000000742; 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..264
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000383820"
FT BINDING 43
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 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 264 AA; 27754 MW; 7C0A50D620E88160 CRC64;
MMNVGQWLTR VRKESPLVHN MTNVVVTNFV ANGLLAVGAS PVMAYAKEEV ADMVRLARAL
VLNIGTLNET DVEAMLIAGK AANEANIPVI FDPVGAGATA YRTETARRIL REVNISILRG
NASEIASIAG EQVRTKGVDA GDVQSDLVDV AKKAAHMFRC VVVITGKDDI VTDGERIVIV
SNGDAMLTKV TGTGCLLSSV LGAFAGVGED VMTSSVAALA YYGVAAEKAA TQAKAPGSFQ
LSFLNALHET SAEEVDQYAR IQGE
