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Database: UniProt
Entry: A0A0X8D3K5_9BACL
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ID   A0A0X8D3K5_9BACL        Unreviewed;       266 AA.
AC   A0A0X8D3K5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Hydroxyethylthiazole kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE            EC=2.7.1.50 {ECO:0000256|HAMAP-Rule:MF_00228};
DE   AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE            Short=TH kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE            Short=Thz kinase {ECO:0000256|HAMAP-Rule:MF_00228};
GN   Name=thiM {ECO:0000256|HAMAP-Rule:MF_00228};
GN   ORFNames=ACH33_10695 {ECO:0000313|EMBL:AMA73277.1};
OS   Aneurinibacillus sp. XH2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA73277.1, ECO:0000313|Proteomes:UP000065566};
RN   [1] {ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA   Xi L.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMA73277.1, ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|EMBL:AMA73277.1,
RC   ECO:0000313|Proteomes:UP000065566};
RA   Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT   "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT   Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT   China.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC       methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000256|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:0000256|ARBA:ARBA00001771, ECO:0000256|HAMAP-
CC         Rule:MF_00228};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|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:0000256|ARBA:ARBA00004868,
CC       ECO:0000256|HAMAP-Rule:MF_00228}.
CC   -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00228}.
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DR   EMBL; CP014140; AMA73277.1; -; Genomic_DNA.
DR   RefSeq; WP_057899008.1; NZ_CP014140.1.
DR   AlphaFoldDB; A0A0X8D3K5; -.
DR   STRING; 1450761.ACH33_10695; -.
DR   KEGG; anx:ACH33_10695; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000065566; 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   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00228};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00228, ECO:0000313|EMBL:AMA73277.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00228};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00228};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00228}; Reference proteome {ECO:0000313|Proteomes:UP000065566};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00228}; Transferase {ECO:0000256|HAMAP-Rule:MF_00228}.
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   266 AA;  27838 MW;  1821A1D9C84DAB12 CRC64;
     MLGQEAAALL LKLREKKPLV HNITNVVVTN FTANGLLALG VSPVMAYAPE EVADMAKIAG
     ALVLNMGTLT RETVEAMLIA GKSANKHGVP VVFDPVGAGA TPFRTEMARR IVNELDIAII
     RGNAAEIANV IGESWEIKGV DAGEKGGDTE ELARKATKAL GTVVAITGKT DVVAGPDKLY
     MIRNGDEMLT RVTGTGCLLT SILGAYAAVE QDFVFAAAAG LASYGVAAEL ARQIVSAPGS
     YQIALLDALY NLEEAQIIEM ADITEK
//
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