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Entry: A0A060LZ46_9BACI
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ID   A0A060LZ46_9BACI        Unreviewed;       259 AA.
AC   A0A060LZ46;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=BleG1_2908 {ECO:0000313|EMBL:AIC95472.1};
OS   Shouchella lehensis G1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95472.1, ECO:0000313|Proteomes:UP000027142};
RN   [1] {ECO:0000313|EMBL:AIC95472.1, ECO:0000313|Proteomes:UP000027142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:AIC95472.1,
RC   ECO:0000313|Proteomes:UP000027142};
RX   PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA   Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA   Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA   Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT   "A comparative genomic analysis of the alkalitolerant soil bacterium
RT   Bacillus lehensis G1.";
RL   Gene 545:253-261(2014).
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; CP003923; AIC95472.1; -; Genomic_DNA.
DR   RefSeq; WP_038482348.1; NZ_CP003923.1.
DR   AlphaFoldDB; A0A060LZ46; -.
DR   STRING; 1246626.BleG1_2908; -.
DR   KEGG; ble:BleG1_2908; -.
DR   PATRIC; fig|1246626.3.peg.2896; -.
DR   eggNOG; COG2145; Bacteria.
DR   HOGENOM; CLU_019943_0_1_9; -.
DR   OrthoDB; 9778146at2; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000027142; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00228};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00228, ECO:0000313|EMBL:AIC95472.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00228};
KW   Membrane {ECO:0000256|SAM:Phobius};
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:UP000027142};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00228}; Transferase {ECO:0000256|HAMAP-Rule:MF_00228};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        178..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   259 AA;  27540 MW;  6885682130088C96 CRC64;
     MSTLRQQNPL IHCMTNLVVT NFTANGLLAI GASPVMAYAK EETHEMAEAA DALLLNIGTP
     SETVVESMIH AGQAANKKGT PVILDPVGAG ATSFRNEMIA RILQHVDITL IRGNAGEIAA
     ILGEVGTVKG VDAQIKTDPV VLAKRAAEEL KTLIVVTGEQ DVVTDGSRTV TIKNGHEWLT
     RVVGTGCLLG GVLAAYLAIN RDDKIKAAAE GLAYYGVAAE RAYAKASDRG VASFQLEFLD
     ALSTLSEEEA ESFYRMEWL
//
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