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Database: UniProt
Entry: A0A255IAT9_9FIRM
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ID   A0A255IAT9_9FIRM        Unreviewed;       274 AA.
AC   A0A255IAT9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=C8E03_101752 {ECO:0000313|EMBL:PXV96119.1}, CG710_010440
GN   {ECO:0000313|EMBL:RDY31305.1};
OS   Lachnotalea glycerini.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnotalea.
OX   NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY31305.1, ECO:0000313|Proteomes:UP000216411};
RN   [1] {ECO:0000313|EMBL:RDY31305.1, ECO:0000313|Proteomes:UP000216411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY31305.1,
RC   ECO:0000313|Proteomes:UP000216411};
RX   PubMed=29051240;
RA   Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA   Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT   "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT   glycerini Isolated from Water in Quebec City, Canada.";
RL   Genome Announc. 5:e01059-17(2017).
RN   [2] {ECO:0000313|EMBL:PXV96119.1, ECO:0000313|Proteomes:UP000247523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28816 {ECO:0000313|EMBL:PXV96119.1,
RC   ECO:0000313|Proteomes:UP000247523};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RDY31305.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY31305.1};
RA   Quirk P.G., Krulwich T.A.;
RL   Submitted (JUL-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDY31305.1}.
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DR   EMBL; QICS01000001; PXV96119.1; -; Genomic_DNA.
DR   EMBL; NOKA02000018; RDY31305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255IAT9; -.
DR   OrthoDB; 9778146at2; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000216411; Unassembled WGS sequence.
DR   Proteomes; UP000247523; Unassembled WGS sequence.
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; 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:RDY31305.1};
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:UP000216411};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00228};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00228, ECO:0000313|EMBL:RDY31305.1}.
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   274 AA;  29490 MW;  6E5EEBBE197EE908 CRC64;
     MIERIIENVR SNTPLIHCIT NYVTVNDVAN VLLACGASPI MADDINEAAE ITSICSGLDI
     NIGTLNTRTI EAMIKAGKKA NELGHITVLD PVGAGASKLR TDTAFELLKE IRFSVIRGNI
     SEIKSLYQGS STSNGVDANV SDRITEANLE ETISFAKELS KKTKAVIAIT GAIDIIADEN
     KAYVIQNGHP IMSKITGTGC MLTGIIAAYC AANPSQILEA TKAAVICEGL AGEKAYEKMQ
     ATNGYTSTFR MYLIDYIGEM TDQMIREGMK VEIR
//
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