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
//