ID A0A2W5WW58_9MICO Unreviewed; 296 AA.
AC A0A2W5WW58;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=DNL40_03175 {ECO:0000313|EMBL:PZR55547.1};
OS Xylanimonas oleitrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Xylanimonas.
OX NCBI_TaxID=2607479 {ECO:0000313|EMBL:PZR55547.1, ECO:0000313|Proteomes:UP000248783};
RN [1] {ECO:0000313|EMBL:PZR55547.1, ECO:0000313|Proteomes:UP000248783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PW21 {ECO:0000313|EMBL:PZR55547.1,
RC ECO:0000313|Proteomes:UP000248783};
RA Nagkirti P., Shaikh A., Gowdaman V., Engineer A.E., Dagar S.,
RA Dhakephalkar P.K.;
RT "Whole genome sequencing of a novel hydrocarbon degrading bacterial strain,
RT PW21 isolated from oil contaminated produced water sample.";
RL Submitted (JUN-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:PZR55547.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QKWH01000001; PZR55547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W5WW58; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000248783; 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:PZR55547.1};
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:UP000248783};
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:PZR55547.1}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ SEQUENCE 296 AA; 28992 MW; 9249F3B8B3D85A9D CRC64;
MSTAVPGPDG AVTSSSDPGP DPQSWPGLAP QVADVVRSVR QSAPLVHCIT NVVVTNFTAN
VVLAAGAAPA MVATPAESGV MAGAASALLV NLGTVEGDQP DGMRVAVEAA TASGVPWVLD
PVAIGALPLR TALAAELFER GPAVVRGNAS EVQALAGGRG GRGVDSLDTP DDVRETALHL
ARGSGAVVAV SGTVDLLTDG VRVVRVHAGH PLLTRVTGVG CSLGALVAAC AAVTDDRLLA
ATAATAWMCV AGDLAAAAHP GPGSFAVALV DRLADVAPEA VADLAGLVAE RSGAAA
//
