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Database: UniProt
Entry: K6W8L4_9MICO
LinkDB: K6W8L4_9MICO
Original site: K6W8L4_9MICO 
ID   K6W8L4_9MICO            Unreviewed;       268 AA.
AC   K6W8L4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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   ECO:0000313|EMBL:GAB95540.1};
GN   ORFNames=KILIM_022_00240 {ECO:0000313|EMBL:GAB95540.1};
OS   Kineosphaera limosa NBRC 100340.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Kineosphaera.
OX   NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB95540.1, ECO:0000313|Proteomes:UP000008366};
RN   [1] {ECO:0000313|EMBL:GAB95540.1, ECO:0000313|Proteomes:UP000008366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB95540.1,
RC   ECO:0000313|Proteomes:UP000008366};
RA   Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA   Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL   Submitted (AUG-2012) 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:GAB95540.1}.
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DR   EMBL; BAHD01000022; GAB95540.1; -; Genomic_DNA.
DR   RefSeq; WP_006592072.1; NZ_BAHD01000022.1.
DR   AlphaFoldDB; K6W8L4; -.
DR   STRING; 1184609.KILIM_022_00240; -.
DR   eggNOG; COG2145; Bacteria.
DR   OrthoDB; 8909021at2; -.
DR   UniPathway; UPA00060; UER00139.
DR   Proteomes; UP000008366; 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:GAB95540.1};
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:UP000008366};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00228}; Transferase {ECO:0000256|HAMAP-Rule:MF_00228}.
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ   SEQUENCE   268 AA;  26707 MW;  9B4F000EABF8647C CRC64;
     MNDSPITAAQ VGEALDALRN EGPLVQCLTN IVVTNWTANV LLAAGAAPAM VDNEQEAGLF
     AGVASGVLVN LGTPQENTVA GMRAAVAGAK DASTPWVLDP VAAGGLPWRT EIARELVAAG
     APTIIRGNAS EIAGLAGGAG GRGVDSTDTP DAVREVAQDL ARANSCVVAV SGAVDLLTDG
     RRTVRLANGH EWLTRVTGVG CSLGALMAGF AGVVDDPLVA AASATGLLTV AADQAAQGAQ
     GPGTFAVALL DRLASLSADD LVEQVRLS
//
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