THIM_ECOLI
ID THIM_ECOLI Reviewed; 262 AA.
AC P76423; Q9S6P4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE EC=2.7.1.50 {ECO:0000255|HAMAP-Rule:MF_00228};
DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE Short=TH kinase {ECO:0000255|HAMAP-Rule:MF_00228};
DE Short=Thz kinase {ECO:0000255|HAMAP-Rule:MF_00228};
GN Name=thiM {ECO:0000255|HAMAP-Rule:MF_00228};
GN OrderedLocusNames=b2104, JW2091;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-262.
RC STRAIN=K12;
RX PubMed=10075431; DOI=10.1099/13500872-145-2-495;
RA Mizote T., Tsuda M., Smith D.D.S., Nakayama H., Nakazawa T.;
RT "Cloning and characterization of the thiD/J gene of Escherichia coli
RT encoding a thiamin-synthesizing bifunctional enzyme,
RT hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase.";
RL Microbiology 145:495-501(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND GENE NAME.
RC STRAIN=K12;
RX PubMed=2542220; DOI=10.1128/jb.171.6.3228-3232.1989;
RA Mizote T., Nakayama H.;
RT "The thiM locus and its relation to phosphorylation of hydroxyethylthiazole
RT in Escherichia coli.";
RL J. Bacteriol. 171:3228-3232(1989).
CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|HAMAP-
CC Rule:MF_00228, ECO:0000269|PubMed:2542220}.
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:0000255|HAMAP-Rule:MF_00228,
CC ECO:0000269|PubMed:2542220};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00228,
CC ECO:0000269|PubMed:2542220}.
CC -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00228}.
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DR EMBL; U00096; AAC75165.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15972.1; -; Genomic_DNA.
DR EMBL; D88442; BAA76743.1; -; Genomic_DNA.
DR PIR; G64977; G64977.
DR RefSeq; NP_416607.1; NC_000913.3.
DR RefSeq; WP_001195564.1; NZ_SSZK01000011.1.
DR AlphaFoldDB; P76423; -.
DR SMR; P76423; -.
DR BioGRID; 4261165; 306.
DR IntAct; P76423; 2.
DR STRING; 511145.b2104; -.
DR PaxDb; P76423; -.
DR PRIDE; P76423; -.
DR EnsemblBacteria; AAC75165; AAC75165; b2104.
DR EnsemblBacteria; BAA15972; BAA15972; BAA15972.
DR GeneID; 945142; -.
DR KEGG; ecj:JW2091; -.
DR KEGG; eco:b2104; -.
DR PATRIC; fig|1411691.4.peg.143; -.
DR EchoBASE; EB3822; -.
DR eggNOG; COG2145; Bacteria.
DR HOGENOM; CLU_019943_0_1_6; -.
DR InParanoid; P76423; -.
DR OMA; KRPLVHN; -.
DR PhylomeDB; P76423; -.
DR BioCyc; EcoCyc:THZ-KIN-MON; -.
DR BioCyc; MetaCyc:THZ-KIN-MON; -.
DR BRENDA; 2.7.1.50; 2026.
DR UniPathway; UPA00060; UER00139.
DR PRO; PR:P76423; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052673; F:prenol kinase activity; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0036172; P:thiamine salvage; IMP:EcoCyc.
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; SSF53613; 1.
DR TIGRFAMs; TIGR00694; thiM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..262
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000156933"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ SEQUENCE 262 AA; 27339 MW; 720774031BA7AC4B CRC64;
MQVDLLGSAQ SAHALHLFHQ HSPLVHCMTN DVVQTFTANT LLALGASPAM VIETEEASQF
AAIASALLIN VGTLTQPRAQ AMRAAVEQAK SSQTPWTLDP VAVGALDYRR HFCHELLSFK
PAAIRGNASE IMALAGIANG GRGVDTTDAA ANAIPAAQTL ARETGAIVVV TGEMDYVTDG
HRIIGIHGGD PLMTKVVGTG CALSAVVAAC CALPGDTLEN VASACHWMKQ AGERAVARSE
GPGSFVPHFL DALWQLTQEV QA
