THIM_ARATH
ID THIM_ARATH Reviewed; 276 AA.
AC Q9LIQ4;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Hydroxyethylthiazole kinase;
DE EC=2.7.1.50;
DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase;
DE Short=TH kinase;
DE Short=Thz kinase;
GN Name=THIM; OrderedLocusNames=At3g24030; ORFNames=F14O13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND INDUCTION BY THIAMINE AND
RP 4-METHYL-5-(2-PHOSPHONOOXYETHYL)THIAZOLE.
RX PubMed=23816351; DOI=10.1016/j.phytochem.2013.05.017;
RA Yazdani M., Zallot R., Tunc-Ozdemir M., de Crecy-Lagard V., Shintani D.K.,
RA Hanson A.D.;
RT "Identification of the thiamin salvage enzyme thiazole kinase in
RT Arabidopsis and maize.";
RL Phytochemistry 94:68-73(2013).
CC -!- FUNCTION: Thiazole kinase involved in thiamine salvage pathway.
CC {ECO:0000269|PubMed:23816351}.
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:0000269|PubMed:23816351};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30.5 uM for thiazole {ECO:0000269|PubMed:23816351};
CC KM=44.8 uM for ATP {ECO:0000269|PubMed:23816351};
CC Note=kcat is 0.068 sec(-1) for thiazole. kcat is 0.069 sec(-1) for
CC ATP.;
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-
CC methylthiazole: step 1/1.
CC -!- INDUCTION: Not regulated by thiamine or 4-methyl-5-(2-
CC phosphonooxyethyl)thiazole. {ECO:0000269|PubMed:23816351}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:23816351}.
CC -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000305}.
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DR EMBL; AP001297; BAB03021.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76846.1; -; Genomic_DNA.
DR EMBL; BT010426; AAQ62427.1; -; mRNA.
DR EMBL; AK175955; BAD43718.1; -; mRNA.
DR RefSeq; NP_001319628.1; NM_001338665.1.
DR AlphaFoldDB; Q9LIQ4; -.
DR SMR; Q9LIQ4; -.
DR STRING; 3702.AT3G24030.1; -.
DR PaxDb; Q9LIQ4; -.
DR PRIDE; Q9LIQ4; -.
DR ProteomicsDB; 246442; -.
DR EnsemblPlants; AT3G24030.1; AT3G24030.1; AT3G24030.
DR GeneID; 821988; -.
DR Gramene; AT3G24030.1; AT3G24030.1; AT3G24030.
DR KEGG; ath:AT3G24030; -.
DR Araport; AT3G24030; -.
DR TAIR; locus:2076171; AT3G24030.
DR eggNOG; ENOG502QS2M; Eukaryota.
DR HOGENOM; CLU_019943_0_1_1; -.
DR InParanoid; Q9LIQ4; -.
DR OMA; KRPLVHN; -.
DR OrthoDB; 936564at2759; -.
DR PhylomeDB; Q9LIQ4; -.
DR BioCyc; ARA:AT3G24030-MON; -.
DR BRENDA; 2.7.1.50; 399.
DR UniPathway; UPA00060; UER00139.
DR PRO; PR:Q9LIQ4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIQ4; baseline and differential.
DR Genevisible; Q9LIQ4; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0036172; P:thiamine salvage; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..276
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000424279"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 276 AA; 28795 MW; 7A8B70E56E4942E0 CRC64;
MESKSEQNEW SSGVWAHLTA VRQQSPLVQC ITNFVSMDLV ANTLLSAGAS PAMVHSVVEI
PDFTPHIHAL CVNVGTLTPD WLPSMKAAAE LASQLRKPWV LDPAAVSCSG FRLKACLELI
ELKPTVIKGN GSEIIALSSA SRGQTKGADS SHESTDAIEA AKSLAMSSGA VVAVSGAVDI
VTDGKQVIGV HNGTKMMQQI TATGCSLAGL IVAFLAIDSS RVLEATVSAM AVFGIAGELG
EAMANGPASL RMHLIDCLYG LDETTVLKRV NVTRLG
