THIM_MAIZE
ID THIM_MAIZE Reviewed; 280 AA.
AC K7VCB9;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 51.
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; ORFNames=ZEAMMB73_814699;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Maize Genome Sequencing Project;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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=21.8 uM for thiazole {ECO:0000269|PubMed:23816351};
CC KM=17.5 uM for ATP {ECO:0000269|PubMed:23816351};
CC Note=kcat is 1.79 sec(-1) for thiazole. kcat is 2.39 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 -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000305}.
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DR EMBL; CM000784; AFW80762.1; -; Genomic_DNA.
DR RefSeq; XP_008655910.1; XM_008657688.1.
DR AlphaFoldDB; K7VCB9; -.
DR SMR; K7VCB9; -.
DR STRING; 4577.GRMZM2G094558_P01; -.
DR PaxDb; K7VCB9; -.
DR PRIDE; K7VCB9; -.
DR EnsemblPlants; Zm00001eb341310_T001; Zm00001eb341310_P001; Zm00001eb341310.
DR GeneID; 103635163; -.
DR Gramene; Zm00001eb341310_T001; Zm00001eb341310_P001; Zm00001eb341310.
DR KEGG; zma:103635163; -.
DR MaizeGDB; 9023993; -.
DR eggNOG; ENOG502QS2M; Eukaryota.
DR HOGENOM; CLU_019943_0_1_1; -.
DR OMA; KRPLVHN; -.
DR OrthoDB; 936564at2759; -.
DR BRENDA; 2.7.1.50; 6752.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000007305; Chromosome 8.
DR ExpressionAtlas; K7VCB9; baseline and differential.
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; Plasmid;
KW Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..280
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000424280"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 280 AA; 29029 MW; 7F5EBCDB951BBFCA CRC64;
MDVGAKEEEM GQVWWGHRAW SLLSAVRARA PLVQCITNLV SMDIAANVLL AAGASPAMVH
SLREVPDFTP RCDAVYVNVG TLSEDWLPSM RAAASAGRPW VLDPVAAAAS GFRMKACLEL
LSLCPAVVRG NASEILALAS RSTAASSNFK GVDSSHCSVD AIEAAKALAL SSSAVVAVSG
AVDFVTDGKQ VISVSNGVPM MQKITATGCA VTALIAAFVA MEPSDAIVAA ACALAIFGLV
GEIGMESAKG PASLRMHLID ALYCLNEETV TSRVRISLRP
