THIM_PYRHO
ID THIM_PYRHO Reviewed; 265 AA.
AC O58877;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
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}; OrderedLocusNames=PH1157;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RG RIKEN structural genomics initiative (RSGI);
RT "Structure of hydroxyethylthiazole kinase protein from Pyrococcus
RT horikoshii OT3.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00228};
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 -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00228}.
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DR EMBL; BA000001; BAA30257.1; -; Genomic_DNA.
DR PIR; G71057; G71057.
DR RefSeq; WP_010885242.1; NC_000961.1.
DR PDB; 3HPD; X-ray; 1.85 A; A=1-265.
DR PDBsum; 3HPD; -.
DR AlphaFoldDB; O58877; -.
DR SMR; O58877; -.
DR STRING; 70601.3257574; -.
DR EnsemblBacteria; BAA30257; BAA30257; BAA30257.
DR GeneID; 1443477; -.
DR KEGG; pho:PH1157; -.
DR eggNOG; arCOG00019; Archaea.
DR OMA; KRPLVHN; -.
DR OrthoDB; 70640at2157; -.
DR BRENDA; 2.7.1.50; 7183.
DR UniPathway; UPA00060; UER00139.
DR EvolutionaryTrace; O58877; -.
DR Proteomes; UP000000752; Chromosome.
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; SSF53613; 1.
DR TIGRFAMs; TIGR00694; thiM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Thiamine biosynthesis; Transferase.
FT CHAIN 1..265
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000156972"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT HELIX 2..14
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:3HPD"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3HPD"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 69..85
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 160..172
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 210..231
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:3HPD"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3HPD"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:3HPD"
SQ SEQUENCE 265 AA; 28954 MW; 5D38EB1846CA02BA CRC64;
MKFIIEALKR VRERRPLVHN ITNFVVMNTT ANALLALGAS PVMAHAEEEL EEMIRLADAV
VINIGTLDSG WRRSMVKATE IANELGKPIV LDPVGAGATK FRTRVSLEIL SRGVDVLKGN
FGEISALLGE EGKTRGVDSL EYGEEEAKKL TMNAAREFNT TVAVTGAVDY VSDGRRTFAV
YNGHELLGRV TGTGCMVAAL TGAFVAVTEP LKATTSALVT FGIAAEKAYE EAKYPGSFHV
KLYDWLYRIN ENVIRTYAKV REVEL
