THIM_KLEP7
ID THIM_KLEP7 Reviewed; 257 AA.
AC A6TBJ8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=KPN78578_25080; ORFNames=KPN_02551;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR77969.1; -; Genomic_DNA.
DR RefSeq; WP_015875043.1; NC_009648.1.
DR PDB; 6JYY; X-ray; 2.00 A; A/B/C=1-257.
DR PDBsum; 6JYY; -.
DR AlphaFoldDB; A6TBJ8; -.
DR SMR; A6TBJ8; -.
DR STRING; 272620.KPN_02551; -.
DR jPOST; A6TBJ8; -.
DR EnsemblBacteria; ABR77969; ABR77969; KPN_02551.
DR KEGG; kpn:KPN_02551; -.
DR HOGENOM; CLU_019943_0_1_6; -.
DR OMA; KRPLVHN; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000000265; 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; Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..257
FT /note="Hydroxyethylthiazole kinase"
FT /id="PRO_0000336562"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:6JYY"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6JYY"
FT TURN 100..104
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:6JYY"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 216..235
FT /evidence="ECO:0007829|PDB:6JYY"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:6JYY"
SQ SEQUENCE 257 AA; 26117 MW; 5C7582B4D9F9A382 CRC64;
MPELLNPAPV AHLRHLLRAH SPLVHCMTND VVQTFTANVL LAVGASPAMV IDPREAAQFA
AIADALLINV GTLTEDRAVA MRAAVEHARQ AGKPWTLDPV AVGALTVRTA FCHELLALQP
AAIRGNASEI LALAGMSAGG RGVDTTDTAA AALPAAQALA RRLATVVAVT GEVDYVTDGE
RVLSVAGGNP LMTRVVGTGC ALSAVVAASA ALPGDRLENV AAACGLMKQA GAIAARQGGP
GSFIPAFLDA LYQEVQG
