THIM2_CLOBH
ID THIM2_CLOBH Reviewed; 265 AA.
AC A5I421; A7G5F7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Hydroxyethylthiazole kinase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00228};
DE Short=TH kinase 2 {ECO:0000255|HAMAP-Rule:MF_00228};
DE Short=Thz kinase 2 {ECO:0000255|HAMAP-Rule:MF_00228};
GN Name=thiM2 {ECO:0000255|HAMAP-Rule:MF_00228};
GN OrderedLocusNames=CBO2253, CLC_2176;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL83792.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM412317; CAL83792.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000727; ABS36898.1; -; Genomic_DNA.
DR RefSeq; WP_011986722.1; NC_009698.1.
DR RefSeq; YP_001254744.1; NC_009495.1.
DR RefSeq; YP_001388022.1; NC_009698.1.
DR AlphaFoldDB; A5I421; -.
DR SMR; A5I421; -.
DR GeneID; 5186508; -.
DR KEGG; cbh:CLC_2176; -.
DR KEGG; cbo:CBO2253; -.
DR PATRIC; fig|413999.7.peg.2222; -.
DR HOGENOM; CLU_019943_0_0_9; -.
DR UniPathway; UPA00060; UER00139.
DR PRO; PR:A5I421; -.
DR Proteomes; UP000001986; 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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..265
FT /note="Hydroxyethylthiazole kinase 2"
FT /id="PRO_0000383843"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00228"
SQ SEQUENCE 265 AA; 28576 MW; F2F92C9C43F88AE8 CRC64;
MQIRQSIKLK KPLIHYITNP ISINDCANII LAAGAKPIMA EHPLEVSEIT SVSKSLGVNL
GNITDNKMKS MLISGKTAYE NKIPQVIDLV GVGCSKLRLD YAKKFISECH PNVIKGNMSE
IKAIYGIKSS AKGIDVGACD IITKQNFDEN IEMIKRLSME TGSVVAATGV VDIISNGTYT
YIISNGCEML SMITGTGCML TGLIASYISS ENILDGTVLA VALMGICGEL SQHAKGTGSF
RNELTDNMFS ISDDIIIKKI RINSY
