ID   THIM_BACSU              Reviewed;         272 AA.
AC   P39593;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 159.
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}; Synonyms=thiK, ywbJ;
GN   OrderedLocusNames=BSU38300; ORFNames=ipa-25d;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=9139923; DOI=10.1128/jb.179.9.3030-3035.1997;
RA   Zhang Y., Taylor S.V., Chiu H.-J., Begley T.P.;
RT   "Characterization of the Bacillus subtilis thiC operon involved in thiamine
RT   biosynthesis.";
RL   J. Bacteriol. 179:3030-3035(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, COFACTOR,
RP   SUBUNIT, AND MUTAGENESIS OF CYS-198.
RX   PubMed=10891066; DOI=10.1021/bi0000061;
RA   Campobasso N., Mathews I.I., Begley T.P., Ealick S.E.;
RT   "Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from
RT   Bacillus subtilis at 1.5 A resolution.";
RL   Biochemistry 39:7868-7877(2000).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC       methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|HAMAP-
CC       Rule:MF_00228, ECO:0000269|PubMed:9139923}.
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         ECO:0000269|PubMed:9139923};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10891066};
CC       Note=Binds 2 magnesium ions per subunit. The first is coordinated via
CC       water, the second is coordinated to ATP but its significance is
CC       unclear. {ECO:0000269|PubMed:10891066};
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       ECO:0000269|PubMed:9139923}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10891066}.
CC   -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00228}.
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DR   EMBL; X73124; CAA51581.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15856.1; -; Genomic_DNA.
DR   PIR; S39680; S39680.
DR   RefSeq; NP_391709.1; NC_000964.3.
DR   RefSeq; WP_003244274.1; NZ_JNCM01000034.1.
DR   PDB; 1C3Q; X-ray; 2.00 A; A/B/C=1-272.
DR   PDB; 1EKK; X-ray; 2.00 A; A/B=1-272.
DR   PDB; 1EKQ; X-ray; 1.50 A; A/B=1-272.
DR   PDB; 1ESJ; X-ray; 1.80 A; A/B/C=1-272.
DR   PDB; 1ESQ; X-ray; 2.50 A; A/B/C=1-272.
DR   PDBsum; 1C3Q; -.
DR   PDBsum; 1EKK; -.
DR   PDBsum; 1EKQ; -.
DR   PDBsum; 1ESJ; -.
DR   PDBsum; 1ESQ; -.
DR   AlphaFoldDB; P39593; -.
DR   SMR; P39593; -.
DR   STRING; 224308.BSU38300; -.
DR   DrugBank; DB02969; 5-(2-hydroxyethyl)-4-methylthiazole.
DR   PaxDb; 224308-BSU38300; -.
DR   EnsemblBacteria; CAB15856; CAB15856; BSU_38300.
DR   GeneID; 938519; -.
DR   KEGG; bsu:BSU38300; -.
DR   PATRIC; fig|224308.179.peg.4146; -.
DR   eggNOG; COG2145; Bacteria.
DR   InParanoid; P39593; -.
DR   OrthoDB; 9778146at2; -.
DR   PhylomeDB; P39593; -.
DR   BioCyc; BSUB:BSU38300-MONOMER; -.
DR   BioCyc; MetaCyc:BSU38300-MONOMER; -.
DR   BRENDA; 2.7.1.50; 658.
DR   UniPathway; UPA00060; UER00139.
DR   EvolutionaryTrace; P39593; -.
DR   Proteomes; UP000001570; 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   NCBIfam; TIGR00694; thiM; 1.
DR   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF02110; HK; 1.
DR   PIRSF; PIRSF000513; Thz_kinase; 1.
DR   PRINTS; PR01099; HYETHTZKNASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 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..272
FT                   /note="Hydroxyethylthiazole kinase"
FT                   /id="PRO_0000156927"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228,
FT                   ECO:0000269|PubMed:10891066"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00228,
FT                   ECO:0000269|PubMed:10891066"
FT   MUTAGEN         198
FT                   /note="C->A: Reduces activity by 60%."
FT                   /evidence="ECO:0000269|PubMed:10891066"
FT   MUTAGEN         198
FT                   /note="C->D: Increases activity 10-fold."
FT                   /evidence="ECO:0000269|PubMed:10891066"
FT   MUTAGEN         198
FT                   /note="C->S: Reduces activity by 80%."
FT                   /evidence="ECO:0000269|PubMed:10891066"
FT   HELIX           3..16
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          19..23
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           52..58
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           71..86
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           102..114
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           124..130
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:1ESJ"
FT   HELIX           148..161
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          169..175
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          180..183
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           188..192
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           196..208
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           214..236
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   TURN            237..239
FT                   /evidence="ECO:0007829|PDB:1EKK"
FT   HELIX           241..254
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   HELIX           257..263
FT                   /evidence="ECO:0007829|PDB:1EKQ"
FT   STRAND          266..269
FT                   /evidence="ECO:0007829|PDB:1EKQ"
SQ   SEQUENCE   272 AA;  28213 MW;  868DDDC0B03DCEAF CRC64;
     MDAQSAAKCL TAVRRHSPLV HSITNNVVTN FTANGLLALG ASPVMAYAKE EVADMAKIAG
     ALVLNIGTLS KESVEAMIIA GKSANEHGVP VILDPVGAGA TPFRTESARD IIREVRLAAI
     RGNAAEIAHT VGVTDWLIKG VDAGEGGGDI IRLAQQAAQK LNTVIAITGE VDVIADTSHV
     YTLHNGHKLL TKVTGAGCLL TSVVGAFCAV EENPLFAAIA AISSYGVAAQ LAAQQTADKG
     PGSFQIELLN KLSTVTEQDV QEWATIERVT VS
//