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
//
