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Protein

Hydroxyethylthiazole kinase

Gene

thiM

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).1 PublicationUniRule annotation

Catalytic activityi

ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole.1 PublicationUniRule annotation

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit. The first is coordinated via water, the second is coordinated to ATP but its significance is unclear.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451Substrate; via amide nitrogen1 PublicationUniRule annotation
Binding sitei121 – 1211ATP
Binding sitei168 – 1681ATP
Binding sitei195 – 1951Substrate; via amide nitrogen1 PublicationUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. hydroxyethylthiazole kinase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. thiamine biosynthetic process Source: UniProtKB-KW
  2. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU38300-MONOMER.
MetaCyc:BSU38300-MONOMER.
UniPathwayiUPA00060; UER00139.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyethylthiazole kinaseUniRule annotation (EC:2.7.1.50UniRule annotation)
Alternative name(s):
4-methyl-5-beta-hydroxyethylthiazole kinaseUniRule annotation
Short name:
TH kinaseUniRule annotation
Short name:
Thz kinaseUniRule annotation
Gene namesi
Name:thiMUniRule annotation
Synonyms:thiK, ywbJ
Ordered Locus Names:BSU38300
ORF Names:ipa-25d
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU38300. [Micado]

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981C → A: Reduces activity by 60%. 1 Publication
Mutagenesisi198 – 1981C → D: Increases activity 10-fold. 1 Publication
Mutagenesisi198 – 1981C → S: Reduces activity by 80%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272Hydroxyethylthiazole kinasePRO_0000156927Add
BLAST

Proteomic databases

PaxDbiP39593.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi224308.BSU38300.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614Combined sources
Beta strandi19 – 235Combined sources
Turni26 – 283Combined sources
Helixi29 – 3911Combined sources
Beta strandi42 – 443Combined sources
Turni49 – 513Combined sources
Helixi52 – 587Combined sources
Beta strandi59 – 657Combined sources
Helixi71 – 8616Combined sources
Beta strandi91 – 944Combined sources
Helixi102 – 11413Combined sources
Beta strandi118 – 1225Combined sources
Helixi124 – 1307Combined sources
Beta strandi133 – 1386Combined sources
Helixi148 – 16114Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi169 – 1757Combined sources
Beta strandi180 – 1834Combined sources
Helixi188 – 1925Combined sources
Helixi196 – 20813Combined sources
Helixi214 – 23623Combined sources
Turni237 – 2393Combined sources
Helixi241 – 25414Combined sources
Helixi257 – 2637Combined sources
Beta strandi266 – 2694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3QX-ray2.00A/B/C1-272[»]
1EKKX-ray2.00A/B1-272[»]
1EKQX-ray1.50A/B1-272[»]
1ESJX-ray1.80A/B/C1-272[»]
1ESQX-ray2.50A/B/C1-272[»]
ProteinModelPortaliP39593.
SMRiP39593. Positions 1-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39593.

Family & Domainsi

Sequence similaritiesi

Belongs to the Thz kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2145.
HOGENOMiHOG000114352.
InParanoidiP39593.
KOiK00878.
OMAiSPVMAHA.
OrthoDBiEOG628F8M.
PhylomeDBiP39593.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_00228. Thz_kinase.
InterProiIPR000417. Hyethyz_kinase.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF02110. HK. 1 hit.
[Graphical view]
PIRSFiPIRSF000513. Thz_kinase. 1 hit.
PRINTSiPR01099. HYETHTZKNASE.
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00694. thiM. 1 hit.

Sequencei

Sequence statusi: Complete.

P39593-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDAQSAAKCL TAVRRHSPLV HSITNNVVTN FTANGLLALG ASPVMAYAKE
60 70 80 90 100
EVADMAKIAG ALVLNIGTLS KESVEAMIIA GKSANEHGVP VILDPVGAGA
110 120 130 140 150
TPFRTESARD IIREVRLAAI RGNAAEIAHT VGVTDWLIKG VDAGEGGGDI
160 170 180 190 200
IRLAQQAAQK LNTVIAITGE VDVIADTSHV YTLHNGHKLL TKVTGAGCLL
210 220 230 240 250
TSVVGAFCAV EENPLFAAIA AISSYGVAAQ LAAQQTADKG PGSFQIELLN
260 270
KLSTVTEQDV QEWATIERVT VS
Length:272
Mass (Da):28,213
Last modified:February 1, 1995 - v1
Checksum:i868DDDC0B03DCEAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51581.1.
AL009126 Genomic DNA. Translation: CAB15856.1.
PIRiS39680.
RefSeqiNP_391709.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15856; CAB15856; BSU38300.
GeneIDi938519.
KEGGibsu:BSU38300.
PATRICi18979706. VBIBacSub10457_4015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51581.1.
AL009126 Genomic DNA. Translation: CAB15856.1.
PIRiS39680.
RefSeqiNP_391709.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3QX-ray2.00A/B/C1-272[»]
1EKKX-ray2.00A/B1-272[»]
1EKQX-ray1.50A/B1-272[»]
1ESJX-ray1.80A/B/C1-272[»]
1ESQX-ray2.50A/B/C1-272[»]
ProteinModelPortaliP39593.
SMRiP39593. Positions 1-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU38300.

Proteomic databases

PaxDbiP39593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15856; CAB15856; BSU38300.
GeneIDi938519.
KEGGibsu:BSU38300.
PATRICi18979706. VBIBacSub10457_4015.

Organism-specific databases

GenoListiBSU38300. [Micado]

Phylogenomic databases

eggNOGiCOG2145.
HOGENOMiHOG000114352.
InParanoidiP39593.
KOiK00878.
OMAiSPVMAHA.
OrthoDBiEOG628F8M.
PhylomeDBiP39593.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00139.
BioCyciBSUB:BSU38300-MONOMER.
MetaCyc:BSU38300-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39593.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_00228. Thz_kinase.
InterProiIPR000417. Hyethyz_kinase.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF02110. HK. 1 hit.
[Graphical view]
PIRSFiPIRSF000513. Thz_kinase. 1 hit.
PRINTSiPR01099. HYETHTZKNASE.
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00694. thiM. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis."
    Zhang Y., Taylor S.V., Chiu H.-J., Begley T.P.
    J. Bacteriol. 179:3030-3035(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  4. "Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution."
    Campobasso N., Mathews I.I., Begley T.P., Ealick S.E.
    Biochemistry 39:7868-7877(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, COFACTOR, SUBUNIT, MUTAGENESIS OF CYS-198.

Entry informationi

Entry nameiTHIM_BACSU
AccessioniPrimary (citable) accession number: P39593
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.