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P39593 (THIM_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxyethylthiazole kinase

EC=2.7.1.50
Alternative name(s):
4-methyl-5-beta-hydroxyethylthiazole kinase
Short name=TH kinase
Short name=Thz kinase
Gene names
Name:thiM
Synonyms:thiK, ywbJ
Ordered Locus Names:BSU38300
ORF Names:ipa-25d
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. HAMAP-Rule MF_00228

Cofactor

Binds 2 magnesium ions per subunit. The first is coordinated via water, the second is coordinated to ATP but its significance is unclear.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1. HAMAP-Rule MF_00228

Subunit structure

Homotrimer. Ref.4

Sequence similarities

Belongs to the Thz kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Hydroxyethylthiazole kinase HAMAP-Rule MF_00228
PRO_0000156927

Sites

Binding site451Substrate; via amide nitrogen
Binding site1211ATP
Binding site1681ATP
Binding site1951Substrate; via amide nitrogen

Experimental info

Mutagenesis1981C → A: Reduces activity by 60%. Ref.4
Mutagenesis1981C → D: Increases activity 10-fold. Ref.4
Mutagenesis1981C → S: Reduces activity by 80%. Ref.4

Secondary structure

............................................... 272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39593 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 868DDDC0B03DCEAF

FASTA27228,213
        10         20         30         40         50         60 
MDAQSAAKCL TAVRRHSPLV HSITNNVVTN FTANGLLALG ASPVMAYAKE EVADMAKIAG 

        70         80         90        100        110        120 
ALVLNIGTLS KESVEAMIIA GKSANEHGVP VILDPVGAGA TPFRTESARD IIREVRLAAI 

       130        140        150        160        170        180 
RGNAAEIAHT VGVTDWLIKG VDAGEGGGDI IRLAQQAAQK LNTVIAITGE VDVIADTSHV 

       190        200        210        220        230        240 
YTLHNGHKLL TKVTGAGCLL TSVVGAFCAV EENPLFAAIA AISSYGVAAQ LAAQQTADKG 

       250        260        270 
PGSFQIELLN KLSTVTEQDV QEWATIERVT VS 

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees."
Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.
Mol. Microbiol. 10:371-384(1993) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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: CHARACTERIZATION.
[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, HOMOTRIMERIZATION, MUTAGENESIS OF CYS-198.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73124 Genomic DNA. Translation: CAA51581.1.
AL009126 Genomic DNA. Translation: CAB15856.1.
PIRS39680.
RefSeqNP_391709.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP39593.
SMRP39593. Positions 1-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU38300.

Proteomic databases

PaxDbP39593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15856; CAB15856; BSU38300.
GeneID938519.
KEGGbsu:BSU38300.
PATRIC18979706. VBIBacSub10457_4015.

Organism-specific databases

GenoListBSU38300. [Micado]

Phylogenomic databases

eggNOGCOG2145.
HOGENOMHOG000114352.
KOK00878.
OMASPVMAHA.
OrthoDBEOG628F8M.
ProtClustDBPRK09355.

Enzyme and pathway databases

BioCycBSUB:BSU38300-MONOMER.
MetaCyc:BSU38300-MONOMER.
UniPathwayUPA00060; UER00139.

Family and domain databases

HAMAPMF_00228. Thz_kinase.
InterProIPR000417. Hyethyz_kinase.
[Graphical view]
PfamPF02110. HK. 1 hit.
[Graphical view]
PIRSFPIRSF000513. Thz_kinase. 1 hit.
PRINTSPR01099. HYETHTZKNASE.
TIGRFAMsTIGR00694. thiM. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP39593.

Entry information

Entry nameTHIM_BACSU
AccessionPrimary (citable) accession number: P39593
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList