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Reviewed, UniProtKB/Swiss-Prot P39593 (THIM_BACSU)

Last modified June 16, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hydroxyethylthiazole kinase
    EC=2.7.1.50
Alternative name(s):
    4-methyl-5-beta-hydroxyethylthiazole kinase
      Short name=Thz kinase
      Short name=TH kinase
Gene names
Name: thiM
Synonyms: thiK, ywbJ
Ordered Locus Names: BSU38300
ORF Names: ipa-25d
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 MF_00228

Cofactor

Binds 2 magnesium ions per subunit. The second one is coordinated to ATP but its significance is unclear. HAMAP MF_00228

Pathway

Cofactor biosynthesis; thiamine pyrophosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 4-methyl-5-(2-hydroxyethyl)-thiazole: step 1/1. HAMAP 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 MF_00228
PRO_0000156927

Sites

Metal binding941Magnesium 1 HAMAP MF_00228
Metal binding1261Magnesium 1 HAMAP MF_00228
Binding site451Substrate; via amide nitrogen HAMAP MF_00228
Binding site1211ATP HAMAP MF_00228
Binding site1681ATP HAMAP MF_00228
Binding site1951Substrate; via amide nitrogen HAMAP MF_00228

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
P39593-1 [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: 7934828] [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: 9384377] [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: 9139923] [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: 10891066] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, HOMOTRIMERIZATION, MUTAGENESIS OF CYS-198.

Cross-references

Sequence databases

X73124 Genomic DNA. Translation: CAA51581.1.
AL009126 Genomic DNA. Translation: CAB15856.1.
PIRS39680.
RefSeqNP_391709.1.

3D structure databases

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[»]
ModBaseSearch...

Genome annotation databases

GeneID938519.
GenomeReviewsGene locus BSU38300 in contig AL009126_GR.
KEGGbsu:BSU38300.
NMPDRfig|224308.1.peg.3835.

Organism-specific databases

SubtiListBG10571. thiM. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP39593.
OMAP39593. ASPVMAH.

Enzyme and pathway databases

BioCycBSUB224308:BSU3826-MON.
BRENDA2.7.1.50. 150.

Family and domain databases

HAMAPMF_00228.
[Tree]
InterProIPR000417. Hyethyz_kinase.
IPR011144. Hyethyz_kinsmonf.
[Graphical view]
PANTHERPTHR20857:SF14. Hyethyz_kinase. 1 hit.
PfamPF02110. HK. 1 hit.
[Graphical view]
PIRSFPIRSF000513. Thz_kinase. 1 hit.
PRINTSPR01099. HYETHTZKNASE.
TIGRFAMsTIGR00694. thiM. 1 hit.
ProtoNetSearch...

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: June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents