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O34664 (THIN_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 75. 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:
Thiamine pyrophosphokinase

Short name=TPK
EC=2.7.6.2
Alternative name(s):
Thiamine diphosphokinase
Gene names
Name:thiN
Synonyms:yloS
Ordered Locus Names:BSU15800
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate.

Catalytic activity

ATP + thiamine = AMP + thiamine diphosphate.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.

Sequence similarities

Belongs to the thiamine pyrophosphokinase family.

Biophysicochemical properties

Kinetic parameters:

KM=20 µM for thiamine

KM=1 mM for ATP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Thiamine pyrophosphokinase
PRO_0000072516

Secondary structure

........................................... 214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34664 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 77BBA150330F4679

FASTA21424,099
        10         20         30         40         50         60 
MKTINIVAGG PKNLIPDLTG YTDEHTLWIG VDKGTVTLLD AGIIPVEAFG DFDSITEQER 

        70         80         90        100        110        120 
RRIEKAAPAL HVYQAEKDQT DLDLALDWAL EKQPDIIQIF GITGGRADHF LGNIQLLYKG 

       130        140        150        160        170        180 
VKTNIKIRLI DKQNHIQMFP PGEYDIEKDE NKRYISFIPF SEDIHELTLT GFKYPLNNCH 

       190        200        210 
ITLGSTLCIS NELIHSRGTF SFAKGILIMI RSTD 

« Hide

References

« Hide 'large scale' references
[1]"A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome."
Foulger D., Errington J.
Microbiology 144:801-805(1998) [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]"Identification of the two missing bacterial genes involved in thiamine salvage: thiamine pyrophosphokinase and thiamine kinase."
Melnick J., Lis E., Park J.-H., Kinsland C., Mori H., Baba T., Perkins J., Schyns G., Vassieva O., Osterman A., Begley T.P.
J. Bacteriol. 186:3660-3662(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13937 Genomic DNA. Translation: CAA74253.1.
AL009126 Genomic DNA. Translation: CAB13453.1.
PIRC69879.
RefSeqNP_389462.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LM8X-ray2.60A/B/C/D1-214[»]
ProteinModelPortalO34664.
SMRO34664. Positions 2-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU15800.

Proteomic databases

PaxDbO34664.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13453; CAB13453; BSU15800.
GeneID937714.
KEGGbsu:BSU15800.
PATRIC18974967. VBIBacSub10457_1675.

Organism-specific databases

GenoListBSU15800. [Micado]

Phylogenomic databases

eggNOGCOG1564.
HOGENOMHOG000037072.
KOK00949.
OMAITYCPEG.
OrthoDBEOG62NX6M.
ProtClustDBCLSK887291.

Enzyme and pathway databases

BioCycBSUB:BSU15800-MONOMER.
MetaCyc:BSU15800-MONOMER.
UniPathwayUPA00060; UER00597.

Family and domain databases

Gene3D2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.
InterProIPR006282. Thi_PPkinase.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]
PfamPF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]
SMARTSM00983. TPK_B1_binding. 1 hit.
[Graphical view]
SUPFAMSSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
TIGRFAMsTIGR01378. thi_PPkinase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO34664.

Entry information

Entry nameTHIN_BACSU
AccessionPrimary (citable) accession number: O34664
Secondary accession number(s): Q799K8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 75 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