SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O34664

- THIN_BACSU

UniProt

O34664 - THIN_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Thiamine pyrophosphokinase

Gene
thiN, yloS, BSU15800
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate.

Catalytic activityi

ATP + thiamine = AMP + thiamine diphosphate.

Kineticsi

  1. KM=20 µM for thiamine
  2. KM=1 mM for ATP

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: UniProtKB-KW
  3. thiamine diphosphokinase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU15800-MONOMER.
MetaCyc:BSU15800-MONOMER.
UniPathwayiUPA00060; UER00597.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine pyrophosphokinase (EC:2.7.6.2)
Short name:
TPK
Alternative name(s):
Thiamine diphosphokinase
Gene namesi
Name:thiN
Synonyms:yloS
Ordered Locus Names:BSU15800
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU15800. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 214214Thiamine pyrophosphokinasePRO_0000072516Add
BLAST

Proteomic databases

PaxDbiO34664.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU15800.

Structurei

Secondary structure

1
214
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75
Helixi12 – 143
Helixi19 – 213
Beta strandi26 – 316
Helixi33 – 419
Beta strandi46 – 505
Helixi57 – 6610
Beta strandi71 – 733
Beta strandi77 – 793
Helixi81 – 9212
Beta strandi95 – 1017
Helixi107 – 12216
Beta strandi126 – 1316
Beta strandi134 – 1396
Beta strandi141 – 1477
Beta strandi154 – 1596
Beta strandi164 – 17411
Beta strandi176 – 1816
Beta strandi189 – 1913
Beta strandi193 – 20513
Beta strandi207 – 2126

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LM8X-ray2.60A/B/C/D1-214[»]
ProteinModelPortaliO34664.
SMRiO34664. Positions 2-214.

Miscellaneous databases

EvolutionaryTraceiO34664.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1564.
HOGENOMiHOG000037072.
KOiK00949.
OMAiITYCPEG.
OrthoDBiEOG62NX6M.
PhylomeDBiO34664.

Family and domain databases

Gene3Di2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.
InterProiIPR006282. Thi_PPkinase.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]
PfamiPF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]
SMARTiSM00983. TPK_B1_binding. 1 hit.
[Graphical view]
SUPFAMiSSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
TIGRFAMsiTIGR01378. thi_PPkinase. 1 hit.

Sequencei

Sequence statusi: Complete.

O34664-1 [UniParc]FASTAAdd to Basket

« Hide

MKTINIVAGG PKNLIPDLTG YTDEHTLWIG VDKGTVTLLD AGIIPVEAFG    50
DFDSITEQER RRIEKAAPAL HVYQAEKDQT DLDLALDWAL EKQPDIIQIF 100
GITGGRADHF LGNIQLLYKG VKTNIKIRLI DKQNHIQMFP PGEYDIEKDE 150
NKRYISFIPF SEDIHELTLT GFKYPLNNCH ITLGSTLCIS NELIHSRGTF 200
SFAKGILIMI RSTD 214
Length:214
Mass (Da):24,099
Last modified:January 1, 1998 - v1
Checksum:i77BBA150330F4679
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13937 Genomic DNA. Translation: CAA74253.1.
AL009126 Genomic DNA. Translation: CAB13453.1.
PIRiC69879.
RefSeqiNP_389462.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13453; CAB13453; BSU15800.
GeneIDi937714.
KEGGibsu:BSU15800.
PATRICi18974967. VBIBacSub10457_1675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13937 Genomic DNA. Translation: CAA74253.1 .
AL009126 Genomic DNA. Translation: CAB13453.1 .
PIRi C69879.
RefSeqi NP_389462.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LM8 X-ray 2.60 A/B/C/D 1-214 [» ]
ProteinModelPortali O34664.
SMRi O34664. Positions 2-214.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU15800.

Proteomic databases

PaxDbi O34664.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13453 ; CAB13453 ; BSU15800 .
GeneIDi 937714.
KEGGi bsu:BSU15800.
PATRICi 18974967. VBIBacSub10457_1675.

Organism-specific databases

GenoListi BSU15800. [Micado ]

Phylogenomic databases

eggNOGi COG1564.
HOGENOMi HOG000037072.
KOi K00949.
OMAi ITYCPEG.
OrthoDBi EOG62NX6M.
PhylomeDBi O34664.

Enzyme and pathway databases

UniPathwayi UPA00060 ; UER00597 .
BioCyci BSUB:BSU15800-MONOMER.
MetaCyc:BSU15800-MONOMER.

Miscellaneous databases

EvolutionaryTracei O34664.

Family and domain databases

Gene3Di 2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.
InterProi IPR006282. Thi_PPkinase.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view ]
Pfami PF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view ]
SMARTi SM00983. TPK_B1_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
TIGRFAMsi TIGR01378. thi_PPkinase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTHIN_BACSU
AccessioniPrimary (citable) accession number: O34664
Secondary accession number(s): Q799K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 77 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