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O34664

- THIN_BACSU

UniProt

O34664 - THIN_BACSU

Protein

Thiamine pyrophosphokinase

Gene

thiN

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO34664.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiamine pyrophosphokinase family.Curated

    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

    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: October 1, 2014
    This is version 78 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