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Protein

Thiamine pyrophosphokinase

Gene

thiN

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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

    Pathway:ithiamine diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes thiamine diphosphate from thiamine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Thiamine pyrophosphokinase (thiN)
    This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine diphosphate from thiamine, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    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 Componenti: 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.Bsubs1_010100008721.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    InParanoidiO34664.
    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

            10         20         30         40         50
    MKTINIVAGG PKNLIPDLTG YTDEHTLWIG VDKGTVTLLD AGIIPVEAFG
    60 70 80 90 100
    DFDSITEQER RRIEKAAPAL HVYQAEKDQT DLDLALDWAL EKQPDIIQIF
    110 120 130 140 150
    GITGGRADHF LGNIQLLYKG VKTNIKIRLI DKQNHIQMFP PGEYDIEKDE
    160 170 180 190 200
    NKRYISFIPF SEDIHELTLT GFKYPLNNCH ITLGSTLCIS NELIHSRGTF
    210
    SFAKGILIMI RSTD
    Length:214
    Mass (Da):24,099
    Last modified:January 1, 1998 - v1
    Checksum:i77BBA150330F4679
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13937 Genomic DNA. Translation: CAA74253.1.
    AL009126 Genomic DNA. Translation: CAB13453.1.
    PIRiC69879.
    RefSeqiNP_389462.1. NC_000964.3.
    WP_003245470.1. NZ_JNCM01000035.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13937 Genomic DNA. Translation: CAA74253.1.
    AL009126 Genomic DNA. Translation: CAB13453.1.
    PIRiC69879.
    RefSeqiNP_389462.1. NC_000964.3.
    WP_003245470.1. NZ_JNCM01000035.1.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100008721.

    Proteomic databases

    PaxDbiO34664.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    GenoListiBSU15800. [Micado]

    Phylogenomic databases

    eggNOGiCOG1564.
    HOGENOMiHOG000037072.
    InParanoidiO34664.
    KOiK00949.
    OMAiITYCPEG.
    OrthoDBiEOG62NX6M.
    PhylomeDBiO34664.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiO34664.

    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.
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 83 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

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.