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P14193

- KPRS_BACSU

UniProt

P14193 - KPRS_BACSU

Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi134 – 1341MagnesiumSequence Analysis
    Metal bindingi136 – 1361MagnesiumSequence Analysis
    Metal bindingi145 – 1451MagnesiumSequence Analysis
    Metal bindingi149 – 1491MagnesiumSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinase activity Source: UniProtKB-KW
    3. magnesium ion binding Source: UniProtKB-HAMAP
    4. ribose phosphate diphosphokinase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 5-phosphoribose 1-diphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. nucleotide biosynthetic process Source: UniProtKB-KW
    3. ribonucleoside monophosphate biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU00510-MONOMER.
    UniPathwayiUPA00087; UER00172.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribose-phosphate pyrophosphokinase (EC:2.7.6.1)
    Short name:
    RPPK
    Alternative name(s):
    Phosphoribosyl pyrophosphate synthase
    Short name:
    P-Rib-PP synthase
    Short name:
    PRPP synthase
    Gene namesi
    Name:prs
    Ordered Locus Names:BSU00510
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU00510. [Micado]

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Ribose-phosphate pyrophosphokinasePRO_0000141110Add
    BLAST

    Proteomic databases

    PaxDbiP14193.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    IntActiP14193. 2 interactions.
    MINTiMINT-8366005.
    STRINGi224308.BSU00510.

    Structurei

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 145
    Helixi19 – 2911
    Beta strandi36 – 405
    Beta strandi42 – 443
    Beta strandi46 – 505
    Beta strandi58 – 625
    Helixi69 – 8517
    Beta strandi89 – 979
    Turni99 – 1024
    Helixi114 – 12512
    Beta strandi129 – 1346
    Helixi138 – 1436
    Beta strandi148 – 1514
    Helixi154 – 1629
    Turni163 – 1653
    Beta strandi168 – 1758
    Helixi176 – 1783
    Helixi179 – 18810
    Beta strandi193 – 1975
    Beta strandi210 – 2134
    Beta strandi219 – 2235
    Beta strandi225 – 2295
    Helixi231 – 24212
    Beta strandi246 – 2516
    Beta strandi253 – 2553
    Helixi261 – 2666
    Beta strandi268 – 2769
    Beta strandi288 – 2936
    Helixi296 – 30813
    Helixi313 – 3153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DKRX-ray2.30A/B1-317[»]
    1DKUX-ray2.20A/B1-317[»]
    1IBSX-ray2.80A/B1-317[»]
    ProteinModelPortaliP14193.
    SMRiP14193. Positions 2-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14193.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni217 – 23014Binding of phosphoribosylpyrophosphateSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0462.
    HOGENOMiHOG000210451.
    KOiK00948.
    OMAiVNEHLME.
    OrthoDBiEOG6Z99XQ.
    PhylomeDBiP14193.

    Family and domain databases

    Gene3Di3.40.50.2020. 2 hits.
    HAMAPiMF_00583_B. RibP_PPkinase_B.
    InterProiIPR000842. PRib_PP_synth_CS.
    IPR029099. Pribosyltran_N.
    IPR029057. PRTase-like.
    IPR005946. Rib-P_diPkinase.
    [Graphical view]
    PfamiPF14572. Pribosyl_synth. 1 hit.
    PF13793. Pribosyltran_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
    PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14193-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNQYGDKNL KIFSLNSNPE LAKEIADIVG VQLGKCSVTR FSDGEVQINI    50
    EESIRGCDCY IIQSTSDPVN EHIMELLIMV DALKRASAKT INIVIPYYGY 100
    ARQDRKARSR EPITAKLFAN LLETAGATRV IALDLHAPQI QGFFDIPIDH 150
    LMGVPILGEY FEGKNLEDIV IVSPDHGGVT RARKLADRLK APIAIIDKRR 200
    PRPNVAEVMN IVGNIEGKTA ILIDDIIDTA GTITLAANAL VENGAKEVYA 250
    CCTHPVLSGP AVERINNSTI KELVVTNSIK LPEEKKIERF KQLSVGPLLA 300
    EAIIRVHEQQ SVSYLFS 317
    Length:317
    Mass (Da):34,868
    Last modified:January 1, 1990 - v1
    Checksum:i0D37FC81668111EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16518 Genomic DNA. Translation: CAA34523.1.
    D26185 Genomic DNA. Translation: BAA05286.1.
    AL009126 Genomic DNA. Translation: CAB11827.1.
    PIRiS05372. KIBSRS.
    RefSeqiNP_387932.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB11827; CAB11827; BSU00510.
    GeneIDi936985.
    KEGGibsu:BSU00510.
    PATRICi18971573. VBIBacSub10457_0052.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16518 Genomic DNA. Translation: CAA34523.1 .
    D26185 Genomic DNA. Translation: BAA05286.1 .
    AL009126 Genomic DNA. Translation: CAB11827.1 .
    PIRi S05372. KIBSRS.
    RefSeqi NP_387932.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DKR X-ray 2.30 A/B 1-317 [» ]
    1DKU X-ray 2.20 A/B 1-317 [» ]
    1IBS X-ray 2.80 A/B 1-317 [» ]
    ProteinModelPortali P14193.
    SMRi P14193. Positions 2-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P14193. 2 interactions.
    MINTi MINT-8366005.
    STRINGi 224308.BSU00510.

    Proteomic databases

    PaxDbi P14193.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB11827 ; CAB11827 ; BSU00510 .
    GeneIDi 936985.
    KEGGi bsu:BSU00510.
    PATRICi 18971573. VBIBacSub10457_0052.

    Organism-specific databases

    GenoListi BSU00510. [Micado ]

    Phylogenomic databases

    eggNOGi COG0462.
    HOGENOMi HOG000210451.
    KOi K00948.
    OMAi VNEHLME.
    OrthoDBi EOG6Z99XQ.
    PhylomeDBi P14193.

    Enzyme and pathway databases

    UniPathwayi UPA00087 ; UER00172 .
    BioCyci BSUB:BSU00510-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14193.

    Family and domain databases

    Gene3Di 3.40.50.2020. 2 hits.
    HAMAPi MF_00583_B. RibP_PPkinase_B.
    InterProi IPR000842. PRib_PP_synth_CS.
    IPR029099. Pribosyltran_N.
    IPR029057. PRTase-like.
    IPR005946. Rib-P_diPkinase.
    [Graphical view ]
    Pfami PF14572. Pribosyl_synth. 1 hit.
    PF13793. Pribosyltran_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    TIGRFAMsi TIGR01251. ribP_PPkin. 1 hit.
    PROSITEi PS00114. PRPP_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the tms and prs genes of Bacillus subtilis."
      Nilsson D., Hove-Jensen B., Arnvig K.
      Mol. Gen. Genet. 218:565-571(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
      Ogasawara N., Nakai S., Yoshikawa H.
      DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "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.
    4. "Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase."
      Eriksen T.A., Kadziola A., Bentsen A.-K., Harlow K.W., Larsen S.
      Nat. Struct. Biol. 7:303-308(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiKPRS_BACSU
    AccessioniPrimary (citable) accession number: P14193
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 123 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