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P14193

- KPRS_BACSU

UniProt

P14193 - KPRS_BACSU

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Protein
Ribose-phosphate pyrophosphokinase
Gene
prs, BSU00510
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi134 – 1341Magnesium Reviewed prediction
Metal bindingi136 – 1361Magnesium Reviewed prediction
Metal bindingi145 – 1451Magnesium Reviewed prediction
Metal bindingi149 – 1491Magnesium Reviewed prediction

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
Complete GO annotation...

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
Complete GO annotation...

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 UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Ribose-phosphate pyrophosphokinaseUniRule annotation
PRO_0000141110Add
BLAST

Proteomic databases

PaxDbiP14193.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP14193.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 23014Binding of phosphoribosylpyrophosphate Reviewed prediction
Add
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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 122 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

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