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Protein

Ribose-phosphate pyrophosphokinase 1

Gene

PRS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5).2 Publications

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.3 Publications

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase 2 (PRS2), Ribose-phosphate pyrophosphokinase 4 (PRS4), Ribose-phosphate pyrophosphokinase 1 (PRS1), Ribose-phosphate pyrophosphokinase 5 (PRS5), Ribose-phosphate pyrophosphokinase 3 (PRS3)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281MagnesiumSequence analysis
Metal bindingi130 – 1301MagnesiumSequence analysis
Metal bindingi143 – 1431MagnesiumSequence analysis

GO - Molecular functioni

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: SGD
  • fungal-type cell wall organization Source: SGD
  • nucleotide biosynthetic process Source: UniProtKB-KW
  • ribonucleoside monophosphate biosynthetic process Source: InterPro
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

BioCyciYEAST:YKL181W-MONOMER.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 1 (EC:2.7.6.1)
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 1
Gene namesi
Name:PRS1
Synonyms:PPS1, PRP1, PRPS, PRPS1
Ordered Locus Names:YKL181W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL181W.
SGDiS000001664. PRS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • ribose phosphate diphosphokinase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Ribose-phosphate pyrophosphokinase 1PRO_0000141086Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei271 – 2711PhosphoserineCombined sources
Modified residuei295 – 2951PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32895.
PeptideAtlasiP32895.

PTM databases

iPTMnetiP32895.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PRS2P386203EBI-9869,EBI-9873
PRS3P386894EBI-9869,EBI-9877

Protein-protein interaction databases

BioGridi33941. 38 interactions.
DIPiDIP-4857N.
IntActiP32895. 10 interactions.
MINTiMINT-488484.

Structurei

3D structure databases

ProteinModelPortaliP32895.
SMRiP32895. Positions 5-197, 310-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000076044.
HOGENOMiHOG000210451.
InParanoidiP32895.
KOiK00948.
OMAiPMTMSHA.
OrthoDBiEOG78M0B7.

Family and domain databases

Gene3Di3.40.50.2020. 3 hits.
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. 3 hits.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32895-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKCKIFVGN SHPELGNMVC QRLGIEPAPC TLKKFANGET SVQIGVSVRD
60 70 80 90 100
EDVYVIQSGS PSINDDIMEL LILVSACRGG SARKITAVIP QFPYSKQCKM
110 120 130 140 150
KRHRGAITAR MLANLLVMAG ADHVVSMDLH ASQMQGFFTK PVDNLYGGPS
160 170 180 190 200
LAKWIRENVE DYEDAVVVSK NPGGTKRVTA LADSLKINFA MIHTDRRRSK
210 220 230 240 250
DLYSQNKDLQ QLKLRKQSML RKNRPIIRQG DHPNEEENII LSNGIQTARI
260 270 280 290 300
RNGHVIGDDE ADDDEDAILE SDSELHSIDG LDSHGLGGTY DAVDSEDEEE
310 320 330 340 350
IPVLYREQLI TLVGNVRGRS AIILDDMIDR PGSFISAAEH LVQNCGAKKV
360 370 380 390 400
YVVATHGIFT GDCLEELEKS DAIDTIVVTN TYPISGERIA GSKKLVTIDV
410 420
SPIFAECIRR DHYGESISVL FDSLAAL
Length:427
Mass (Da):47,047
Last modified:October 1, 1993 - v1
Checksum:iF3E93ACB25E703FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04130 Genomic DNA. Translation: AAA21811.1.
X70069 Genomic DNA. Translation: CAA49674.1.
X74151 Genomic DNA. Translation: CAA52257.1.
Z28181 Genomic DNA. Translation: CAA82024.1.
BK006944 Genomic DNA. Translation: DAA08986.1.
PIRiS30558.
RefSeqiNP_012740.1. NM_001179747.1.

Genome annotation databases

EnsemblFungiiYKL181W; YKL181W; YKL181W.
GeneIDi853654.
KEGGisce:YKL181W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04130 Genomic DNA. Translation: AAA21811.1.
X70069 Genomic DNA. Translation: CAA49674.1.
X74151 Genomic DNA. Translation: CAA52257.1.
Z28181 Genomic DNA. Translation: CAA82024.1.
BK006944 Genomic DNA. Translation: DAA08986.1.
PIRiS30558.
RefSeqiNP_012740.1. NM_001179747.1.

3D structure databases

ProteinModelPortaliP32895.
SMRiP32895. Positions 5-197, 310-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33941. 38 interactions.
DIPiDIP-4857N.
IntActiP32895. 10 interactions.
MINTiMINT-488484.

PTM databases

iPTMnetiP32895.

Proteomic databases

MaxQBiP32895.
PeptideAtlasiP32895.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL181W; YKL181W; YKL181W.
GeneIDi853654.
KEGGisce:YKL181W.

Organism-specific databases

EuPathDBiFungiDB:YKL181W.
SGDiS000001664. PRS1.

Phylogenomic databases

GeneTreeiENSGT00550000076044.
HOGENOMiHOG000210451.
InParanoidiP32895.
KOiK00948.
OMAiPMTMSHA.
OrthoDBiEOG78M0B7.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciYEAST:YKL181W-MONOMER.

Miscellaneous databases

PROiP32895.

Family and domain databases

Gene3Di3.40.50.2020. 3 hits.
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. 3 hits.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Saccharomyces cerevisiae mutation elm4-1 facilitates pseudohyphal differentiation and interacts with a deficiency in phosphoribosylpyrophosphate synthase activity to cause constitutive pseudohyphal growth."
    Blacketer M.J., Madaule P., Myers A.M.
    Mol. Cell. Biol. 14:4671-4681(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in Saccharomyces cerevisiae."
    Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M.
    Yeast 10:1031-1044(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  3. "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene."
    Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.
    Yeast 9:1343-1348(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "PRS1 is a key member of the gene family encoding phosphoribosylpyrophosphate synthetase in Saccharomyces cerevisiae."
    Carter A.T., Beiche F., Hove-Jensen B., Narbad A., Barker P.J., Schweizer L.M., Schweizer M.
    Mol. Gen. Genet. 254:148-156(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY.
  7. "Genetic analysis and enzyme activity suggest the existence of more than one minimal functional unit capable of synthesizing phosphoribosyl pyrophosphate in Saccharomyces cerevisiae."
    Hernando Y., Carter A.T., Parr A., Hove-Jensen B., Schweizer M.
    J. Biol. Chem. 274:12480-12487(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Heterooligomeric phosphoribosyl diphosphate synthase of Saccharomyces cerevisiae: combinatorial expression of the five PRS genes in Escherichia coli."
    Hove-Jensen B.
    J. Biol. Chem. 279:40345-40350(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-271 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKPR1_YEAST
AccessioniPrimary (citable) accession number: P32895
Secondary accession number(s): D6VX20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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 one 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.