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Protein

Ribose-phosphate pyrophosphokinase 5

Gene

PRS5

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).3 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 bindingi242 – 2421MagnesiumSequence analysis
Metal bindingi244 – 2441MagnesiumSequence analysis
Metal bindingi253 – 2531MagnesiumSequence analysis
Metal bindingi257 – 2571MagnesiumSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: InterPro
  • ribose phosphate diphosphokinase activity Source: SGD

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:YOL061W-MONOMER.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 5 (EC:2.7.6.1)
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 5
Gene namesi
Name:PRS5
Synonyms:PRPS5
Ordered Locus Names:YOL061W
ORF Names:O1213
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL061W.
SGDiS000005422. PRS5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Ribose-phosphate pyrophosphokinase 5PRO_0000141090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei119 – 1191PhosphotyrosineCombined sources
Modified residuei120 – 1201PhosphothreonineCombined sources
Modified residuei123 – 1231PhosphoserineCombined sources
Modified residuei127 – 1271PhosphothreonineCombined sources
Modified residuei183 – 1831PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12265.

PTM databases

iPTMnetiQ12265.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PRS2P386204EBI-9886,EBI-9873

Protein-protein interaction databases

BioGridi34340. 56 interactions.
DIPiDIP-1532N.
IntActiQ12265. 7 interactions.
MINTiMINT-404255.

Structurei

3D structure databases

ProteinModelPortaliQ12265.
SMRiQ12265. Positions 5-99, 222-315, 383-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000076044.
HOGENOMiHOG000210451.
InParanoidiQ12265.
KOiK00948.
OMAiCKSASAS.
OrthoDBiEOG78M0B7.

Family and domain databases

Gene3Di3.40.50.2020. 4 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. 4 hits.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMSNIVVFG GDSHPELVTK ICENLDIHPS KVELGKFSNG ETNIALRESV
60 70 80 90 100
REKDVYIIQS GCGQVNDTFM QLLILISACK SASASRVTAV MPYLCYSRQP
110 120 130 140 150
DIPYTAKGAP IISKPKENYT FESHPGTPVS SSLMTQRPGA ESSLKSLDSA
160 170 180 190 200
IRSTINLENP QPIRTPNSSA TANNNFDIKK TLSFSRIPMI PGGKLQNTSN
210 220 230 240 250
STDAGELFNA QNAGYKLWVV QAGTLIAHLL SAAGADHVIT MDLHDPQFPG
260 270 280 290 300
FFDIPVDNLY CKPIAQNYIQ HRIPDYQDAV IVSPDAGGAK RATAIADALE
310 320 330 340 350
LSFALIHKER RSQLLKGPPD ATLTSGGSLP VSPRPLVTTL VSSQNTTSSG
360 370 380 390 400
ATGVAALEMK KTTSTSSTSS QSSNSSKFVQ TTMLVGDVRN KVCIIVDDLV
410 420 430 440 450
DTSYTITRAA KLLKDQGSTK VYALITHGVF SGDALERIGQ SSIDKLIISN
460 470 480 490
TVPQDRTLQY LGKDRVDVID VSCIIGEAIR RIHNGESISM LFEHGW
Length:496
Mass (Da):53,505
Last modified:November 1, 1996 - v1
Checksum:i75C948D40D58256D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74803 Genomic DNA. Translation: CAA99070.1.
X91067 Genomic DNA. Translation: CAA62523.1.
BK006948 Genomic DNA. Translation: DAA10722.1.
PIRiS61716.
RefSeqiNP_014580.1. NM_001183316.1.

Genome annotation databases

EnsemblFungiiYOL061W; YOL061W; YOL061W.
GeneIDi854093.
KEGGisce:YOL061W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74803 Genomic DNA. Translation: CAA99070.1.
X91067 Genomic DNA. Translation: CAA62523.1.
BK006948 Genomic DNA. Translation: DAA10722.1.
PIRiS61716.
RefSeqiNP_014580.1. NM_001183316.1.

3D structure databases

ProteinModelPortaliQ12265.
SMRiQ12265. Positions 5-99, 222-315, 383-494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34340. 56 interactions.
DIPiDIP-1532N.
IntActiQ12265. 7 interactions.
MINTiMINT-404255.

PTM databases

iPTMnetiQ12265.

Proteomic databases

MaxQBiQ12265.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL061W; YOL061W; YOL061W.
GeneIDi854093.
KEGGisce:YOL061W.

Organism-specific databases

EuPathDBiFungiDB:YOL061W.
SGDiS000005422. PRS5.

Phylogenomic databases

GeneTreeiENSGT00550000076044.
HOGENOMiHOG000210451.
InParanoidiQ12265.
KOiK00948.
OMAiCKSASAS.
OrthoDBiEOG78M0B7.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciYEAST:YOL061W-MONOMER.

Miscellaneous databases

PROiQ12265.

Family and domain databases

Gene3Di3.40.50.2020. 4 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. 4 hits.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
    Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
    Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90843 / S288c / FY73.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "PRS5, the fifth member of the phosphoribosyl pyrophosphate synthetase gene family in Saccharomyces cerevisiae, is essential for cell viability in the absence of either PRS1 or PRS3."
    Hernando Y., Parr A., Schweizer M.
    J. Bacteriol. 180:6404-6407(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.
  5. "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.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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.
  9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-119; THR-120; SER-123 AND THR-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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-183, 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 THR-127 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKPR5_YEAST
AccessioniPrimary (citable) accession number: Q12265
Secondary accession number(s): D6W206
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 144 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 3310 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.