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Protein

Phosphoribomutase

Gene

PRM15

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

Major phosphoribomutase that converts ribose 1-phosphate to ribose 5-phosphate. Involved in ribose salvage via the pentose phosphate pathway.1 Publication

Catalytic activityi

Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Kineticsi

  1. KM=2.0 mM for D-glucose 1-phosphate1 Publication
  2. KM=112 µM for D-glucose 1-phosphate1 Publication
  3. KM=750 µM for D-ribose 1-phosphate1 Publication

Vmax=0.11 µmol/min/mg enzyme for D-glucose 1-phosphate1 Publication

Vmax=0.29 µmol/min/mg enzyme for D-ribose 1-phosphate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571SubstrateBy similarity
Binding sitei61 – 611SubstrateBy similarity
Active sitei158 – 1581Phosphoserine intermediateBy similarity
Metal bindingi158 – 1581Magnesium; via phosphate groupBy similarity
Binding sitei168 – 1681SubstrateBy similarity
Metal bindingi325 – 3251MagnesiumBy similarity
Metal bindingi327 – 3271MagnesiumBy similarity
Metal bindingi329 – 3291MagnesiumBy similarity
Binding sitei404 – 4041SubstrateBy similarity
Binding sitei442 – 4421SubstrateBy similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphopentomutase activity Source: SGD

GO - Biological processi

  1. glucose metabolic process Source: UniProtKB-KW
  2. guanosine catabolic process Source: SGD
  3. inosine catabolic process Source: SGD
  4. purine ribonucleoside salvage Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32949-MONOMER.
ReactomeiREACT_285356. Galactose catabolism.
REACT_285362. Glycogen breakdown (glycogenolysis).
REACT_331189. Glycogen synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribomutase1 Publication (EC:5.4.2.71 Publication)
Short name:
PRM
Alternative name(s):
Phosphoglucomutase 31 Publication
Short name:
PGM 3
Gene namesi
Name:PRM151 Publication
Synonyms:PGM31 Publication
Ordered Locus Names:YMR278WImported
ORF Names:YM8021.04
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR278w.
SGDiS000004891. PRM15.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Hyperaccumulates ribose 1-phosphate and upstream purines upon glucose-induced purine nucleoside recycling.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581S → T: Loss of function. 1 Publication
Mutagenesisi326 – 3261P → G: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622PhosphoribomutasePRO_0000148022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei158 – 1581Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03262.
PaxDbiQ03262.

Expressioni

Gene expression databases

GenevestigatoriQ03262.

Interactioni

Protein-protein interaction databases

BioGridi35457. 5 interactions.
DIPiDIP-5066N.
MINTiMINT-519611.
STRINGi4932.YMR278W.

Structurei

3D structure databases

ProteinModelPortaliQ03262.
SMRiQ03262. Positions 55-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1592Substrate bindingBy similarity
Regioni329 – 3302Substrate bindingBy similarity
Regioni428 – 4303Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
InParanoidiQ03262.
KOiK01835.
OMAiVYTPFHG.
OrthoDBiEOG7ZGXC9.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03262-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQGILETVP SDLKDPISLW FKQDRNPKTI EEVTALCKKS DWNELHKRFD
60 70 80 90 100
SRIQFGTAGL RSQMQAGFSR MNTLVVIQAS QGLATYVRQQ FPDNLVAVVG
110 120 130 140 150
HDHRFHSKEF ARATAAAFLL KGFKVHYLNP DHEFVHTPLV PFAVDKLKAS
160 170 180 190 200
VGVMITASHN PKMDNGYKVY YSNGCQIIPP HDHAISDSID ANLEPWANVW
210 220 230 240 250
DFDDVLNKAL KQGKLMYSRE EMLKLYLEEV SKNLVEINPL KLEVKAKPWF
260 270 280 290 300
VYTPMHGVGF DIFSTIVKKT LCLVEGKDYL CVPEQQNPDP SFPTVGFPNP
310 320 330 340 350
EEKGALDIGI NLAEKHDIDL LVANDPDADR FSVAVKDMQS GEWRQLTGNE
360 370 380 390 400
IGFLFAFYEY QKYKSMDKEF QHVHPLAMLN STVSSQMIKK MAEIEGFHYE
410 420 430 440 450
DTLTGFKWIG NRAILLEKKG YYVPFGFEEA IGYMFPAMEH DKDGISASIV
460 470 480 490 500
FLQAYCKWKI DHNLDPLNVL ENGFKKYGVF KEYNGYYVVP NPTVTKDIFD
510 520 530 540 550
YIRNVYTPEG ASYPSSIGEE IEVLYYRDLT TGYQSDTINH KPTLPVDPTS
560 570 580 590 600
QMITVSARPS NGSENEHIRF TIRGSGTEPK LKVYIEACAN EEQRASFLAK
610 620
LTWNVLRREW FRPDEMNIVT KF
Length:622
Mass (Da):71,069
Last modified:November 1, 1997 - v1
Checksum:iE402A69551B36CD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49704 Genomic DNA. Translation: CAA89776.1.
BK006946 Genomic DNA. Translation: DAA10179.1.
PIRiS54585.
RefSeqiNP_014005.1. NM_001182785.1.

Genome annotation databases

EnsemblFungiiYMR278W; YMR278W; YMR278W.
GeneIDi855321.
KEGGisce:YMR278W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49704 Genomic DNA. Translation: CAA89776.1.
BK006946 Genomic DNA. Translation: DAA10179.1.
PIRiS54585.
RefSeqiNP_014005.1. NM_001182785.1.

3D structure databases

ProteinModelPortaliQ03262.
SMRiQ03262. Positions 55-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35457. 5 interactions.
DIPiDIP-5066N.
MINTiMINT-519611.
STRINGi4932.YMR278W.

Proteomic databases

MaxQBiQ03262.
PaxDbiQ03262.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR278W; YMR278W; YMR278W.
GeneIDi855321.
KEGGisce:YMR278W.

Organism-specific databases

CYGDiYMR278w.
SGDiS000004891. PRM15.

Phylogenomic databases

eggNOGiCOG1109.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
InParanoidiQ03262.
KOiK01835.
OMAiVYTPFHG.
OrthoDBiEOG7ZGXC9.

Enzyme and pathway databases

BioCyciYEAST:G3O-32949-MONOMER.
ReactomeiREACT_285356. Galactose catabolism.
REACT_285362. Glycogen breakdown (glycogenolysis).
REACT_331189. Glycogen synthesis.

Miscellaneous databases

NextBioi979026.

Gene expression databases

GenevestigatoriQ03262.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  6. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Molecular characterization reveals that YMR278w encoded protein is environmental stress response homologue of Saccharomyces cerevisiae PGM2."
    Tiwari A., Bhat J.P.
    Biochem. Biophys. Res. Commun. 366:340-345(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-158 AND PRO-326.
  8. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae."
    Walther T., Baylac A., Alkim C., Vax A., Cordier H., Francois J.M.
    FEBS Lett. 586:4114-4118(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
  11. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPGM3_YEAST
AccessioniPrimary (citable) accession number: Q03262
Secondary accession number(s): D6W0A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 125 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 4960 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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.