Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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
  1. Vmax=0.11 µmol/min/mg enzyme for D-glucose 1-phosphate1 Publication
  2. Vmax=0.29 µmol/min/mg enzyme for D-ribose 1-phosphate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei57SubstrateBy similarity1
Binding sitei61SubstrateBy similarity1
Active sitei158Phosphoserine intermediateBy similarity1
Metal bindingi158Magnesium; via phosphate groupBy similarity1
Binding sitei168SubstrateBy similarity1
Metal bindingi325MagnesiumBy similarity1
Metal bindingi327MagnesiumBy similarity1
Metal bindingi329MagnesiumBy similarity1
Binding sitei404SubstrateBy similarity1
Binding sitei442SubstrateBy similarity1

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphopentomutase activity Source: SGD

GO - Biological processi

  • glucose metabolic process Source: UniProtKB-KW
  • guanosine catabolic process Source: SGD
  • inosine catabolic process Source: SGD
  • 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.
ReactomeiR-SCE-3322077. Glycogen synthesis.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-70221. Glycogen breakdown (glycogenolysis).
R-SCE-70370. Galactose catabolism.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).

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
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR278W.
SGDiS000004891. PRM15.

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi158S → T: Loss of function. 1 Publication1
Mutagenesisi326P → G: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480221 – 622PhosphoribomutaseAdd BLAST622

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei158PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03262.
PRIDEiQ03262.

PTM databases

iPTMnetiQ03262.

Interactioni

Protein-protein interaction databases

BioGridi35457. 4 interactors.
DIPiDIP-5066N.
MINTiMINT-519611.

Structurei

3D structure databases

ProteinModelPortaliQ03262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 159Substrate bindingBy similarity2
Regioni329 – 330Substrate bindingBy similarity2
Regioni428 – 430Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
InParanoidiQ03262.
KOiK01835.
OMAiVEVCAFY.
OrthoDBiEOG092C13NP.

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35457. 4 interactors.
DIPiDIP-5066N.
MINTiMINT-519611.

PTM databases

iPTMnetiQ03262.

Proteomic databases

MaxQBiQ03262.
PRIDEiQ03262.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YMR278W.
SGDiS000004891. PRM15.

Phylogenomic databases

GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
InParanoidiQ03262.
KOiK01835.
OMAiVEVCAFY.
OrthoDBiEOG092C13NP.

Enzyme and pathway databases

BioCyciYEAST:G3O-32949-MONOMER.
ReactomeiR-SCE-3322077. Glycogen synthesis.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-70221. Glycogen breakdown (glycogenolysis).
R-SCE-70370. Galactose catabolism.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

PROiQ03262.

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...

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: November 30, 2016
This is version 142 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

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.