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Protein

Phosphoglucomutase 2

Gene

PGM2

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 phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate (PubMed:5784209). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (PubMed:14264884).2 Publications

Catalytic activityi

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.3 Publications

Cofactori

Mg2+2 Publications, Zn2+2 PublicationsNote: Binds 1 magnesium ion per subunit. Can also use Zn2+ as cofactor.2 Publications

Kineticsi

  1. KM=2.24 µM for alpha-D-glucose 1,6-diphosphate1 Publication
  2. KM=23.4 µM for alpha-D-glucose 1-phosphate1 Publication
  3. KM=26 µM for alpha-D-glucose 1-phosphate1 Publication
  4. KM=530 µM for D-ribose 1-phosphate1 Publication

Vmax=33.7 µmol/min/mg enzyme for alpha-D-glucose 1-phosphate1 Publication

Vmax=0.32 µmol/min/mg enzyme for D-ribose 1-phosphate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201SubstrateBy similarity
Binding sitei24 – 241SubstrateBy similarity
Active sitei119 – 1191Phosphoserine intermediateBy similarity
Metal bindingi119 – 1191Magnesium; via phosphate groupBy similarity
Binding sitei132 – 1321SubstrateBy similarity
Metal bindingi290 – 2901MagnesiumBy similarity
Metal bindingi292 – 2921MagnesiumBy similarity
Metal bindingi294 – 2941MagnesiumBy similarity
Binding sitei359 – 3591SubstrateBy similarity
Binding sitei391 – 3911SubstrateBy similarity
Binding sitei522 – 5221SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular calcium ion homeostasis Source: SGD
  2. cellular cation homeostasis Source: SGD
  3. galactose catabolic process Source: SGD
  4. glucose 1-phosphate metabolic process Source: SGD
  5. glucose 6-phosphate metabolic process Source: SGD
  6. glucose metabolic process Source: UniProtKB-KW
  7. glycogen biosynthetic process Source: SGD
  8. trehalose biosynthetic process Source: SGD
  9. UDP-glucose metabolic process 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

BioCyciMetaCyc:MONOMER-17136.
YEAST:YMR105C-MONOMER.
ReactomeiREACT_191292. Glycogen synthesis.
REACT_232344. Galactose catabolism.
REACT_244738. Glycogen breakdown (glycogenolysis).
SABIO-RKP37012.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase 21 Publication (EC:5.4.2.23 Publications)
Short name:
PGM 21 Publication
Alternative name(s):
D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase1 Publication
Glucose phosphomutase 2
Gene namesi
Name:PGM21 Publication
Synonyms:GA-51 Publication, GAL51 Publication
Ordered Locus Names:YMR105CImported
ORF Names:YM9718.04C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR105c.
SGDiS000004711. PGM2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Blocks galactose utilization, but does not impair growth on glucose.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 569568Phosphoglucomutase 2PRO_0000147797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei111 – 1111Phosphothreonine1 Publication
Modified residuei117 – 1171Phosphothreonine1 Publication
Modified residuei119 – 1191Phosphoserine2 Publications

Post-translational modificationi

O-glycosylated with mannose residues (By similarity). Substrate of UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose in a phosphodiester linkage to O-linked mannose (PubMed:8385141, PubMed:7929458).By similarity2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP37012.
PaxDbiP37012.
PeptideAtlasiP37012.
PRIDEiP37012.

Expressioni

Inductioni

Induced in response to galactose and severely repressed in response to glucose.1 Publication

Gene expression databases

ExpressionAtlasiP37012. differential.
GenevestigatoriP37012.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi35280. 85 interactions.
DIPiDIP-6499N.
IntActiP37012. 13 interactions.
MINTiMINT-705119.
STRINGi4932.YMR105C.

Structurei

3D structure databases

ProteinModelPortaliP37012.
SMRiP37012. Positions 4-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 1202Substrate bindingBy similarity
Regioni294 – 2952Substrate bindingBy similarity
Regioni378 – 3803Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG0033.
GeneTreeiENSGT00390000011831.
HOGENOMiHOG000009550.
InParanoidiP37012.
KOiK01835.
OMAiSIQNCIP.
OrthoDBiEOG70S7FF.

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.
IPR005841. Alpha-D-phosphohexomutase_SF.
[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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE
60 70 80 90 100
GSKGATLVVG GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS
110 120 130 140 150
HIMRTYEEKC TGGIILTASH NPGGPENDMG IKYNLSNGGP APESVTNAIW
160 170 180 190 200
EISKKLTSYK IIKDFPELDL GTIGKNKKYG PLLVDIIDIT KDYVNFLKEI
210 220 230 240 250
FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD EFGLPADEVL
260 270 280 290 300
QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG
310 320 330 340 350
YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH
360 370 380 390 400
GLNCYEVPTG WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW
410 420 430 440 450
LNILAIYNKH HPENEASIKT IQNEFWAKYG RTFFTRYDFE KVETEKANKI
460 470 480 490 500
VDQLRAYVTK SGVVNSAFPA DESLKVTDCG DFSYTDLDGS VSDHQGLYVK
510 520 530 540 550
LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE EYLKPIINSV
560
IKFLNFKQVL GTEEPTVRT
Length:569
Mass (Da):63,089
Last modified:June 1, 1994 - v1
Checksum:i45B78AFF8197645E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271T → G AA sequence (PubMed:8385141).Curated
Sequence conflicti32 – 321D → G AA sequence (PubMed:8385141).Curated
Sequence conflicti272 – 2721S → A AA sequence (PubMed:8385141).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74823 Genomic DNA. Translation: CAA52820.1.
U09499 Genomic DNA. Translation: AAA91282.1.
Z49702 Genomic DNA. Translation: CAA89741.1.
AY723853 Genomic DNA. Translation: AAU09770.1.
BK006946 Genomic DNA. Translation: DAA10001.1.
PIRiS41200.
RefSeqiNP_013823.1. NM_001182605.1.

Genome annotation databases

EnsemblFungiiYMR105C; YMR105C; YMR105C.
GeneIDi855131.
KEGGisce:YMR105C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74823 Genomic DNA. Translation: CAA52820.1.
U09499 Genomic DNA. Translation: AAA91282.1.
Z49702 Genomic DNA. Translation: CAA89741.1.
AY723853 Genomic DNA. Translation: AAU09770.1.
BK006946 Genomic DNA. Translation: DAA10001.1.
PIRiS41200.
RefSeqiNP_013823.1. NM_001182605.1.

3D structure databases

ProteinModelPortaliP37012.
SMRiP37012. Positions 4-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35280. 85 interactions.
DIPiDIP-6499N.
IntActiP37012. 13 interactions.
MINTiMINT-705119.
STRINGi4932.YMR105C.

Proteomic databases

MaxQBiP37012.
PaxDbiP37012.
PeptideAtlasiP37012.
PRIDEiP37012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR105C; YMR105C; YMR105C.
GeneIDi855131.
KEGGisce:YMR105C.

Organism-specific databases

CYGDiYMR105c.
SGDiS000004711. PGM2.

Phylogenomic databases

eggNOGiCOG0033.
GeneTreeiENSGT00390000011831.
HOGENOMiHOG000009550.
InParanoidiP37012.
KOiK01835.
OMAiSIQNCIP.
OrthoDBiEOG70S7FF.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17136.
YEAST:YMR105C-MONOMER.
ReactomeiREACT_191292. Glycogen synthesis.
REACT_232344. Galactose catabolism.
REACT_244738. Glycogen breakdown (glycogenolysis).
SABIO-RKP37012.

Miscellaneous databases

NextBioi978502.

Gene expression databases

ExpressionAtlasiP37012. differential.
GenevestigatoriP37012.

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.
IPR005841. Alpha-D-phosphohexomutase_SF.
[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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of hexosephosphate mutases in Saccharomyces cerevisiae."
    Boles E., Liebetrau W., Hofmann M., Zimmermann F.K.
    Eur. J. Biochem. 220:83-96(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Fu L., Bounelis P., Dey N., Browne B.L., Marchase R.B., Bedwell D.M.
    Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase."
    Marchase R.B., Bounelis P., Brumley L.M., Dey N., Browne B., Auger D., Fritz T.A., Kulesza P., Bedwell D.M.
    J. Biol. Chem. 268:8341-8349(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-32 AND 265-275, SUBCELLULAR LOCATION, GLYCOSYLATION.
  7. "A mutation in Saccharomyces that affects phosphoglucomutase activity and galactose utilization."
    Douglas H.C.
    Biochim. Biophys. Acta 52:209-211(1961) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "The effect of mutation of two forms of phosphoglucomutase in Saccharomyces."
    Tsoi A., Douglas H.C.
    Biochim. Biophys. Acta 92:513-520(1964) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: 8050B.
  9. Cited for: FUNCTION.
  10. "Genetic control of phosphoglucomutase variants in Saccharomyces cerevisiae."
    Bevan P., Douglas H.C.
    J. Bacteriol. 98:532-535(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Crystallization and reaction mechanism of yeast phosphoglucomutase."
    Hirose M., Sugimoto E., Sasaki R., Chiaa H.
    J. Biochem. 68:449-457(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  12. "Studies on crystalline yeast phosphoglucomutase: the presence of intrinsic zinc."
    Hirose M., Sugimoto E., Chiba H.
    Biochim. Biophys. Acta 289:137-146(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  13. "Purification and properties of phosphoglucomutase from Fleischmann's yeast."
    Daugherty J.P., Kraemer W.F., Joshi J.G.
    Eur. J. Biochem. 57:115-126(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  14. "Transcription of a yeast phosphoglucomutase isozyme gene is galactose inducible and glucose repressible."
    Oh D., Hopper J.E.
    Mol. Cell. Biol. 10:1415-1422(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  15. "The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae."
    Dey N.B., Bounelis P., Fritz T.A., Bedwell D.M., Marchase R.B.
    J. Biol. Chem. 269:27143-27148(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  18. "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-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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 THR-111; THR-117 AND SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPGM2_YEAST
AccessioniPrimary (citable) accession number: P37012
Secondary accession number(s): D6VZS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 7, 2015
This is version 136 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 3790 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.