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Protein

Phosphoglucomutase

Gene

Pgm

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

This enzyme participates in both the breakdown and synthesis of glucose.1 Publication

Catalytic activityi

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=140 µM for glucose-1-phosphate (for Pgm-A at pH 6.0)1 Publication
  2. KM=158 µM for glucose-1-phosphate (for Pgm-A at pH 7.4)1 Publication
  3. KM=4.4 µM for glucose-1,6-diphosphate (for Pgm-A at pH 6.0)1 Publication
  4. KM=4.4 µM for glucose-1,6-diphosphate (for Pgm-A at pH 7.4)1 Publication
  5. KM=142.2 µM for glucose-1-phosphate (for Pgm-B at pH 6.0)1 Publication
  6. KM=112.4 µM for glucose-1-phosphate (for Pgm-B at pH 7.4)1 Publication
  7. KM=21.7 µM for glucose-1,6-diphosphate (for Pgm-B at pH 6.0)1 Publication
  8. KM=4.2 µM for glucose-1,6-diphosphate (for Pgm-B at pH 7.4)1 Publication
  1. Vmax=32.8 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-A at pH 6.0)1 Publication
  2. Vmax=129 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-A at pH 7.4)1 Publication
  3. Vmax=20.8 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-A at pH 6.0)1 Publication
  4. Vmax=111 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-A at pH 7.4)1 Publication
  5. Vmax=35 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-B at pH 6.0)1 Publication
  6. Vmax=120.9 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-B at pH 7.4)1 Publication
  7. Vmax=14.5 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-B at pH 6.0)1 Publication
  8. Vmax=100 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-B at pH 7.4)1 Publication

pH dependencei

Optimum pH is 7.4-7.6.1 Publication

Temperature dependencei

Pgm-A is more thermostable than Pgm-B.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20SubstrateBy similarity1
Binding sitei24SubstrateBy similarity1
Active sitei116Phosphoserine intermediateBy similarity1
Metal bindingi116Magnesium; via phosphate groupBy similarity1
Binding sitei129SubstrateBy similarity1
Metal bindingi288MagnesiumBy similarity1
Metal bindingi290MagnesiumBy similarity1
Metal bindingi292MagnesiumBy similarity1
Binding sitei357SubstrateBy similarity1
Binding sitei389SubstrateBy similarity1
Binding sitei515SubstrateBy similarity1

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphoglucomutase activity Source: FlyBase

GO - Biological processi

  • galactose catabolic process Source: GO_Central
  • glucose metabolic process Source: GO_Central
  • glycogen biosynthetic process Source: FlyBase

Keywordsi

Molecular functionIsomerase
Biological processCarbohydrate metabolism, Glucose metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-3322077 Glycogen synthesis
R-DME-6798695 Neutrophil degranulation
R-DME-70221 Glycogen breakdown (glycogenolysis)
R-DME-70370 Galactose catabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase (EC:5.4.2.2)
Short name:
PGM
Alternative name(s):
Glucose phosphomutase
Gene namesi
Name:PgmImported
ORF Names:CG5165
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003076 Pgm

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001477891 – 560PhosphoglucomutaseAdd BLAST560

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VUY9
PRIDEiQ9VUY9

PTM databases

iPTMnetiQ9VUY9

Expressioni

Tissue specificityi

Localized primarily to fat bodies in third instar larvae.1 Publication

Gene expression databases

BgeeiFBgn0003076
GenevisibleiQ9VUY9 DM

Interactioni

Protein-protein interaction databases

BioGridi68773, 5 interactors
IntActiQ9VUY9, 7 interactors
STRINGi7227.FBpp0075247

Structurei

3D structure databases

ProteinModelPortaliQ9VUY9
SMRiQ9VUY9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni116 – 117Substrate bindingBy similarity2
Regioni292 – 293Substrate bindingBy similarity2
Regioni376 – 378Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the phosphohexose mutase family.1 Publication

Phylogenomic databases

eggNOGiKOG0625 Eukaryota
COG0033 LUCA
GeneTreeiENSGT00390000011831
InParanoidiQ9VUY9
KOiK01835
OMAiDIYKIYA
OrthoDBiEOG091G0HZ0
PhylomeDBiQ9VUY9

Family and domain databases

InterProiView protein in InterPro
IPR005844 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
IPR036900 A-D-PHexomutase_C_sf
IPR016066 A-D-PHexomutase_CS
IPR005841 Alpha-D-phosphohexomutase_SF
PfamiView protein in Pfam
PF02878 PGM_PMM_I, 1 hit
PF02879 PGM_PMM_II, 1 hit
PF02880 PGM_PMM_III, 1 hit
PF00408 PGM_PMM_IV, 1 hit
PRINTSiPR00509 PGMPMM
SUPFAMiSSF53738 SSF53738, 3 hits
SSF55957 SSF55957, 1 hit
PROSITEiView protein in PROSITE
PS00710 PGM_PMM, 1 hit

Sequencei

Sequence statusi: Complete.

Q9VUY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLTVEIVAT KPYEGQKPGT SGLRKKVKVF TQPNYTENFV QAILEANGAA
60 70 80 90 100
LAGSTLVVGG DGRFYCKEAA ELIVRLSAAN GVSKLLVGQN GILSTPAVSS
110 120 130 140 150
LIRHNKALGG IVLTASHNPG GPENDFGIKF NCENGGPAPD AFTNHIYKIT
160 170 180 190 200
TEIKEYKLVR NLQIDISKVG VTSFDIAGKP FTVEVIDSVA NYVRHMEEIF
210 220 230 240 250
DFAKLKDFVS GKATGKPLKM RIDAMNGVTG SYVREIFLNR LGATESSVVH
260 270 280 290 300
TTPLPDFGGL HPDPNLTYAK DLVDTVAQGD YDIGAAFDGD GDRNMIIGSK
310 320 330 340 350
AFFVTPSDSL AVIAHYLEAI PYFQKNGVQG FARSMPTASA VDLVGRKLGK
360 370 380 390 400
EVFEVPTGWK YFGNLMDAGR LCLCGEESFG TGSNHIREKD GIWAVLAWIS
410 420 430 440 450
VMQHTGKGIE DILKQHWSVY GRNYFTRYDY EECASDPCNE MVATMEKTIT
460 470 480 490 500
APEFVGKSYS SGGKTYKVKE ADNFSYTDPV DKSVATKQGL RIVFEDGSRI
510 520 530 540 550
VVRLSGTGSS GATVRLYIDS YEKENVLGQA SVMLKPLIDI ALEISQLPKF
560
TGRNAPTVIT
Length:560
Mass (Da):60,766
Last modified:May 1, 2000 - v1
Checksum:i10320D78D41C1BEC
GO

Polymorphismi

The polymorphisms show clinal variations. There are 2 common electrophoretic variants, Pgm-A and Pgm-B, which differ in their kinetic and stability parameters. Variations in Pgm are associated with differences in enzyme activity and glycogen content.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti6E → G1 Publication1
Natural varianti9A → T in strain: dpf95_94.1 and zim_26H. 4 Publications1
Natural varianti17K → Q1 Publication1
Natural varianti28K → N1 Publication1
Natural varianti36T → M2 Publications1
Natural varianti50A → V in strain: zim_38H. 1 Publication1
Natural varianti52A → I in strain: zim_36H. 2 Publications1
Natural varianti52A → V in strain: dpf95_48.2, dpf95_100.3 and hfl97_93.0. 2 Publications1
Natural varianti64F → Y in strain: zim_36H. 1 Publication1
Natural varianti109G → A in strain: B4039. 1 Publication1
Natural varianti197E → K in strain: dpf95_56.1. 2 Publications1
Natural varianti235E → K in strain: dpf95_13.0. 2 Publications1
Natural varianti240R → L in strain: dpf95_38.3 and dpf95_4.2. 4 Publications1
Natural varianti245E → D in strain: dpf95_38.3 and dpf95_4.2. 4 Publications1
Natural varianti338A → S in strain: dpf95_36.4. 2 Publications1
Natural varianti341V → M in strain: B4039, dpf95_77.4 and dpf95_90.2. 3 Publications1
Natural varianti346R → K in strain: dpf95_90.2, hfl97_1.0, hfl97_13.0, hfl97_15.0, hfl97_50.0, md90_709.1, zim_36H and zim_39H. 2 Publications1
Natural varianti351E → K1 Publication1
Natural varianti465T → S in strain: dpf95_29.3. 3 Publications1
Natural varianti484V → L in strain: dpf95_38.3, dpf95_4.2, dpf95_44.3, dpf95_48.2, dpf95_53.1, dpf95_56.1, dpf95_85.1, hfl97_1.0, hfl97_13.0, hfl97_15.0, hfl97_50.0, hfl97_93.0, md90_709.1, zim_11S, zim_23H, zim_35S, zim_36H, zim_38H, zim_39H, zim_44H, zim_48S and zim_49S. 3 Publications1
Natural varianti530A → T in strain: dpf95_44.3, dpf95_53.1 and dpf95_85.1. 3 Publications1
Natural varianti540I → F in strain: zim_48S. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290313 Genomic DNA Translation: AAG44900.1
AF290314 Genomic DNA Translation: AAG44901.1
AF290315 Genomic DNA Translation: AAG44902.1
AF290316 Genomic DNA Translation: AAG44903.1
AF290317 Genomic DNA Translation: AAG44904.1
AF290318 Genomic DNA Translation: AAG44905.1
AF290319 Genomic DNA Translation: AAG44906.1
AF290320 Genomic DNA Translation: AAG44907.1
AF290321 Genomic DNA Translation: AAG44908.1
AF290322 Genomic DNA Translation: AAG44909.1
AF290323 Genomic DNA Translation: AAG44910.1
AF290324 Genomic DNA Translation: AAG44911.1
AF290325 Genomic DNA Translation: AAG44912.1
AF290326 Genomic DNA Translation: AAG44913.1
AF290327 Genomic DNA Translation: AAG44914.1
AF290328 Genomic DNA Translation: AAG44915.1
AF290329 Genomic DNA Translation: AAG44916.1
AF290330 Genomic DNA Translation: AAG44917.1
AF290331 Genomic DNA Translation: AAG44918.1
AF290332 Genomic DNA Translation: AAG44919.1
AF290333 Genomic DNA Translation: AAG44920.1
AF290334 Genomic DNA Translation: AAG44921.1
AF290335 Genomic DNA Translation: AAG44922.1
AF290336 Genomic DNA Translation: AAG44923.1
AF290337 Genomic DNA Translation: AAG44924.1
AF290338 Genomic DNA Translation: AAG44925.1
AF290339 Genomic DNA Translation: AAG44926.1
AF290340 Genomic DNA Translation: AAG44927.1
AF290341 Genomic DNA Translation: AAG44928.1
AF290342 Genomic DNA Translation: AAG44929.1
AF290343 Genomic DNA Translation: AAG44930.1
AF290344 Genomic DNA Translation: AAG44931.1
AF290345 Genomic DNA Translation: AAG44932.1
AF290346 Genomic DNA Translation: AAG44933.1
AF290347 Genomic DNA Translation: AAG44934.1
AF290348 Genomic DNA Translation: AAG44935.1
AF290349 Genomic DNA Translation: AAG44936.1
AF290350 Genomic DNA Translation: AAG44937.1
AF290351 Genomic DNA Translation: AAG44938.1
AF290352 Genomic DNA Translation: AAG44939.1
AF290353 Genomic DNA Translation: AAG44940.1
AF290354 Genomic DNA Translation: AAG44941.1
AF290355 Genomic DNA Translation: AAG44942.1
AF290356 Genomic DNA Translation: AAG44943.1
AF416981 mRNA Translation: AAL08565.1
AF416982 mRNA Translation: AAL08566.1
AF416983 mRNA Translation: AAL08567.1
AF416984 mRNA Translation: AAL08568.1
AE014296 Genomic DNA Translation: AAF49533.1
BT010043 mRNA Translation: AAQ22512.1
RefSeqiNP_524675.1, NM_079936.3
UniGeneiDm.1872

Genome annotation databases

EnsemblMetazoaiFBtr0075492; FBpp0075247; FBgn0003076
GeneIDi44010
KEGGidme:Dmel_CG5165

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPGM_DROME
AccessioniPrimary (citable) accession number: Q9VUY9
Secondary accession number(s): Q95VC1
, Q9GN12, Q9GN65, Q9GN80, Q9GN99, Q9GNA0, Q9GNH5, Q9GNJ1, Q9GQ71, Q9GQ72, Q9GQ73, Q9GQ74, Q9GQ75, Q9GQ76, Q9GQ77, Q9GQ78, Q9GQ79, Q9GQ80
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
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