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Protein

Phosphoglucomutase

Gene

Pgm

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201SubstrateBy similarity
Binding sitei24 – 241SubstrateBy similarity
Active sitei116 – 1161Phosphoserine intermediateBy similarity
Metal bindingi116 – 1161Magnesium; via phosphate groupBy similarity
Binding sitei129 – 1291SubstrateBy similarity
Metal bindingi288 – 2881MagnesiumBy similarity
Metal bindingi290 – 2901MagnesiumBy similarity
Metal bindingi292 – 2921MagnesiumBy similarity
Binding sitei357 – 3571SubstrateBy similarity
Binding sitei389 – 3891SubstrateBy similarity
Binding sitei515 – 5151SubstrateBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphoglucomutase activity Source: UniProtKB
  • phosphoglycerate mutase activity Source: FlyBase

GO - Biological processi

  • flight Source: FlyBase
  • galactose catabolic process Source: GO_Central
  • glucose metabolic process Source: GO_Central
  • glycogen biosynthetic process Source: FlyBase
  • lateral inhibition Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003076. Pgm.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560PhosphoglucomutasePRO_0000147789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161Phosphoserine1 Publication

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 interactions.
IntActiQ9VUY9. 7 interactions.
MINTiMINT-1564518.
STRINGi7227.FBpp0075247.

Structurei

3D structure databases

ProteinModelPortaliQ9VUY9.
SMRiQ9VUY9. Positions 8-560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 1172Substrate bindingBy similarity
Regioni292 – 2932Substrate bindingBy similarity
Regioni376 – 3783Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.1 Publication

Phylogenomic databases

eggNOGiKOG0625. Eukaryota.
COG0033. LUCA.
GeneTreeiENSGT00390000011831.
InParanoidiQ9VUY9.
KOiK01835.
OMAiYYARHDY.
OrthoDBiEOG091G0HZ0.
PhylomeDBiQ9VUY9.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61E → G.1 Publication
Natural varianti9 – 91A → T in strain: dpf95_94.1 and zim_26H. 4 Publications
Natural varianti17 – 171K → Q.1 Publication
Natural varianti28 – 281K → N.1 Publication
Natural varianti36 – 361T → M.2 Publications
Natural varianti50 – 501A → V in strain: zim_38H. 1 Publication
Natural varianti52 – 521A → I in strain: zim_36H. 2 Publications
Natural varianti52 – 521A → V in strain: dpf95_48.2, dpf95_100.3 and hfl97_93.0. 2 Publications
Natural varianti64 – 641F → Y in strain: zim_36H. 1 Publication
Natural varianti109 – 1091G → A in strain: B4039. 1 Publication
Natural varianti197 – 1971E → K in strain: dpf95_56.1. 2 Publications
Natural varianti235 – 2351E → K in strain: dpf95_13.0. 2 Publications
Natural varianti240 – 2401R → L in strain: dpf95_38.3 and dpf95_4.2. 4 Publications
Natural varianti245 – 2451E → D in strain: dpf95_38.3 and dpf95_4.2. 4 Publications
Natural varianti338 – 3381A → S in strain: dpf95_36.4. 2 Publications
Natural varianti341 – 3411V → M in strain: B4039, dpf95_77.4 and dpf95_90.2. 3 Publications
Natural varianti346 – 3461R → 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 Publications
Natural varianti351 – 3511E → K.1 Publication
Natural varianti465 – 4651T → S in strain: dpf95_29.3. 3 Publications
Natural varianti484 – 4841V → 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 Publications
Natural varianti530 – 5301A → T in strain: dpf95_44.3, dpf95_53.1 and dpf95_85.1. 3 Publications
Natural varianti540 – 5401I → F in strain: zim_48S. 1 Publication

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9VUY9.
SMRiQ9VUY9. Positions 8-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68773. 5 interactions.
IntActiQ9VUY9. 7 interactions.
MINTiMINT-1564518.
STRINGi7227.FBpp0075247.

PTM databases

iPTMnetiQ9VUY9.

Proteomic databases

PaxDbiQ9VUY9.
PRIDEiQ9VUY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075492; FBpp0075247; FBgn0003076.
GeneIDi44010.
KEGGidme:Dmel_CG5165.

Organism-specific databases

CTDi44010.
FlyBaseiFBgn0003076. Pgm.

Phylogenomic databases

eggNOGiKOG0625. Eukaryota.
COG0033. LUCA.
GeneTreeiENSGT00390000011831.
InParanoidiQ9VUY9.
KOiK01835.
OMAiYYARHDY.
OrthoDBiEOG091G0HZ0.
PhylomeDBiQ9VUY9.

Miscellaneous databases

ChiTaRSiPgm. fly.
GenomeRNAii44010.
PROiQ9VUY9.

Gene expression databases

BgeeiFBgn0003076.
GenevisibleiQ9VUY9. DM.

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...

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 historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 118 of the entry and version 1 of the sequence. [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

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.