Reviewed, UniProtKB/Swiss-Prot Q9VUY9 (PGM_DROME)

Names and origin

Protein names

Recommended name:
    Phosphoglucomutase
      Short name=PGM
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase

Gene names

Name:	Pgm
ORF Names:	CG5165

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	560 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This enzyme participates in both the breakdown and synthesis of glucose. Ref.6
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. Ref.6
Cofactor	Binds 1 magnesium ion per subunit. Ref.6
Tissue specificity	Localized primarily to fat bodies in third instar larvae. Ref.6
Polymorphism	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. Ref.6 Ref.8 Ref.9
Sequence similarities	Belongs to the phosphohexose mutase family. Ref.6
Biophysicochemical properties	Kinetic parameters: KM=140 µM for glucose-1-phosphate (for Pgm-A at pH 6.0) Ref.6 KM=158 µM for glucose-1-phosphate (for Pgm-A at pH 7.4) Ref.6 KM=4.4 µM for glucose-1,6-diphosphate (for Pgm-A at pH 6.0) KM=4.4 µM for glucose-1,6-diphosphate (for Pgm-A at pH 7.4) KM=142.2 µM for glucose-1-phosphate (for Pgm-B at pH 6.0) Ref.6 KM=112.4 µM for glucose-1-phosphate (for Pgm-B at pH 7.4) Ref.6 KM=21.7 µM for glucose-1,6-diphosphate (for Pgm-B at pH 6.0) KM=4.2 µM for glucose-1,6-diphosphate (for Pgm-B at pH 7.4) Vmax=32.8 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-A at pH 6.0) Ref.6 Vmax=129 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-A at pH 7.4) Ref.6 Vmax=20.8 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-A at pH 6.0) Vmax=111 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-A at pH 7.4) Ref.6 Vmax=35 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-B at pH 6.0) Ref.6 Vmax=120.9 µmol/min/mg enzyme toward glucose-1-phosphate (for Pgm-B at pH 7.4) Ref.6 Vmax=14.5 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-B at pH 6.0) Ref.6 Vmax=100 µmol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-B at pH 7.4) pH dependence: Optimum pH is 7.4-7.6. Ref.6 Temperature dependence: Pgm-A is more thermostable than Pgm-B. Ref.6

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glycogen biosynthetic process Ref.9 Inferred from mutant phenotype. Source: FlyBase
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Ref.9 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 560	560	Phosphoglucomutase		PRO_0000147789
Sites
	Active site	116	1	Phosphoserine intermediate By similarity UniProtKB P00949
	Metal binding	116	1	Magnesium; via phosphate group By similarity UniProtKB P00949
	Metal binding	288	1	Magnesium By similarity UniProtKB P00949
	Metal binding	290	1	Magnesium By similarity UniProtKB P00949
	Metal binding	292	1	Magnesium By similarity UniProtKB P00949
Amino acid modifications
	Modified residue	116	1	Phosphoserine Ref.7
Natural variations
	Natural variant	6	1	E → G Ref.2
	Natural variant	9	1	A → T in strain: dpf95_94.1 and zim_26H. Ref.1 Ref.2 Ref.8 Ref.9
	Natural variant	17	1	K → Q Ref.8
	Natural variant	28	1	K → N Ref.8
	Natural variant	36	1	T → M Ref.8 Ref.9
	Natural variant	50	1	A → V in strain: zim_38H. Ref.1
	Natural variant	52	1	A → I in strain: zim_36H. Ref.1 Ref.9
	Natural variant	52	1	A → V in strain: dpf95_48.2, dpf95_100.3 and hfl97_93.0. Ref.1 Ref.9
	Natural variant	64	1	F → Y in strain: zim_36H. Ref.1
	Natural variant	109	1	G → A in strain: B4039. Ref.1
	Natural variant	197	1	E → K in strain: dpf95_56.1. Ref.1 Ref.8
	Natural variant	235	1	E → K in strain: dpf95_13.0. Ref.1 Ref.8
	Natural variant	240	1	R → L in strain: dpf95_38.3 and dpf95_4.2. Ref.1 Ref.2 Ref.8 Ref.9
	Natural variant	245	1	E → D in strain: dpf95_38.3 and dpf95_4.2. Ref.1 Ref.2 Ref.8 Ref.9
	Natural variant	338	1	A → S in strain: dpf95_36.4. Ref.1 Ref.8
	Natural variant	341	1	V → M in strain: B4039, dpf95_77.4 and dpf95_90.2. Ref.1 Ref.8 Ref.9
	Natural variant	346	1	R → 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. Ref.1 Ref.8
	Natural variant	351	1	E → K Ref.8
	Natural variant	465	1	T → S in strain: dpf95_29.3. Ref.1 Ref.8 Ref.9
	Natural variant	484	1	V → 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. Ref.1 Ref.8 Ref.9
	Natural variant	530	1	A → T in strain: dpf95_44.3, dpf95_53.1 and dpf95_85.1. Ref.1 Ref.8 Ref.9
	Natural variant	540	1	I → F in strain: zim_48S. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VUY9-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 10320D78D41C1BEC	FASTA	560	60,766
	10 20 30 40 50 60 MSLTVEIVAT KPYEGQKPGT SGLRKKVKVF TQPNYTENFV QAILEANGAA LAGSTLVVGG 70 80 90 100 110 120 DGRFYCKEAA ELIVRLSAAN GVSKLLVGQN GILSTPAVSS LIRHNKALGG IVLTASHNPG 130 140 150 160 170 180 GPENDFGIKF NCENGGPAPD AFTNHIYKIT TEIKEYKLVR NLQIDISKVG VTSFDIAGKP 190 200 210 220 230 240 FTVEVIDSVA NYVRHMEEIF DFAKLKDFVS GKATGKPLKM RIDAMNGVTG SYVREIFLNR 250 260 270 280 290 300 LGATESSVVH TTPLPDFGGL HPDPNLTYAK DLVDTVAQGD YDIGAAFDGD GDRNMIIGSK 310 320 330 340 350 360 AFFVTPSDSL AVIAHYLEAI PYFQKNGVQG FARSMPTASA VDLVGRKLGK EVFEVPTGWK 370 380 390 400 410 420 YFGNLMDAGR LCLCGEESFG TGSNHIREKD GIWAVLAWIS VMQHTGKGIE DILKQHWSVY 430 440 450 460 470 480 GRNYFTRYDY EECASDPCNE MVATMEKTIT APEFVGKSYS SGGKTYKVKE ADNFSYTDPV 490 500 510 520 530 540 DKSVATKQGL RIVFEDGSRI VVRLSGTGSS GATVRLYIDS YEKENVLGQA SVMLKPLIDI 550 560 ALEISQLPKF TGRNAPTVIT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Extensive amino acid polymorphism at the pgm locus is consistent with adaptive protein evolution in Drosophila melanogaster." Verrelli B.C., Eanes W.F. Genetics 156:1737-1752(2000) [PubMed: 11102370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-9; VAL-50; ILE-52; VAL-52; TYR-64; ALA-109; LYS-197; LYS-235; LEU-240; ASP-245; SER-338; MET-341; LYS-346; SER-465; LEU-484; THR-530 AND PHE-540. Strain: B4039, dpf95_100.3, dpf95_13.0, dpf95_2.0, dpf95_2.1, dpf95_23.1, dpf95_29.3, dpf95_3.0, dpf95_36.4, dpf95_38.3, dpf95_4.2, dpf95_4.3, dpf95_44.3, dpf95_48.2, dpf95_53.1, dpf95_54.0, dpf95_56.1, dpf95_56.2, dpf95_73.1, dpf95_77.4, dpf95_84.3, dpf95_85.1, dpf95_90.2, dpf95_94.1, hfl97_1.0, hfl97_13.0, hfl97_15.0, hfl97_50.0, hfl97_93.0, md90_709.1, sc96_5.3, zim_11S, zim_15S, zim_23H, zim_24S, zim_26H, zim_35S, zim_36H, zim_38H, zim_39H, zim_44H, zim_48S, zim_49S and zim_51S.
[2]	"Doxycycline-induced expression of sense and inverted-repeat constructs modulates phosphogluconate mutase (Pgm) gene expression in adult Drosophila melanogaster." Allikian M.J., Deckert-Cruz D., Rose M.R., Landis G.N., Tower J. Genome Biol. 3:RESEARCH0021.1-RESEARCH0021.10(2002) [PubMed: 12049662] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-6; THR-9; LEU-240 AND ASP-245. Strain: Canton-S.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"Properties of the two common electrophoretic variants of phosphoglucomutase in Drosophila melanogaster." Fucci L., Gaudio L., Rao R., Spano A., Carfagna M. Biochem. Genet. 17:825-836(1979) [PubMed: 44190] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[7]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, MASS SPECTROMETRY. Tissue: Embryo.
[8]	"Clinal variation for amino acid polymorphisms at the Pgm locus in Drosophila melanogaster." Verrelli B.C., Eanes W.F. Genetics 157:1649-1663(2001) [PubMed: 11290720] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS THR-9; GLN-17; ASN-28; MET-36; LYS-197; LYS-235; LEU-240; ASP-245; SER-338; MET-341; LYS-346; LYS-351; SER-465; LEU-484 AND THR-530.
[9]	"The functional impact of Pgm amino acid polymorphism on glycogen content in Drosophila melanogaster." Verrelli B.C., Eanes W.F. Genetics 159:201-210(2001) [PubMed: 11560897] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS THR-9; MET-36; VAL-52; LEU-240; ASP-245; MET-341; SER-465; LEU-484 AND THR-530.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
RefSeq	NP_524675.1.
UniGene	Dm.1872
3D structure databases
HSSP	HSSP built from PDB template 3PMG based on UniProtKB P00949.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VUY9. 4 interactions.
STRING	Q9VUY9.
Proteomic databases
PRIDE	Q9VUY9.
Genome annotation databases
Ensembl	FBtr0075492; FBpp0075247; FBgn0003076; Drosophila melanogaster. [Genome view]
GeneID	44010.
KEGG	dme:Dmel_CG5165.
NMPDR	fig|7227.3.peg.10062.
Organism-specific databases
CTD	44010.
FlyBase	FBgn0003076. Pgm.
Phylogenomic databases
OMA	YMKEAIQ.
Enzyme and pathway databases
BRENDA	5.4.2.2. 48.
Gene expression databases
Bgee	Q9VUY9.
GermOnline	CG5165. Drosophila melanogaster.
Family and domain databases
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. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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. [Graphical view]
PRINTS	PR00509. PGMPMM.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	836588.

Entry information

Entry name

PGM_DROME

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project