PGM_DROME
ID PGM_DROME Reviewed; 560 AA.
AC Q9VUY9; Q95VC1; Q9GN12; Q9GN65; Q9GN80; Q9GN99; Q9GNA0; Q9GNH5; Q9GNJ1;
AC Q9GQ71; Q9GQ72; Q9GQ73; Q9GQ74; Q9GQ75; Q9GQ76; Q9GQ77; Q9GQ78; Q9GQ79;
AC Q9GQ80;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosphoglucomutase;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase;
GN Name=Pgm1 {ECO:0000312|FlyBase:FBgn0003076};
GN ORFNames=CG5165 {ECO:0000312|FlyBase:FBgn0003076};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG44919.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-9; VAL-50; ILE-52;
RP VAL-52; TYR-64; ALA-109; LYS-197; LYS-235; LEU-240; ASP-245; SER-338;
RP MET-341; LYS-346; SER-465; LEU-484; THR-530 AND PHE-540.
RC STRAIN=B4039 {ECO:0000312|EMBL:AAG44916.1},
RC dpf95_100.3 {ECO:0000312|EMBL:AAG44900.1},
RC dpf95_13.0 {ECO:0000312|EMBL:AAG44928.1},
RC dpf95_2.0 {ECO:0000312|EMBL:AAG44903.1},
RC dpf95_2.1 {ECO:0000312|EMBL:AAG44920.1},
RC dpf95_23.1 {ECO:0000312|EMBL:AAG44925.1},
RC dpf95_29.3 {ECO:0000312|EMBL:AAG44924.1},
RC dpf95_3.0 {ECO:0000312|EMBL:AAG44927.1},
RC dpf95_36.4 {ECO:0000312|EMBL:AAG44923.1},
RC dpf95_38.3 {ECO:0000312|EMBL:AAG44913.1},
RC dpf95_4.2 {ECO:0000312|EMBL:AAG44914.1},
RC dpf95_4.3 {ECO:0000312|EMBL:AAG44926.1},
RC dpf95_44.3 {ECO:0000312|EMBL:AAG44912.1},
RC dpf95_48.2 {ECO:0000312|EMBL:AAG44902.1},
RC dpf95_53.1 {ECO:0000312|EMBL:AAG44904.1},
RC dpf95_54.0 {ECO:0000312|EMBL:AAG44921.1},
RC dpf95_56.1 {ECO:0000312|EMBL:AAG44910.1},
RC dpf95_56.2 {ECO:0000312|EMBL:AAG44930.1},
RC dpf95_73.1 {ECO:0000312|EMBL:AAG44919.1},
RC dpf95_77.4 {ECO:0000312|EMBL:AAG44918.1},
RC dpf95_84.3 {ECO:0000312|EMBL:AAG44922.1},
RC dpf95_85.1 {ECO:0000312|EMBL:AAG44911.1},
RC dpf95_90.2 {ECO:0000312|EMBL:AAG44917.1},
RC dpf95_94.1 {ECO:0000312|EMBL:AAG44915.1},
RC hfl97_1.0 {ECO:0000312|EMBL:AAG44905.1},
RC hfl97_13.0 {ECO:0000312|EMBL:AAG44906.1},
RC hfl97_15.0 {ECO:0000312|EMBL:AAG44907.1},
RC hfl97_50.0 {ECO:0000312|EMBL:AAG44908.1},
RC hfl97_93.0 {ECO:0000312|EMBL:AAG44901.1},
RC md90_709.1 {ECO:0000312|EMBL:AAG44909.1},
RC sc96_5.3 {ECO:0000312|EMBL:AAG44929.1},
RC zim_11S {ECO:0000312|EMBL:AAG44941.1},
RC zim_15S {ECO:0000312|EMBL:AAG44937.1},
RC zim_23H {ECO:0000312|EMBL:AAG44933.1},
RC zim_24S {ECO:0000312|EMBL:AAG44940.1},
RC zim_26H {ECO:0000312|EMBL:AAG44931.1},
RC zim_35S {ECO:0000312|EMBL:AAG44939.1},
RC zim_36H {ECO:0000312|EMBL:AAG44935.1},
RC zim_38H {ECO:0000312|EMBL:AAG44934.1},
RC zim_39H {ECO:0000312|EMBL:AAG44936.1},
RC zim_44H {ECO:0000312|EMBL:AAG44932.1},
RC zim_48S {ECO:0000312|EMBL:AAG44942.1},
RC zim_49S {ECO:0000312|EMBL:AAG44943.1}, and
RC zim_51S {ECO:0000312|EMBL:AAG44938.1};
RX PubMed=11102370; DOI=10.1093/genetics/156.4.1737;
RA Verrelli B.C., Eanes W.F.;
RT "Extensive amino acid polymorphism at the pgm locus is consistent with
RT adaptive protein evolution in Drosophila melanogaster.";
RL Genetics 156:1737-1752(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL08565.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-6; THR-9; LEU-240 AND ASP-245.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAL08568.1};
RX PubMed=12049662; DOI=10.1186/gb-2002-3-5-research0021;
RA Allikian M.J., Deckert-Cruz D., Rose M.R., Landis G.N., Tower J.;
RT "Doxycycline-induced expression of sense and inverted-repeat constructs
RT modulates phosphogluconate mutase (Pgm) gene expression in adult Drosophila
RT melanogaster.";
RL Genome Biol. 3:RESEARCH0021.1-RESEARCH0021.10(2002).
RN [3] {ECO:0000312|EMBL:AAF49533.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF49533.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:AAQ22512.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22512.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=44190; DOI=10.1007/bf00504306;
RA Fucci L., Gaudio L., Rao R., Spano A., Carfagna M.;
RT "Properties of the two common electrophoretic variants of
RT phosphoglucomutase in Drosophila melanogaster.";
RL Biochem. Genet. 17:825-836(1979).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8] {ECO:0000305}
RP CHARACTERIZATION OF VARIANTS THR-9; GLN-17; ASN-28; MET-36; LYS-197;
RP LYS-235; LEU-240; ASP-245; SER-338; MET-341; LYS-346; LYS-351; SER-465;
RP LEU-484 AND THR-530.
RX PubMed=11290720; DOI=10.1093/genetics/157.4.1649;
RA Verrelli B.C., Eanes W.F.;
RT "Clinal variation for amino acid polymorphisms at the Pgm locus in
RT Drosophila melanogaster.";
RL Genetics 157:1649-1663(2001).
RN [9] {ECO:0000305}
RP CHARACTERIZATION OF VARIANTS THR-9; MET-36; VAL-52; LEU-240; ASP-245;
RP MET-341; SER-465; LEU-484 AND THR-530.
RX PubMed=11560897; DOI=10.1093/genetics/159.1.201;
RA Verrelli B.C., Eanes W.F.;
RT "The functional impact of Pgm amino acid polymorphism on glycogen content
RT in Drosophila melanogaster.";
RL Genetics 159:201-210(2001).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose. {ECO:0000269|PubMed:44190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000269|PubMed:44190};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:44190};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:44190};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for glucose-1-phosphate (for Pgm-A at pH 6.0)
CC {ECO:0000269|PubMed:44190};
CC KM=158 uM for glucose-1-phosphate (for Pgm-A at pH 7.4)
CC {ECO:0000269|PubMed:44190};
CC KM=4.4 uM for glucose-1,6-diphosphate (for Pgm-A at pH 6.0)
CC {ECO:0000269|PubMed:44190};
CC KM=4.4 uM for glucose-1,6-diphosphate (for Pgm-A at pH 7.4)
CC {ECO:0000269|PubMed:44190};
CC KM=142.2 uM for glucose-1-phosphate (for Pgm-B at pH 6.0)
CC {ECO:0000269|PubMed:44190};
CC KM=112.4 uM for glucose-1-phosphate (for Pgm-B at pH 7.4)
CC {ECO:0000269|PubMed:44190};
CC KM=21.7 uM for glucose-1,6-diphosphate (for Pgm-B at pH 6.0)
CC {ECO:0000269|PubMed:44190};
CC KM=4.2 uM for glucose-1,6-diphosphate (for Pgm-B at pH 7.4)
CC {ECO:0000269|PubMed:44190};
CC Vmax=32.8 umol/min/mg enzyme toward glucose-1-phosphate (for Pgm-A at
CC pH 6.0) {ECO:0000269|PubMed:44190};
CC Vmax=129 umol/min/mg enzyme toward glucose-1-phosphate (for Pgm-A at
CC pH 7.4) {ECO:0000269|PubMed:44190};
CC Vmax=20.8 umol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-
CC A at pH 6.0) {ECO:0000269|PubMed:44190};
CC Vmax=111 umol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-A
CC at pH 7.4) {ECO:0000269|PubMed:44190};
CC Vmax=35 umol/min/mg enzyme toward glucose-1-phosphate (for Pgm-B at
CC pH 6.0) {ECO:0000269|PubMed:44190};
CC Vmax=120.9 umol/min/mg enzyme toward glucose-1-phosphate (for Pgm-B
CC at pH 7.4) {ECO:0000269|PubMed:44190};
CC Vmax=14.5 umol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-
CC B at pH 6.0) {ECO:0000269|PubMed:44190};
CC Vmax=100 umol/min/mg enzyme toward glucose-1,6-diphosphate (for Pgm-B
CC at pH 7.4) {ECO:0000269|PubMed:44190};
CC pH dependence:
CC Optimum pH is 7.4-7.6. {ECO:0000269|PubMed:44190};
CC Temperature dependence:
CC Pgm-A is more thermostable than Pgm-B. {ECO:0000269|PubMed:44190};
CC -!- TISSUE SPECIFICITY: Localized primarily to fat bodies in third instar
CC larvae. {ECO:0000269|PubMed:44190}.
CC -!- POLYMORPHISM: The polymorphisms show clinal variations. There are 2
CC common electrophoretic variants, Pgm-A and Pgm-B, which differ in their
CC kinetic and stability parameters. Variations in Pgm are associated with
CC differences in enzyme activity and glycogen content.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000269|PubMed:44190}.
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DR EMBL; AF290313; AAG44900.1; -; Genomic_DNA.
DR EMBL; AF290314; AAG44901.1; -; Genomic_DNA.
DR EMBL; AF290315; AAG44902.1; -; Genomic_DNA.
DR EMBL; AF290316; AAG44903.1; -; Genomic_DNA.
DR EMBL; AF290317; AAG44904.1; -; Genomic_DNA.
DR EMBL; AF290318; AAG44905.1; -; Genomic_DNA.
DR EMBL; AF290319; AAG44906.1; -; Genomic_DNA.
DR EMBL; AF290320; AAG44907.1; -; Genomic_DNA.
DR EMBL; AF290321; AAG44908.1; -; Genomic_DNA.
DR EMBL; AF290322; AAG44909.1; -; Genomic_DNA.
DR EMBL; AF290323; AAG44910.1; -; Genomic_DNA.
DR EMBL; AF290324; AAG44911.1; -; Genomic_DNA.
DR EMBL; AF290325; AAG44912.1; -; Genomic_DNA.
DR EMBL; AF290326; AAG44913.1; -; Genomic_DNA.
DR EMBL; AF290327; AAG44914.1; -; Genomic_DNA.
DR EMBL; AF290328; AAG44915.1; -; Genomic_DNA.
DR EMBL; AF290329; AAG44916.1; -; Genomic_DNA.
DR EMBL; AF290330; AAG44917.1; -; Genomic_DNA.
DR EMBL; AF290331; AAG44918.1; -; Genomic_DNA.
DR EMBL; AF290332; AAG44919.1; -; Genomic_DNA.
DR EMBL; AF290333; AAG44920.1; -; Genomic_DNA.
DR EMBL; AF290334; AAG44921.1; -; Genomic_DNA.
DR EMBL; AF290335; AAG44922.1; -; Genomic_DNA.
DR EMBL; AF290336; AAG44923.1; -; Genomic_DNA.
DR EMBL; AF290337; AAG44924.1; -; Genomic_DNA.
DR EMBL; AF290338; AAG44925.1; -; Genomic_DNA.
DR EMBL; AF290339; AAG44926.1; -; Genomic_DNA.
DR EMBL; AF290340; AAG44927.1; -; Genomic_DNA.
DR EMBL; AF290341; AAG44928.1; -; Genomic_DNA.
DR EMBL; AF290342; AAG44929.1; -; Genomic_DNA.
DR EMBL; AF290343; AAG44930.1; -; Genomic_DNA.
DR EMBL; AF290344; AAG44931.1; -; Genomic_DNA.
DR EMBL; AF290345; AAG44932.1; -; Genomic_DNA.
DR EMBL; AF290346; AAG44933.1; -; Genomic_DNA.
DR EMBL; AF290347; AAG44934.1; -; Genomic_DNA.
DR EMBL; AF290348; AAG44935.1; -; Genomic_DNA.
DR EMBL; AF290349; AAG44936.1; -; Genomic_DNA.
DR EMBL; AF290350; AAG44937.1; -; Genomic_DNA.
DR EMBL; AF290351; AAG44938.1; -; Genomic_DNA.
DR EMBL; AF290352; AAG44939.1; -; Genomic_DNA.
DR EMBL; AF290353; AAG44940.1; -; Genomic_DNA.
DR EMBL; AF290354; AAG44941.1; -; Genomic_DNA.
DR EMBL; AF290355; AAG44942.1; -; Genomic_DNA.
DR EMBL; AF290356; AAG44943.1; -; Genomic_DNA.
DR EMBL; AF416981; AAL08565.1; -; mRNA.
DR EMBL; AF416982; AAL08566.1; -; mRNA.
DR EMBL; AF416983; AAL08567.1; -; mRNA.
DR EMBL; AF416984; AAL08568.1; -; mRNA.
DR EMBL; AE014296; AAF49533.1; -; Genomic_DNA.
DR EMBL; BT010043; AAQ22512.1; -; mRNA.
DR RefSeq; NP_524675.1; NM_079936.3.
DR AlphaFoldDB; Q9VUY9; -.
DR SMR; Q9VUY9; -.
DR BioGRID; 68773; 6.
DR IntAct; Q9VUY9; 7.
DR STRING; 7227.FBpp0075247; -.
DR iPTMnet; Q9VUY9; -.
DR PaxDb; Q9VUY9; -.
DR PRIDE; Q9VUY9; -.
DR DNASU; 44010; -.
DR EnsemblMetazoa; FBtr0075492; FBpp0075247; FBgn0003076.
DR GeneID; 44010; -.
DR KEGG; dme:Dmel_CG5165; -.
DR CTD; 5236; -.
DR FlyBase; FBgn0003076; Pgm1.
DR VEuPathDB; VectorBase:FBgn0003076; -.
DR eggNOG; KOG0625; Eukaryota.
DR GeneTree; ENSGT00940000173602; -.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; Q9VUY9; -.
DR OMA; DIYKIYA; -.
DR OrthoDB; 555015at2759; -.
DR PhylomeDB; Q9VUY9; -.
DR Reactome; R-DME-3322077; Glycogen synthesis.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SABIO-RK; Q9VUY9; -.
DR SignaLink; Q9VUY9; -.
DR BioGRID-ORCS; 44010; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Pgm; fly.
DR GenomeRNAi; 44010; -.
DR PRO; PR:Q9VUY9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003076; Expressed in capitellum (Drosophila) and 25 other tissues.
DR Genevisible; Q9VUY9; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:FlyBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:FlyBase.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573; PTHR22573; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..560
FT /note="Phosphoglucomutase"
FT /id="PRO_0000147789"
FT ACT_SITE 116
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 24
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 116
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 292
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 293
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 357
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 376
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 378
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 389
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 6
FT /note="E -> G"
FT /evidence="ECO:0000269|PubMed:12049662"
FT VARIANT 9
FT /note="A -> T (in strain: dpf95_94.1 and zim_26H)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720, ECO:0000269|PubMed:11560897,
FT ECO:0000269|PubMed:12049662"
FT VARIANT 17
FT /note="K -> Q"
FT /evidence="ECO:0000269|PubMed:11290720"
FT VARIANT 28
FT /note="K -> N"
FT /evidence="ECO:0000269|PubMed:11290720"
FT VARIANT 36
FT /note="T -> M"
FT /evidence="ECO:0000269|PubMed:11290720,
FT ECO:0000269|PubMed:11560897"
FT VARIANT 50
FT /note="A -> V (in strain: zim_38H)"
FT /evidence="ECO:0000269|PubMed:11102370"
FT VARIANT 52
FT /note="A -> I (in strain: zim_36H)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11560897"
FT VARIANT 52
FT /note="A -> V (in strain: dpf95_48.2, dpf95_100.3 and
FT hfl97_93.0)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11560897"
FT VARIANT 64
FT /note="F -> Y (in strain: zim_36H)"
FT /evidence="ECO:0000269|PubMed:11102370"
FT VARIANT 109
FT /note="G -> A (in strain: B4039)"
FT /evidence="ECO:0000269|PubMed:11102370"
FT VARIANT 197
FT /note="E -> K (in strain: dpf95_56.1)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720"
FT VARIANT 235
FT /note="E -> K (in strain: dpf95_13.0)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720"
FT VARIANT 240
FT /note="R -> L (in strain: dpf95_38.3 and dpf95_4.2)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720, ECO:0000269|PubMed:11560897,
FT ECO:0000269|PubMed:12049662"
FT VARIANT 245
FT /note="E -> D (in strain: dpf95_38.3 and dpf95_4.2)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720, ECO:0000269|PubMed:11560897,
FT ECO:0000269|PubMed:12049662"
FT VARIANT 338
FT /note="A -> S (in strain: dpf95_36.4)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720"
FT VARIANT 341
FT /note="V -> M (in strain: B4039, dpf95_77.4 and
FT dpf95_90.2)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720, ECO:0000269|PubMed:11560897"
FT VARIANT 346
FT /note="R -> K (in strain: dpf95_90.2, hfl97_1.0,
FT hfl97_13.0, hfl97_15.0, hfl97_50.0, md90_709.1, zim_36H and
FT zim_39H)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720"
FT VARIANT 351
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:11290720"
FT VARIANT 465
FT /note="T -> S (in strain: dpf95_29.3)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720, ECO:0000269|PubMed:11560897"
FT VARIANT 484
FT /note="V -> L (in strain: dpf95_38.3, dpf95_4.2,
FT dpf95_44.3, dpf95_48.2, dpf95_53.1, dpf95_56.1, dpf95_85.1,
FT hfl97_1.0, hfl97_13.0, hfl97_15.0, hfl97_50.0, hfl97_93.0,
FT md90_709.1, zim_11S, zim_23H, zim_35S, zim_36H, zim_38H,
FT zim_39H, zim_44H, zim_48S and zim_49S)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720, ECO:0000269|PubMed:11560897"
FT VARIANT 530
FT /note="A -> T (in strain: dpf95_44.3, dpf95_53.1 and
FT dpf95_85.1)"
FT /evidence="ECO:0000269|PubMed:11102370,
FT ECO:0000269|PubMed:11290720, ECO:0000269|PubMed:11560897"
FT VARIANT 540
FT /note="I -> F (in strain: zim_48S)"
FT /evidence="ECO:0000269|PubMed:11102370"
SQ SEQUENCE 560 AA; 60766 MW; 10320D78D41C1BEC CRC64;
MSLTVEIVAT KPYEGQKPGT SGLRKKVKVF TQPNYTENFV QAILEANGAA LAGSTLVVGG
DGRFYCKEAA ELIVRLSAAN GVSKLLVGQN GILSTPAVSS LIRHNKALGG IVLTASHNPG
GPENDFGIKF NCENGGPAPD AFTNHIYKIT TEIKEYKLVR NLQIDISKVG VTSFDIAGKP
FTVEVIDSVA NYVRHMEEIF DFAKLKDFVS GKATGKPLKM RIDAMNGVTG SYVREIFLNR
LGATESSVVH TTPLPDFGGL HPDPNLTYAK DLVDTVAQGD YDIGAAFDGD GDRNMIIGSK
AFFVTPSDSL AVIAHYLEAI PYFQKNGVQG FARSMPTASA VDLVGRKLGK EVFEVPTGWK
YFGNLMDAGR LCLCGEESFG TGSNHIREKD GIWAVLAWIS VMQHTGKGIE DILKQHWSVY
GRNYFTRYDY EECASDPCNE MVATMEKTIT APEFVGKSYS SGGKTYKVKE ADNFSYTDPV
DKSVATKQGL RIVFEDGSRI VVRLSGTGSS GATVRLYIDS YEKENVLGQA SVMLKPLIDI
ALEISQLPKF TGRNAPTVIT
