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Database: UniProt
Entry: A0A251QJA9_PRUPE
LinkDB: A0A251QJA9_PRUPE
Original site: A0A251QJA9_PRUPE 
ID   A0A251QJA9_PRUPE        Unreviewed;       544 AA.
AC   A0A251QJA9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=PRUPE_2G213100 {ECO:0000313|EMBL:ONI23868.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI23868.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI23868.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
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:0000256|ARBA:ARBA00000443};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; CM007652; ONI23868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251QJA9; -.
DR   EnsemblPlants; ONI23868; ONI23868; PRUPE_2G213100.
DR   Gramene; ONI23868; ONI23868; PRUPE_2G213100.
DR   Proteomes; UP000006882; Chromosome g2.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03089; PMM_PGM; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882}.
FT   DOMAIN          23..166
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          202..302
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          307..408
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   544 AA;  58129 MW;  90337DBE95584DDC CRC64;
     MEAAPSTAAV PNLDKVDFLK LQNGSDIRGV AVAGVEGEPL NLTEPVSEAI AAGFAAWLLE
     KKKADGSRRL SISVGHDSRI SAKKLEDAIS RGIAGAGLDV VQYGLASTPA MFNSTVTEDD
     AFLCPVDGSI MITASHLPYN RNGFKFFTNA GGLGKADIKN ILERAADIYN KFTAEGLTSS
     KGKAVASVKR VDYMNVYTSD LVKAVRKAAG NIEKPLEGFH IVVDAGNGAG GFFAAKVLEP
     LGAVTSGSQF LEPDGMFPNH IPNPEDKTAM KAITQAVLDN KADLGIIFDT DVDRSAAVDS
     TGLEFNRNRL IALMSAIVLE EHPGTTIVTD SVTSDGLTTF IEKKLGGKHH RFKRGYKNVI
     DEAIRLNSVG EESHLAIETS GHGALKENHW LDDGAYLMVK ILNKIASARA SGQTGGSKVL
     TGLLEGLQEP AFSVELRLKI NQSHQDLKGG SFRDYGEAVL KHLENYIDSD PKLQKAPVNY
     EGVRVSGYGG WFLLRLSLHD PVLPLNIEAP SNNDAVLLGN VVRAALKEFS ALDTSALDKF
     VQAS
//
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