ID   PGM_ENTDI               Reviewed;         553 AA.
AC   O18719;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Phosphoglucomutase;
DE            Short=PGM;
DE            EC=5.4.2.2;
DE   AltName: Full=Glucose phosphomutase;
GN   Name=pgm;
OS   Entamoeba dispar.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=46681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9497037; DOI=10.1016/s0166-6851(97)00147-3;
RA   Ortner S., Binder M., Scheiner O., Wiedermann G., Duchene M.;
RT   "Molecular and biochemical characterization of phosphoglucomutases from
RT   Entamoeba histolytica and Entomoeba dispar.";
RL   Mol. Biochem. Parasitol. 90:121-129(1997).
CC   -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC       of glucose. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; Y14445; CAA74797.1; -; mRNA.
DR   AlphaFoldDB; O18719; -.
DR   SMR; O18719; -.
DR   VEuPathDB; AmoebaDB:EDI_174890; -.
DR   OMA; DIYKIYA; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..553
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000147791"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        117
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         117..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         293..294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         371..373
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         509
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
SQ   SEQUENCE   553 AA;  60907 MW;  901BD8D2365E97DD CRC64;
     MQATVKRYPT TPISGQTMGT SGLRKRASEV ENTPNYLENF VNAMFNAASN LQKPGKIIIG
     GDGRYLNLKA LDIIIRVALS RGFTDIVVGK SGFMSTPAES ATIIRRKAEA GFIMTASHNP
     AGKDHGDFGL KLNMSNGGPA PLEVTSKIEE SARNIKEIVI AELNKPLTID TIGDIEIECE
     GKKAIVHVID PLEDYIAYLH ECFDFEKLKQ FVSKYHLKVQ VDGFNAVTGI YNKKVFCELL
     GLPESSLKNA IPMPDFGGKH PDPNLTYAAE LVHAVIPEDS PYDIGFAFDG DGDRNLIVGR
     GAFVSPSDSL AILSTKYNDI PFFVKNGFKG VARSMPTSAA VDHVTSITET PTGWKFFGNL
     MDSGKISLCG EESFGTGCCG IREKDGIWAA LCWVSILAAE SERAQRLVGV KEILENHWAK
     YGRNYYQRYD FDEVDKKAAE DMMQMMRDNA KTVKCDLNGV PLKFCDDFEY HDSVDGSVTS
     KQGIRFVFED GSRIIFRLSG TGSVGATIRV YFDKYSKDYK ADQNKMLADM VTVAYAVSQI
     TKFTGREKPS VVT