PGM_ENTHI
ID PGM_ENTHI Reviewed; 553 AA.
AC O15820;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Phosphoglucomutase;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase;
GN Name=pgm;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SFL-3;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y14444; CAA74796.1; -; mRNA.
DR AlphaFoldDB; O15820; -.
DR SMR; O15820; -.
DR STRING; 5759.rna_EHI_110120-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_013710; -.
DR VEuPathDB; AmoebaDB:EHI7A_004200; -.
DR VEuPathDB; AmoebaDB:EHI8A_001790; -.
DR VEuPathDB; AmoebaDB:EHI_110120; -.
DR VEuPathDB; AmoebaDB:KM1_014890; -.
DR eggNOG; KOG0625; Eukaryota.
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_0000147792"
FT REGION 1..25
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; 60788 MW; 2312137FC0A0865A CRC64;
MQATIKRYPT SPISGQTLGT SGLRKRASEV ENTPNYLENF VNAMFNAASN LQKPGKIIIG
GDGRYLNLKA LDIIIRVALS RGFTDIVVGK SGFMSTPAES ATIIRRKAEA GFIMTASHNP
AGKEHGDFGL KLNMSNGGPA PIEVTSKIEE SARNIKEIVI AELNKPLNID SVGDIEIECE
GKKAVVHVID PLEDYIAYLH ECFDFENLKQ FVSKYHLKVQ VDGFNAVTGI YNKKVFCELL
GLPESSLKNA IPMPDFGGKH PDPNLTYAAE LVHAVIPEDS PYDIGFAFDG DGDRNLIVGR
GAFVSPSDSL AILSTKYNDI PFFVKNGFKG VARSMPTSAA VDHVTSITET PTGWKFFGNL
MDSGKISLCG EESFGTGCCG IREKDGIWAA LCWVSILAAE SERAQRLVGV KEILESHWAK
YGRNYYQRYD FDEVDKKAAE DMMQMMRDNA KTVKCDLNGV PLKFCDDFEY HDSVDGSVTS
KQGIRFVFED GSRIIFRLSG TGSVGATIRV YFDKYSKDYK ADQTKVLADM VTVAYAVSQI
TKFTGREKPS VVT
