ID   PGMC_POPTN              Reviewed;         582 AA.
AC   Q9ZSQ4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Phosphoglucomutase, cytoplasmic;
DE            Short=PGM;
DE            EC=5.4.2.2;
DE   AltName: Full=Glucose phosphomutase;
GN   Name=PGM1; Synonyms=PGM;
OS   Populus tremula (European aspen).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=113636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cambium;
RA   Sterky F., Sievertzon M., Kleczkowski L.A.;
RT   "Molecular cloning of a cDNA encoding a cytosolic form of
RT   phosphoglucomutase from cambium of poplar (Populus tremula x
RT   tremuloides).";
RL   (er) Plant Gene Register PGR98-205(1998).
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; AF097938; AAD13031.1; -; mRNA.
DR   PRIDE; Q9ZSQ4; -.
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:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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; 2.
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   Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW   Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..582
FT                   /note="Phosphoglucomutase, cytoplasmic"
FT                   /id="PRO_0000147805"
FT   ACT_SITE        124
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         124..125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         303..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         386..388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         535
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
SQ   SEQUENCE   582 AA;  63124 MW;  458FFC7C6C09BD56 CRC64;
     MVLFNVSRVE TTPFGDQKPG TSGLRKKVKV FKQPNYLQNF VQSTFNALTP QNVRGATLVV
     SGDGRYFSKD AIQIITKMAA GNGLRRVWVG QNGLLSTPAV SAVIRERVGV DGSKATGAFI
     LTASHNPGGP NEDFGIKYNM ENGGPAPEGI TDKIYENTKT IKEYLTADLP DVDITTIGVT
     SFSGSEGQFD VEVFDSASDY IKLMKSIFDF ESIRKLLSSP KFTFCYDALH GVAGAYAKRI
     FVEELGAQES SLLNCVPKED FGGGHPDPNL TYAKELVARM GLGKSNSEVE PPEFGAAADG
     DADRNMVLGK RFFVTPSDSV AIIAANAVEA IPYFSAGLKG VARSMPTSAA LDVVAKSLNL
     KFFEVPTGWK FFGNLMDAGL CSVCGEESFG TGSDHIREKD GIWAVLAWLS ILAYKNRENL
     GGGKLVTVED IVHNHWATYG RHYYTRYDYE NVDAGAAKEL MACLVKLQSS LTEVNEIVSG
     IQSDVSKVVH ADEFEYKDPV DGSISKHQGI RYLFEDGSRL VFRLSGTGSE GATIRLYIEQ
     YEKDPSKTGR DSQDALAPLV AVALGLXKMQ EFTGRSAPTV IT