ID   PGMC_BROIN              Reviewed;         581 AA.
AC   Q9SNX2;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Phosphoglucomutase, cytoplasmic;
DE            Short=PGM;
DE            EC=5.4.2.2;
DE   AltName: Full=Glucose phosphomutase;
GN   Name=PGM1;
OS   Bromus inermis (Smooth brome grass) (Bromopsis inermis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Bromeae; Bromus.
OX   NCBI_TaxID=15371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sritubtim S., Lee S.P.;
RT   "Expression of a phosphoglucomutase in bromegrass suspension culture cells
RT   during abscisic acid induced freezing tolerance.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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; AF197925; AAF04862.1; -; mRNA.
DR   AlphaFoldDB; Q9SNX2; -.
DR   SMR; Q9SNX2; -.
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..581
FT                   /note="Phosphoglucomutase, cytoplasmic"
FT                   /id="PRO_0000147800"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        123
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         123..124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         302..303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         385..387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         534
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
SQ   SEQUENCE   581 AA;  62673 MW;  2EDE54521A0F027D CRC64;
     MVFSVAKKDT TPYEGQKPGT SGLRKKVTVF QQPHYLANFV QSTFNALPAE EVKGATIVVS
     GDGRYFSKDA VQIIAKMAAA NGVRRVWVGQ GSLLSTPAVS AIIRERIAAD GSKATGGFIL
     TASHNPGGPT EDFGIKYNMG NGGPAPESVT DKIFSNTKTI SEYLIAEDLP DVDISVIGVT
     TFTGPEGPFD VDVFDSATEY VKLMKTIFDF ESIKKLLASP KFSFCFDGMH GVAGAYAKRI
     FVDELGASES SLLNCVPKED FGGGHPDPNL TYAKELVDRM GLGKTSNVEP PEFGAAADGD
     ADRNMILGKR FFVTPSDSVA IIAANAVQSI PYFASGLKGV ARSMPTSAAL DVVAKNLNLK
     FFEVPTGWKF FGNLMDAGMC SVCGEESFGT GSDHIREKDG IWAVLAWLSI LAYKNKDNLG
     GDKLVTVENI VLQHWGIYGR HYYTRYDYEN VDAEAAKELM ANLVKMQSSL SDVNKLIKEI
     QPNVADVVSA DEFEYTDPVD GSVSKHQGIR YLFGDGSRLV FRLSGTGSVG ATIRIYIEQY
     EKDSSKTGRE SSDALSPLVD VALKLSKIQE LTGRSAPTVI T