PGMC_MESCR
ID PGMC_MESCR Reviewed; 583 AA.
AC P93262;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Phosphoglucomutase, cytoplasmic;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase;
GN Name=PGM1;
OS Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Aizoaceae; Mesembryanthemum;
OC Mesembryanthemum subgen. Cryophytum.
OX NCBI_TaxID=3544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Michalowski C.B., Quigley-Landreau F., Bohnert H.J.;
RL Submitted (JAN-1997) 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; U84888; AAB41895.1; -; mRNA.
DR PIR; T12574; T12574.
DR AlphaFoldDB; P93262; -.
DR SMR; P93262; -.
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..583
FT /note="Phosphoglucomutase, cytoplasmic"
FT /id="PRO_0000147803"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 304..305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 387..389
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 536
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 583 AA; 63446 MW; F7418E2CE4C716A2 CRC64;
MATFKVSRVE TKPYDGQKPG TSGLRKKVKV FAQPHYLENF VQSTFDALTA DKIKGKTLVV
SGDGRYYSEQ AIQTIIKMSA ANGVKSVWVG QDGLLSTPAV SAVIRERVGK DGSKASGAFI
LTASHNPGGP NEDFGIKYNM ENGGPAQEGV TNKIYENTTT IKEYLIAKEL PNVNISKTGV
TSFSGPDGQF DVEVFDATET YVKLMKSIFD FQAIKKLLSI PSFTFCYDAL HGVAGVYAKR
IFVDELGANE SSLLNCTPKE DFGGGHPDPN LTYAKELVER MGLGKSNTQG EPPEFGAAAD
GDADRNMILG KRFFVTPSDS VAIIAANAVE AIPYFSGGLK GVARSMPTSA ALDVVAKHLN
LKFFEVPTGW KFFGNLMDAG VCSICGEESF GTGSDHVREK DGIWAVLAWL SILAHKNKDN
LNGEKLVTVE DIVCQHWATY GRHYYTRYDY ENVDAGGAKE LMAYLVNLQS DLSKVNNIVK
GVHSGVANVI AADEFEYKDP VDGSVSKHQG IRYMFEDGSR LIFRLSGTGS EGATIRLYIE
QYEKDSSKTG RDSQEALKPL VDVALKLSKM QEFSGRSEPT VIT
