PGMC_SOLTU
ID PGMC_SOLTU Reviewed; 583 AA.
AC Q9M4G4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Phosphoglucomutase, cytoplasmic;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase;
GN Name=PGM1; Synonyms=PGM I;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tuber;
RA Tauberger E.;
RL Thesis (1999), Freie Universitaet Berlin, Germany.
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; AJ240054; CAB93681.1; -; mRNA.
DR RefSeq; NP_001275333.1; NM_001288404.1.
DR AlphaFoldDB; Q9M4G4; -.
DR SMR; Q9M4G4; -.
DR PRIDE; Q9M4G4; -.
DR GeneID; 102579912; -.
DR KEGG; sot:102579912; -.
DR InParanoid; Q9M4G4; -.
DR OrthoDB; 555015at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..583
FT /note="Phosphoglucomutase, cytoplasmic"
FT /id="PRO_0000147806"
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; 63470 MW; DF3E24B9972C7CCA CRC64;
MANFKVSRVE TTPFEGQKPG TSGLRKKVKV FIQPHYLQNF VQATFNALGA DRVEGATLVV
SGDGRYYSKD AIQIITKMAA ANGVRRVWIG QNGLLSTPAV SAVVRERVGA DGSKATGAFI
LTASHNPGGP HEDFGIKYNM ENGGPAPEGI TNKIYENTTT IKEYLIAEGL PDVDISTTGV
SSFEGPKGKF DVDVFDSTSD YLKLLKSIFD FPAIQKLLSS PKFSFCYDAL HGVAGVHAKR
IFVEELGANE SSLVNCVPKE DFGGGHPDPN LTYAKELVAR MGLSKTHSEP NPPEFGAAAD
GDGDRNMVLG KRFFVTPSDS VAIIAANAVQ AIPYFSGGLK GVARSMPTSA ALDIVAKHLN
LKFFEVPTGW KFFGNLMDAG MCSICGEESF GTGSDHIREK DGIWAVLAWL SILAYKNKDN
LGEGNLVSVE DIVRQHWAIY GRHYYTRYDY ENVNADGAKD LMAHLVKLQS SIDEVNKLIK
GIRSDVSNVV HADEFEYKDP VDGSVSKHQG IRYLFEDGSR LVFRLSGTGS EGATIRLYIE
QYEKDSSKIG RDSQEALAPL VEVALKLSKM QEYTSRSAPT VIT
