ID PGMC_PEA Reviewed; 582 AA.
AC Q9SM60;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 89.
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 Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BC1; TISSUE=Cotyledon;
RX PubMed=10759514; DOI=10.1104/pp.122.4.1187;
RA Harrison C.J., Mould R.M., Leech M.J., Johnson S.A., Turner L.,
RA Schreck S.L., Baird K.M., Jack P.L., Rawsthorne S., Hedley C.L., Wang T.L.;
RT "The rug3 locus of pea encodes plastidial phosphoglucomutase.";
RL Plant Physiol. 122:1187-1192(2000).
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; AJ250769; CAB60127.1; -; mRNA.
DR AlphaFoldDB; Q9SM60; -.
DR SMR; Q9SM60; -.
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 CDD; cd03085; PGM1; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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; 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:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
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_0000147804"
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 535
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 582 AA; 63325 MW; 5FF85499D031E2EB CRC64;
MALFTVSRIQ TTPFDGQKPG TSGLRKKVKV FVQPHYLENF VQASFNALTE GKVRGATLVV
SGDGRYYSEQ AIQIITKMAA ANGVRRIWIG QNGLLSTPAV SAVIRERVGV DGSKATGSFI
LTASHNPGGP NEDFGIKYNM ENGGPAPEGI TNKIYENTTT IKEYLIAPDL PNVDITTVGV
TNFTGPEGPF DIEVFDSASD YIKLMKSIFD FESIRKLLTS PKFSFCYDAL HGVAGAYAKR
IFVDELGAQE NSLINCVPKE DFGGGHPDPN LTYAKELVAR MGLGKSEPEG EVPEFGAAAD
GDADRNMVLG KRFFVTPSDS VAIIAANAVE AIPYFSAGLK GVARSMPTSA ALDVVAKHLN
LKFFEVPTGW KFFGNLMDAG LCSVCGEESF GTGSDHIREK DGIWAVLAWL SILAYKTKDN
LESKLVSVED IVRQHWATYG RHYYTRYDYE NVDAGAAKEL MAHLVKLQSS LPEVNEIIKG
ASSDVSKVVH GDEFEYNDPV DGSISSHQGI RYLFEDGSRL IFRLSGTGSE GATIRLYIEQ
YEKDPSKIGR LSHEALAPLV EAALKLSKME EFTGRSAPTV IT
//
