PGMP_PEA
ID PGMP_PEA Reviewed; 626 AA.
AC Q9SM59;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Phosphoglucomutase, chloroplastic;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase;
DE Flags: Precursor;
GN Name=PGMP; Synonyms=RUG3;
OS Pisum sativum (Garden pea).
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: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ250770; CAB60128.1; -; mRNA.
DR AlphaFoldDB; Q9SM59; -.
DR SMR; Q9SM59; -.
DR PRIDE; Q9SM59; -.
DR EnsemblPlants; Psat6g201960.1; Psat6g201960.1.cds; Psat6g201960.
DR Gramene; Psat6g201960.1; Psat6g201960.1.cds; Psat6g201960.
DR GO; GO:0009507; C:chloroplast; 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; 1.
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; Chloroplast; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Plastid; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..626
FT /note="Phosphoglucomutase, chloroplastic"
FT /id="PRO_0000023897"
FT ACT_SITE 184
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 353..354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 436..438
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 626 AA; 68575 MW; B820E069AFA0D34E CRC64;
MAFCYRLDNF IISAFKPKHS NVPLSIHHSS SNFPSFKVQN FPFRVRYNSA IRATSSSSST
PTTIAEPNDI KINSIPTKPI EGQKTGTSGL RKKVKVFKQE NYLANWIQAL FNSLPPEDYK
NGLLVLGGDG RYFNKEAAQI IIKIAAGNGV GKILVGKEGI LSTPAVSAVI RKREANGGFI
MSASHNPGGP EYDWGIKFNY SSGQPAPESI TDKIYGNTLS ISEIKIADIP DVDLSNVGVT
KFGSFSVEVI DPVSDYLELL ETVFDFQLIK SLISRPDFRF TFDAMHAVAG AYATPIFVDK
LSASLDSISN GIPLEDFGHG HPDPNLTYAK DLVKIMYAEN GPDFGAASDG DGDRNMILGT
SFFVTPSDSV AVIAANAKEA IPYFKDSIKG LARSMPTSGA LDRVAEKLNL PFFEVPTGWK
FFGNLMDAGN LSICGEESFG TGSDHIREKD GIWAVLAWLS IIAHRNKDTK PGEKLVSVSD
VVKEHWATYG RNFFSRYDYE ECESEGANKM IEYLRELLSK SKPGDKYGSY VLQFADDFTY
TDPVDGSVVS KQGVRFVFTD GSRIIYRLSG TGSAGATVRV YIEQFEPDVS KHDVDAQIAL
KPLIDLALSV SKLKDFTGRE KPTVIT
