PGMP_BRANA
ID PGMP_BRANA Reviewed; 629 AA.
AC Q9SMM0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
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;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ascari;
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}.
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DR EMBL; AJ250771; CAB60109.1; -; mRNA.
DR RefSeq; NP_001302927.1; NM_001315998.1.
DR AlphaFoldDB; Q9SMM0; -.
DR SMR; Q9SMM0; -.
DR GeneID; 106423685; -.
DR KEGG; bna:106423685; -.
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; 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 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; Plastid; Transit peptide.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..629
FT /note="Phosphoglucomutase, chloroplastic"
FT /id="PRO_0000023896"
FT ACT_SITE 187
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 356..357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 439..441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 582
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 629 AA; 68554 MW; D67A6937B7B60F1A CRC64;
MSSTYARFDT VFLLSRFAGA KYSPLWPSSS SSSHSSLLSS GIHLRAKPNS RLRSVTGASS
SSSGPIIAGS ESIEIKSLPT KPIEGQKTGT SGLRKKVKVF MQDNYLANWI QALFNSLPLE
DYKDATLVLG GDGRYFNKEA SQIIIKIAAG NGVGKILVGQ EGILSTPAVS AVIRKRKANG
GFIMSASHNP GGPEYDWGIK FNYSSGQPAP ESITDKIYGN TLSISEIKVA EIPDIDLSHV
GVTKYGNFSV EVIDPISDYL ELMEDVFDFD LIRGLLSRSD FGFMFDAMHA VTGAYAKPIF
VDNLEAKPDS ISNGVPLEDF GHGHPDPNLT YAKDLVDVMY RDDGPDFGAA SDGDGDRNMV
LGNKFFVTPS DSVAIIAANA QEAIPYFRAG PKGLARSMPT SGALDRVAEK LKLPFFEVPT
GWKFFGNLMD AGKLSICGEE SFGTGSDHIR EKDGIWAVLA WLSILAHRIK DKKPGEKLVS
VADVVNEYWA TYGRNFFSRY DYEECESEGA NKMIEYLRDI VAKSKAGENY GNYVLQFADD
FSYKDPVDGS VASKQGVRFV FTDGSRIIYR LSGNGSAGAT VRIYIEQFEP DVSKHDVDAQ
IAIKPLIDLA LSVSKLKEFT GREKPTVIT
