PGMP_SOLTU
ID PGMP_SOLTU Reviewed; 632 AA.
AC Q9M4G5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=PGM II;
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: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AJ240053; CAB93680.1; -; mRNA.
DR RefSeq; NP_001275281.1; NM_001288352.1.
DR AlphaFoldDB; Q9M4G5; -.
DR SMR; Q9M4G5; -.
DR PRIDE; Q9M4G5; -.
DR GeneID; 102585015; -.
DR KEGG; sot:102585015; -.
DR InParanoid; Q9M4G5; -.
DR OrthoDB; 555015at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 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; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..632
FT /note="Phosphoglucomutase, chloroplastic"
FT /id="PRO_0000023898"
FT ACT_SITE 190
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 190..191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 359..360
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 442..444
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 585
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 632 AA; 68906 MW; 4F1EAF33784EF735 CRC64;
MAMESALTST RVSIPSLCSG ISSSHHHHRS LSFLNFPKLS SFKYSFRTIS PVPFVVSASS
VSPSSPSTSV AQSQDLKIKS VPTKPIEGQK TGTSGLRKKV KVFMQDNYLA NWIQALFNSL
PLEDYKNGLL VLGGDGRYFN REAAQIIIKI AAGNGVGKIL VGKDGILSTQ AVSAVIRKRE
ANGGFIMSAS HNPGGPEYDW GIKFNYSSGQ PAPESITDKI YGNTLSISEI KIADIPDVDL
SQLGVTKYGN FSVEVVDPVA DYLELMENVF DFSLIRSLVS RPDFRFVFDA MHAVTGAYAK
PIFVDKLGAS LESIANGVPL EDFGHGHPDP NLTYAEDLVN ILYGENGPDF GAASDGDGDR
NMILGRSFFV TPSDSVAIIA AQCQYAIHYF QSGPKGLARS MPTSGSLDRV AQKLNLPFFE
VPTGWKFFGN LMDAGKLSIC GEESFGTGSD HIREKDGIWA VLAWLSILAY RNKDKKSGEK
LVSVADVVKD HWATYGRNFF SRYDYEECES EGANNMIEYL RDLISKSKAG DKYGSYSLDF
ADDFAYTDPV DGSVASKQGV RFVFSDGSRI IFRLSGTGSA GATVRIYIEQ FEPDVSKHDM
DAQIALKPLI DLALSVSKLK DFTGREKPTV IT
