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 22-FEB-2023, entry version 88. 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). 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}. 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; 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; 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: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 Pfam; PF00408; PGM_PMM_IV; 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 //