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 02-OCT-2024, entry version 91. DE RecName: Full=Phosphoglucomutase, cytoplasmic; DE Short=PGM; DE EC=5.4.2.2 {ECO:0000250|UniProtKB:P93804}; 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: Catalyzes the reversible isomerization of alpha-D-glucose 1- CC phosphate to alpha-D-glucose 6-phosphate (By similarity). The mechanism CC proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate CC (By similarity). This enzyme participates in both the breakdown and CC synthesis of glucose (By similarity). {ECO:0000250|UniProtKB:P36871, CC ECO:0000250|UniProtKB:P93804}. 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; Evidence={ECO:0000250|UniProtKB:P93804}; CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = CC alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]; CC Xref=Rhea:RHEA:68748, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:58392, ChEBI:CHEBI:58601, CC ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P93804}; CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = alpha- CC D-glucose 6-phosphate + O-phospho-L-seryl-[protein]; CC Xref=Rhea:RHEA:68752, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:58225, ChEBI:CHEBI:58392, CC ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P93804}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00949}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949}; CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00949}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P93804}. 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; 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 25 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 124 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" 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 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 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" 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 305 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 368 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 387 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 389 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 400 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT MOD_RES 124 FT /note="Phosphoserine" 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 //