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 07-JAN-2015, entry version 70. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC 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., RA 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 CC synthesis of glucose. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose CC 6-phosphate. 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. CC {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 ProteinModelPortal; Q9SM60; -. DR SMR; Q9SM60; 6-582. DR PRIDE; 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 Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. 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; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. 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; Cytoplasm; Glucose metabolism; Isomerase; KW Magnesium; Metal-binding; Phosphoprotein. FT CHAIN 1 582 Phosphoglucomutase, cytoplasmic. FT /FTId=PRO_0000147804. FT REGION 124 125 Substrate binding. FT {ECO:0000250|UniProtKB:P00949}. FT REGION 304 305 Substrate binding. FT {ECO:0000250|UniProtKB:P00949}. FT REGION 387 389 Substrate binding. FT {ECO:0000250|UniProtKB:P00949}. FT ACT_SITE 124 124 Phosphoserine intermediate. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 124 124 Magnesium; via phosphate group. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 300 300 Magnesium. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 302 302 Magnesium. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 304 304 Magnesium. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 21 21 Substrate. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 25 25 Substrate. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 137 137 Substrate. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 368 368 Substrate. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 400 400 Substrate. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 535 535 Substrate. FT {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 //