ID PGM1_RAT Reviewed; 562 AA. AC P38652; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 152. DE RecName: Full=Phosphoglucomutase-1; DE Short=PGM 1; DE EC=5.4.2.2 {ECO:0000269|PubMed:8224913}; DE AltName: Full=Glucose phosphomutase 1; GN Name=Pgm1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE RP SPECIFICITY. RC TISSUE=Liver; RX PubMed=8224913; DOI=10.1016/0378-1119(93)90649-n; RA Rivera A.A., Elton T.S., Dey N.B., Bounelis P., Marchase R.B.; RT "Isolation and expression of a rat liver cDNA encoding RT phosphoglucomutase."; RL Gene 133:261-266(1993). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-134; SER-213; RP SER-369; SER-477; SER-485; SER-505; THR-507; SER-509 AND SER-541, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1- CC phosphate to alpha-D-glucose 6-phosphate (PubMed:8224913). The CC mechanism proceeds via the intermediate compound alpha-D-glucose 1,6- CC bisphosphate (Probable). This enzyme participates in both the breakdown CC and synthesis of glucose (By similarity). CC {ECO:0000250|UniProtKB:P36871, ECO:0000269|PubMed:8224913, CC ECO:0000305|PubMed:8224913}. 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:0000269|PubMed:8224913}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + alpha-D-glucose 1-phosphate = 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:0000305|PubMed:8224913}; CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = O- CC phospho-L-seryl-[protein] + alpha-D-glucose 6-phosphate; 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:0000305|PubMed:8224913}; 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. CC -!- TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:8224913}. CC -!- PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances CC enzymatic activity. {ECO:0000250|UniProtKB:P36871}. 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; L11694; AAA16862.1; -; mRNA. DR PIR; JC2011; PMRT. DR AlphaFoldDB; P38652; -. DR SMR; P38652; -. DR FunCoup; P38652; 1275. DR STRING; 10116.ENSRNOP00000013785; -. DR iPTMnet; P38652; -. DR PhosphoSitePlus; P38652; -. DR SwissPalm; P38652; -. DR jPOST; P38652; -. DR PaxDb; 10116-ENSRNOP00000013785; -. DR UCSC; RGD:3316; rat. DR AGR; RGD:3316; -. DR RGD; 3316; Pgm1. DR eggNOG; KOG0625; Eukaryota. DR InParanoid; P38652; -. DR PhylomeDB; P38652; -. DR Reactome; R-RNO-3322077; Glycogen synthesis. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis). DR Reactome; R-RNO-70370; Galactose catabolism. DR SABIO-RK; P38652; -. DR PRO; PR:P38652; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0030018; C:Z disc; IDA:RGD. DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD. DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:UniProtKB. DR GO; GO:0071259; P:cellular response to magnetism; IEP:RGD. DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose, Leloir pathway; ISO:RGD. DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB. DR GO; GO:0005980; P:glycogen catabolic process; ISO:RGD. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; TAS:RGD. DR CDD; cd03085; PGM1; 1. DR FunFam; 3.30.310.50:FF:000002; Phosphoglucomutase 5; 1. DR FunFam; 3.40.120.10:FF:000004; Phosphoglucomutase 5; 1. DR FunFam; 3.40.120.10:FF:000005; Phosphoglucomutase 5; 1. DR FunFam; 3.40.120.10:FF:000007; Phosphoglucomutase 5; 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 NCBIfam; NF005737; PRK07564.1-1; 1. DR PANTHER; PTHR22573:SF37; PHOSPHOGLUCOMUTASE-1; 1. DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1. DR Pfam; PF24947; PGM1_C_vert_fung; 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 1: Evidence at protein level; KW Acetylation; Carbohydrate metabolism; Cytoplasm; Glucose metabolism; KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..562 FT /note="Phosphoglucomutase-1" FT /id="PRO_0000147780" FT ACT_SITE 117 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 23 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 117 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via phosphate group" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 290 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 292 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 292 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 293 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 357 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 376 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 378 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 MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 16 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 115 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 134 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 185 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 349 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 353 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 369 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 378 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 419 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 467 FT /note="Phosphothreonine; by PAK1" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 477 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 485 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 507 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 541 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" SQ SEQUENCE 562 AA; 61403 MW; 584FAC13B7C3B256 CRC64; MVKIVTVKTQ AYPDQKPGTS GLRKRVKVFQ GNANYAENFI QSIVSTVEPA LRQEATLVVG GDGRFYMTEA IQLIVRIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAIC PDLKVDLGVL GKQQFDLENK FKPFTVEIVD SVEAYATMLR NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ASYETPTGWK FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQRVE DILKDHWQKF GRNFFTRYDY EEVEAEGANK MMKDLEALML DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV DGSISKNQGL RLIFADGSRI IFRLSGTGSA GATIRLYIDS YEKDAAKINQ DPQVMLAPLI SIALKVSQLQ ERTGRTAPTV IT //