ID PGM1_YEAST Reviewed; 570 AA. AC P33401; D6VX68; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 04-NOV-2026, entry version 207. DE RecName: Full=Phosphoglucomutase 1 {ECO:0000303|PubMed:5784209}; DE Short=PGM 1 {ECO:0000303|PubMed:5784209}; DE EC=5.4.2.2 {ECO:0000269|PubMed:23103740}; DE AltName: Full=Glucose phosphomutase 1; GN Name=PGM1 {ECO:0000303|PubMed:5784209}; GN OrderedLocusNames=YKL127W {ECO:0000312|SGD:S000001610}; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8119301; DOI=10.1111/j.1432-1033.1994.tb18601.x; RA Boles E., Liebetrau W., Hofmann M., Zimmermann F.K.; RT "A family of hexosephosphate mutases in Saccharomyces cerevisiae."; RL Eur. J. Biochem. 220:83-96(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP FUNCTION. RC STRAIN=8050B; RX PubMed=14264884; DOI=10.1016/0926-6569(64)90011-2; RA Tsoi A., Douglas H.C.; RT "The effect of mutation of two forms of phosphoglucomutase in RT Saccharomyces."; RL Biochim. Biophys. Acta 92:513-520(1964). RN [5] RP FUNCTION. RX PubMed=5231755; DOI=10.1073/pnas.57.5.1482; RA Joshi J.G., Hooper J., Kuwaki T., Sakurada T., Swanson J.R., Handler P.; RT "Phosphoglucomutase. V. Multiple forms of phosphoglucomutase."; RL Proc. Natl. Acad. Sci. U.S.A. 57:1482-1489(1967). RN [6] RP FUNCTION. RX PubMed=5784209; DOI=10.1128/jb.98.2.532-535.1969; RA Bevan P., Douglas H.C.; RT "Genetic control of phosphoglucomutase variants in Saccharomyces RT cerevisiae."; RL J. Bacteriol. 98:532-535(1969). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=23103740; DOI=10.1016/j.febslet.2012.09.042; RA Walther T., Baylac A., Alkim C., Vax A., Cordier H., Francois J.M.; RT "The PGM3 gene encodes the major phosphoribomutase in the yeast RT Saccharomyces cerevisiae."; RL FEBS Lett. 586:4114-4118(2012). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Minor phosphoglucomutase isozyme that catalyzes the CC reversible interconversion of alpha-D-glucose 1-phosphate and alpha-D- CC glucose 6-phosphate (PubMed:23103740, PubMed:5784209). The mechanism CC proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate CC (Probable). Constitutes about 10-20% of the phosphoglucomutase activity CC in the cell (PubMed:14264884, PubMed:5231755). Key enzyme in hexose CC metabolism. The forward reaction is an essential step in the energy CC metabolism of galactose since the product of the galactose pathway CC enzymes in yeast is glucose 1-phosphate. The reverse reaction is an CC essential step for biosynthesis when carbon sources other than CC galactose are the energy source because glucose 1-phosphate is the CC starting point for the synthesis of UDP-glucose, which acts as a CC precursor for the synthesis of oligosaccharides and trehalose CC (PubMed:14264884). {ECO:0000269|PubMed:14264884, CC ECO:0000269|PubMed:23103740, ECO:0000269|PubMed:5231755, CC ECO:0000269|PubMed:5784209, ECO:0000305|PubMed:23103740}. 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:23103740}; 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:23103740}; 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:23103740}; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=60 uM for alpha-D-glucose 1-phosphate CC {ECO:0000269|PubMed:23103740}; CC Vmax=0.24 umol/min/mg enzyme for alpha-D-glucose 1-phosphate CC {ECO:0000269|PubMed:23103740}; CC Vmax=0.06 umol/min/mg enzyme for D-ribose 1-phosphate CC {ECO:0000269|PubMed:23103740}; CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P37012}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 9820 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; X72016; CAA50895.1; -; Genomic_DNA. DR EMBL; Z28127; CAA81968.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09034.1; -; Genomic_DNA. DR PIR; S41199; S41199. DR RefSeq; NP_012795.1; NM_001179693.1. DR AlphaFoldDB; P33401; -. DR SMR; P33401; -. DR BioGRID; 34009; 193. DR DIP; DIP-4098N; -. DR FunCoup; P33401; 574. DR IntAct; P33401; 10. DR STRING; 4932.YKL127W; -. DR iPTMnet; P33401; -. DR PaxDb; 4932-YKL127W; -. DR PeptideAtlas; P33401; -. DR EnsemblFungi; YKL127W_mRNA; YKL127W; YKL127W. DR GeneID; 853732; -. DR KEGG; sce:YKL127W; -. DR AGR; SGD:S000001610; -. DR SGD; S000001610; PGM1. DR VEuPathDB; FungiDB:YKL127W; -. DR eggNOG; KOG0625; Eukaryota. DR HOGENOM; CLU_009330_0_1_1; -. DR InParanoid; P33401; -. DR OMA; AAMYDFL; -. DR OrthoDB; 2291at2759; -. DR BioCyc; MetaCyc:YKL127W-MONOMER; -. DR BioCyc; YEAST:YKL127W-MONOMER; -. DR Reactome; R-SCE-3322077; Glycogen synthesis. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis). DR Reactome; R-SCE-70370; Galactose catabolism. DR SABIO-RK; P33401; -. DR BioGRID-ORCS; 853732; 2 hits in 10 CRISPR screens. DR PRO; PR:P33401; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P33401; protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. 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; IGI:SGD. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0019388; P:galactose catabolic process; IGI:SGD. DR GO; GO:0019255; P:glucose 1-phosphate metabolic process; IGI:SGD. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IGI:SGD. DR GO; GO:0005978; P:glycogen biosynthetic process; IGI:SGD. DR GO; GO:0005992; P:trehalose biosynthetic process; IGI:SGD. DR GO; GO:0006011; P:UDP-alpha-D-glucose metabolic process; IGI:SGD. 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:000006; Phosphoglucomutase PgmA; 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:SF2; PHOSPHOGLUCOMUTASE; 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 INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..570 FT /note="Phosphoglucomutase 1" FT /id="PRO_0000147796" FT ACT_SITE 120 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 24 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 120 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 120 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via phosphate group" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 295 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 296 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 360 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 379 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 381 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT BINDING 392 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000250|UniProtKB:P00949" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" SQ SEQUENCE 570 AA; 63112 MW; D6C5EA41AC62CE85 CRC64; MSLLIDSVPT VAYKDQKPGT SGLRKKTKVF MDEPHYTENF IQATMQSIPN GSEGTTLVVG GDGRFYNDVI MNKIAAVGAA NGVRKLVIGQ GGLLSTPAAS HIIRTYEEKC TGGGIILTAS HNPGGPENDL GIKYNLPNGG PAPESVTNAI WEASKKLTHY KIIKNFPKLN LNKLGKNQKY GPLLVDIIDP AKAYVQFLKE IFDFDLIKSF LAKQRKDKGW KLLFDSLNGI TGPYGKAIFV DEFGLPAEEV LQNWHPLPDF GGLHPDPNLT YARTLVDRVD REKIAFGAAS DGDGDRNMIY GYGPAFVSPG DSVAIIAEYA PEIPYFAKQG IYGLARSFPT SSAIDRVAAK KGLRCYEVPT GWKFFCALFD AKKLSICGEE SFGTGSNHIR EKDGLWAIIA WLNILAIYHR RNPEKEASIK TIQDEFWNEY GRTFFTRYDY EHIECEQAEK VVALLSEFVS RPNVCGSHFP ADESLTVIDC GDFSYRDLDG SISENQGLFV KFSNGTKFVL RLSGTGSSGA TIRLYVEKYT DKKENYGQTA DVFLKPVINS IVKFLRFKEI LGTDEPTVRT //