PMG1_YEAST
ID PMG1_YEAST Reviewed; 247 AA.
AC P00950; D6VX45; Q02117;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Phosphoglycerate mutase 1;
DE Short=PGAM 1;
DE EC=5.4.2.11 {ECO:0000269|PubMed:1386023};
DE AltName: Full=BPG-dependent PGAM 1;
DE AltName: Full=MPGM 1;
DE AltName: Full=Phosphoglyceromutase 1;
GN Name=GPM1; Synonyms=GPM; OrderedLocusNames=YKL152C; ORFNames=YKL607;
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 PRELIMINARY PROTEIN SEQUENCE OF 2-247.
RX PubMed=6127696; DOI=10.1098/rspb.1982.0026;
RA Fothergill L.A., Harkins R.N.;
RT "The amino acid sequence of yeast phosphoglycerate mutase.";
RL Proc. R. Soc. Lond., B, Biol. Sci. 215:19-44(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2831102; DOI=10.1016/0014-5793(88)81161-x;
RA White M.F., Fothergill-Gilmore L.A.;
RT "Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 229:383-387(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1834353; DOI=10.1007/bf00312781;
RA Heinisch J.J., von Borstel R.C., Rodicio R.M.;
RT "Sequence and localization of the gene encoding yeast phosphoglycerate
RT mutase.";
RL Curr. Genet. 20:167-171(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=8462867; DOI=10.1016/0378-1119(93)90319-x;
RA Rodicio R., Heinisch J.J., Hollenberg C.P.;
RT "Transcriptional control of yeast phosphoglycerate mutase-encoding gene.";
RL Gene 125:125-133(1993).
RN [8]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=ATCC 26786 / X2180-1A;
RA Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 110-114 AND 204-217.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9509572;
RX DOI=10.1002/(sici)1097-0061(199712)13:16<1519::aid-yea211>3.0.co;2-u;
RA Norbeck J., Blomberg A.;
RT "Two-dimensional electrophoretic separation of yeast proteins using a non-
RT linear wide range (pH 3-10) immobilized pH gradient in the first dimension;
RT reproducibility and evidence for isoelectric focusing of alkaline (pI > 7)
RT proteins.";
RL Yeast 13:1519-1534(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-182, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1386023; DOI=10.1111/j.1432-1033.1992.tb17099.x;
RA White M.F., Fothergill-Gilmore L.A.;
RT "Development of a mutagenesis, expression and purification system for yeast
RT phosphoglycerate mutase. Investigation of the role of active-site His181.";
RL Eur. J. Biochem. 207:709-714(1992).
RN [11]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-169, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8240286; DOI=10.1042/bj2950743;
RA White M.F., Fothergill-Gilmore L.A., Kelly S.M., Price N.C.;
RT "Dissociation of the tetrameric phosphoglycerate mutase from yeast by a
RT mutation in the subunit contact region.";
RL Biochem. J. 295:743-748(1993).
RN [12]
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 [13]
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 [14]
RP SUBCELLULAR LOCATION.
RX PubMed=16962558; DOI=10.1016/j.bbabio.2006.07.001;
RA Brandina I., Graham J., Lemaitre-Guillier C., Entelis N.,
RA Krasheninnikov I., Sweetlove L., Tarassov I., Martin R.P.;
RT "Enolase takes part in a macromolecular complex associated to mitochondria
RT in yeast.";
RL Biochim. Biophys. Acta 1757:1217-1228(2006).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-116 AND SER-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-127 AND SER-197, AND
RP IDENTIFICATION BY 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49; SER-116; SER-128 AND
RP SER-197, AND IDENTIFICATION BY 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [22]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-57; LYS-71; LYS-139;
RP LYS-175 AND LYS-191, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH
RP 3-PHOSPHO-D-GLYCERATE, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=6115412; DOI=10.1098/rstb.1981.0066;
RA Winn S.I., Watson H.C., Harkins R.N., Fothergill L.A.;
RT "Structure and activity of phosphoglycerate mutase.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:121-130(1981).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=9512715; DOI=10.1006/jmbi.1997.1554;
RA Rigden D.J., Alexeev D., Phillips S.E.V.P., Fothergill-Gilmore L.A.;
RT "The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate
RT mutase.";
RL J. Mol. Biol. 276:449-459(1998).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP 3-PHOSPHO-D-GLYCERATE, SUBUNIT, AND ACTIVE SITE.
RX PubMed=10531478; DOI=10.1107/s0907444999009944;
RA Crowhurst G.S., Dalby A.R., Isupov M.N., Campbell J.W., Littlechild J.A.;
RT "Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at
RT 1.7 A.";
RL Acta Crystallogr. D 55:1822-1826(1999).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=10064712; DOI=10.1006/jmbi.1999.2566;
RA Rigden D.J., Walter R.A., Phillips S.E., Fothergill-Gilmore L.A.;
RT "Sulphate ions observed in the 2.12 A structure of a new crystal form of S.
RT cerevisiae phosphoglycerate mutase provide insights into understanding the
RT catalytic mechanism.";
RL J. Mol. Biol. 286:1507-1517(1999).
RN [27] {ECO:0007744|PDB:1BQ3, ECO:0007744|PDB:1BQ4}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=10369755; DOI=10.1006/jmbi.1999.2848;
RA Rigden D.J., Walter R.A., Phillips S.E., Fothergill-Gilmore L.A.;
RT "Polyanionic inhibitors of phosphoglycerate mutase: combined structural and
RT biochemical analysis.";
RL J. Mol. Biol. 289:691-699(1999).
CC -!- FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-
CC bisphosphoglycerate as the primer of the reaction. Can also Catalyzes
CC the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
CC {ECO:0000269|PubMed:1386023, ECO:0000269|PubMed:8240286}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000269|PubMed:1386023};
CC -!- ACTIVITY REGULATION: Inhibited by inositol hexakisphosphate and benzene
CC tri-, tetra- and hexacarboxylates. {ECO:0000269|PubMed:10369755}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=740 uM for 3-phosphoglycerate {ECO:0000269|PubMed:1386023,
CC ECO:0000269|PubMed:8240286};
CC KM=8.1 uM for 2,3-bisphosphoglycerate (for mutase reaction)
CC {ECO:0000269|PubMed:1386023, ECO:0000269|PubMed:8240286};
CC KM=2.4 uM for 2,3-bisphosphoglycerate (for phosphatase reaction)
CC {ECO:0000269|PubMed:1386023, ECO:0000269|PubMed:8240286};
CC Note=kcat is 490 sec(-1) for the mutase reaction, 0.0074 sec(-1) for
CC the synthase reaction and 0.0087 sec(-1) for the phosphatase reaction
CC with 3-phosphoglycerate as substrate. {ECO:0000269|PubMed:1386023};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SUBUNIT: Homotetramer: dimer of dimers. {ECO:0000269|PubMed:10064712,
CC ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478,
CC ECO:0000269|PubMed:6115412, ECO:0000269|PubMed:8240286,
CC ECO:0000269|PubMed:9512715}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:16962558}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}; Cytoplasmic
CC side {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}.
CC Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
CC -!- MISCELLANEOUS: Present with 172000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; X06408; CAA29698.1; -; Genomic_DNA.
DR EMBL; X58789; CAA41595.1; -; Genomic_DNA.
DR EMBL; Z26877; CAA81501.1; -; Genomic_DNA.
DR EMBL; Z28152; CAA81994.1; -; Genomic_DNA.
DR EMBL; S57976; AAB26026.1; ALT_TERM; Genomic_DNA.
DR EMBL; BK006944; DAA09011.1; -; Genomic_DNA.
DR PIR; S00358; PMBYY.
DR RefSeq; NP_012770.1; NM_001179718.1.
DR PDB; 1BQ3; X-ray; 2.70 A; A/B/C/D=2-247.
DR PDB; 1BQ4; X-ray; 2.50 A; A/B/C/D=2-247.
DR PDB; 1QHF; X-ray; 1.70 A; A/B=2-241.
DR PDB; 3PGM; X-ray; 2.80 A; A/B=2-247.
DR PDB; 4PGM; X-ray; 2.30 A; A/B/C/D=2-247.
DR PDB; 5PGM; X-ray; 2.12 A; A/B/C/D/E/F/G/H=2-247.
DR PDBsum; 1BQ3; -.
DR PDBsum; 1BQ4; -.
DR PDBsum; 1QHF; -.
DR PDBsum; 3PGM; -.
DR PDBsum; 4PGM; -.
DR PDBsum; 5PGM; -.
DR AlphaFoldDB; P00950; -.
DR SMR; P00950; -.
DR BioGRID; 33985; 113.
DR DIP; DIP-6260N; -.
DR IntAct; P00950; 116.
DR MINT; P00950; -.
DR STRING; 4932.YKL152C; -.
DR iPTMnet; P00950; -.
DR COMPLUYEAST-2DPAGE; P00950; -.
DR SWISS-2DPAGE; P00950; -.
DR MaxQB; P00950; -.
DR PaxDb; P00950; -.
DR PRIDE; P00950; -.
DR TopDownProteomics; P00950; -.
DR EnsemblFungi; YKL152C_mRNA; YKL152C; YKL152C.
DR GeneID; 853705; -.
DR KEGG; sce:YKL152C; -.
DR SGD; S000001635; GPM1.
DR VEuPathDB; FungiDB:YKL152C; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P00950; -.
DR OMA; RMLPYWY; -.
DR BioCyc; MetaCyc:YKL152C-MON; -.
DR BioCyc; YEAST:YKL152C-MON; -.
DR BRENDA; 5.4.2.11; 984.
DR SABIO-RK; P00950; -.
DR UniPathway; UPA00109; UER00186.
DR EvolutionaryTrace; P00950; -.
DR PRO; PR:P00950; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P00950; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:SGD.
DR GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR GO; GO:0006096; P:glycolytic process; IMP:SGD.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis; Isomerase;
KW Isopeptide bond; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..247
FT /note="Phosphoglycerate mutase 1"
FT /id="PRO_0000179839"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:10064712,
FT ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412,
FT ECO:0000269|PubMed:9512715"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:10064712"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10369755,
FT ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10369755,
FT ECO:0000269|PubMed:10531478"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10531478"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10369755,
FT ECO:0000269|PubMed:6115412"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10369755"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10369755"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10369755,
FT ECO:0000269|PubMed:6115412"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:10064712"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 49
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 169
FT /note="K->P: Causes dissociation of the homotetramer to
FT dimers at low concentrations."
FT /evidence="ECO:0000269|PubMed:8240286"
FT MUTAGEN 182
FT /note="H->A: Reduces kcat of the mutase reaction 10000-
FT fold."
FT /evidence="ECO:0000269|PubMed:1386023"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:1QHF"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:1QHF"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:1QHF"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3PGM"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3PGM"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:1QHF"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:1QHF"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1QHF"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1QHF"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3PGM"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1QHF"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3PGM"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1QHF"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1QHF"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1QHF"
SQ SEQUENCE 247 AA; 27609 MW; 45E1A9CCDBDC104D CRC64;
MPKLVLVRHG QSEWNEKNLF TGWVDVKLSA KGQQEAARAG ELLKEKKVYP DVLYTSKLSR
AIQTANIALE KADRLWIPVN RSWRLNERHY GDLQGKDKAE TLKKFGEEKF NTYRRSFDVP
PPPIDASSPF SQKGDERYKY VDPNVLPETE SLALVIDRLL PYWQDVIAKD LLSGKTVMIA
AHGNSLRGLV KHLEGISDAD IAKLNIPTGI PLVFELDENL KPSKPSYYLD PEAAAAGAAA
VANQGKK
