ID   PGM2_YEAST              Reviewed;         569 AA.
AC   P37012; D6VZS7;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Phosphoglucomutase 2 {ECO:0000303|PubMed:5784209};
DE            Short=PGM 2 {ECO:0000303|PubMed:5784209};
DE            EC=5.4.2.2 {ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:23103740, ECO:0000269|PubMed:4992300};
DE   AltName: Full=D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase {ECO:0000303|PubMed:14264884};
DE   AltName: Full=Glucose phosphomutase 2;
GN   Name=PGM2 {ECO:0000303|PubMed:5784209};
GN   Synonyms=GA-5 {ECO:0000303|PubMed:13887540}, GAL5
GN   {ECO:0000303|PubMed:2138705};
GN   OrderedLocusNames=YMR105C {ECO:0000312|SGD:S000004711};
GN   ORFNames=YM9718.04C;
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 [GENOMIC DNA].
RA   Fu L., Bounelis P., Dey N., Browne B.L., Marchase R.B., Bedwell D.M.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   PROTEIN SEQUENCE OF 15-32 AND 265-275, SUBCELLULAR LOCATION, AND
RP   GLYCOSYLATION.
RX   PubMed=8385141; DOI=10.1016/s0021-9258(18)53101-x;
RA   Marchase R.B., Bounelis P., Brumley L.M., Dey N., Browne B., Auger D.,
RA   Fritz T.A., Kulesza P., Bedwell D.M.;
RT   "Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic
RT   glycoprotein and the acceptor for a Glc-phosphotransferase.";
RL   J. Biol. Chem. 268:8341-8349(1993).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=13887540; DOI=10.1016/0006-3002(61)90924-6;
RA   Douglas H.C.;
RT   "A mutation in Saccharomyces that affects phosphoglucomutase activity and
RT   galactose utilization.";
RL   Biochim. Biophys. Acta 52:209-211(1961).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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   [9]
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   [10]
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   [11]
RP   CATALYTIC ACTIVITY.
RX   PubMed=4992300; DOI=10.1093/oxfordjournals.jbchem.a129375;
RA   Hirose M., Sugimoto E., Sasaki R., Chiaa H.;
RT   "Crystallization and reaction mechanism of yeast phosphoglucomutase.";
RL   J. Biochem. 68:449-457(1970).
RN   [12]
RP   COFACTOR.
RX   PubMed=4628805; DOI=10.1016/0005-2744(72)90116-7;
RA   Hirose M., Sugimoto E., Chiba H.;
RT   "Studies on crystalline yeast phosphoglucomutase: the presence of intrinsic
RT   zinc.";
RL   Biochim. Biophys. Acta 289:137-146(1972).
RN   [13]
RP   CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=1100398; DOI=10.1111/j.1432-1033.1975.tb02282.x;
RA   Daugherty J.P., Kraemer W.F., Joshi J.G.;
RT   "Purification and properties of phosphoglucomutase from Fleischmann's
RT   yeast.";
RL   Eur. J. Biochem. 57:115-126(1975).
RN   [14]
RP   INDUCTION.
RX   PubMed=2138705; DOI=10.1128/mcb.10.4.1415-1422.1990;
RA   Oh D., Hopper J.E.;
RT   "Transcription of a yeast phosphoglucomutase isozyme gene is galactose
RT   inducible and glucose repressible.";
RL   Mol. Cell. Biol. 10:1415-1422(1990).
RN   [15]
RP   GLYCOSYLATION.
RX   PubMed=7929458; DOI=10.1016/s0021-9258(18)47136-0;
RA   Dey N.B., Bounelis P., Fritz T.A., Bedwell D.M., Marchase R.B.;
RT   "The glycosylation of phosphoglucomutase is modulated by carbon source and
RT   heat shock in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 269:27143-27148(1994).
RN   [16]
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   [17]
RP   IDENTIFICATION BY 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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; THR-117 AND SER-119, AND
RP   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   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   [21]
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: Major phosphoglucomutase isozyme that catalyzes the
CC       reversible interconversion of glucose 1-phosphate and glucose 6-
CC       phosphate (PubMed:5784209). Constitutes about 80-90% of the
CC       phosphoglucomutase activity in the cell (PubMed:14264884,
CC       PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction
CC       is an essential step in the energy metabolism of galactose since the
CC       product of the galactose pathway enzymes in yeast is glucose 1-
CC       phosphate. The reverse reaction is an essential step for biosynthesis
CC       when carbon sources other than galactose are the energy source because
CC       glucose 1-phosphate is the starting point for the synthesis of UDP-
CC       glucose, which acts as a precursor for the synthesis of
CC       oligosaccharides and trehalose (PubMed:14264884).
CC       {ECO:0000269|PubMed:14264884, ECO:0000269|PubMed:5231755}.
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:1100398,
CC         ECO:0000269|PubMed:23103740, ECO:0000269|PubMed:4992300};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:4628805};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:4628805};
CC       Note=Binds 1 magnesium ion per subunit. Can also use Zn(2+) as
CC       cofactor. {ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:4628805};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.24 uM for alpha-D-glucose 1,6-diphosphate
CC         {ECO:0000269|PubMed:1100398};
CC         KM=23.4 uM for alpha-D-glucose 1-phosphate
CC         {ECO:0000269|PubMed:1100398};
CC         KM=26 uM for alpha-D-glucose 1-phosphate
CC         {ECO:0000269|PubMed:23103740};
CC         KM=530 uM for D-ribose 1-phosphate {ECO:0000269|PubMed:23103740};
CC         Vmax=33.7 umol/min/mg enzyme for alpha-D-glucose 1-phosphate
CC         {ECO:0000269|PubMed:23103740};
CC         Vmax=0.32 umol/min/mg enzyme for D-ribose 1-phosphate
CC         {ECO:0000269|PubMed:23103740};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1100398}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8385141}.
CC   -!- INDUCTION: Induced in response to galactose and severely repressed in
CC       response to glucose. {ECO:0000269|PubMed:2138705}.
CC   -!- PTM: O-glycosylated with mannose residues (By similarity). Substrate of
CC       UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose
CC       in a phosphodiester linkage to O-linked mannose (PubMed:8385141,
CC       PubMed:7929458). {ECO:0000250|UniProtKB:P47244,
CC       ECO:0000269|PubMed:7929458, ECO:0000269|PubMed:8385141}.
CC   -!- DISRUPTION PHENOTYPE: Blocks galactose utilization, but does not impair
CC       growth on glucose. {ECO:0000269|PubMed:14264884}.
CC   -!- MISCELLANEOUS: Present with 3790 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; X74823; CAA52820.1; -; Genomic_DNA.
DR   EMBL; U09499; AAA91282.1; -; Genomic_DNA.
DR   EMBL; Z49702; CAA89741.1; -; Genomic_DNA.
DR   EMBL; AY723853; AAU09770.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10001.1; -; Genomic_DNA.
DR   PIR; S41200; S41200.
DR   RefSeq; NP_013823.1; NM_001182605.1.
DR   AlphaFoldDB; P37012; -.
DR   SMR; P37012; -.
DR   BioGRID; 35280; 127.
DR   DIP; DIP-6499N; -.
DR   IntAct; P37012; 28.
DR   MINT; P37012; -.
DR   STRING; 4932.YMR105C; -.
DR   iPTMnet; P37012; -.
DR   MaxQB; P37012; -.
DR   PaxDb; 4932-YMR105C; -.
DR   PeptideAtlas; P37012; -.
DR   EnsemblFungi; YMR105C_mRNA; YMR105C; YMR105C.
DR   GeneID; 855131; -.
DR   KEGG; sce:YMR105C; -.
DR   AGR; SGD:S000004711; -.
DR   SGD; S000004711; PGM2.
DR   VEuPathDB; FungiDB:YMR105C; -.
DR   eggNOG; KOG0625; Eukaryota.
DR   GeneTree; ENSGT00940000173602; -.
DR   HOGENOM; CLU_009330_0_1_1; -.
DR   InParanoid; P37012; -.
DR   OMA; WIQDRAN; -.
DR   OrthoDB; 5476118at2759; -.
DR   BioCyc; MetaCyc:YMR105C-MONOMER; -.
DR   BioCyc; YEAST:YMR105C-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; P37012; -.
DR   BioGRID-ORCS; 855131; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P37012; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P37012; 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; IMP:SGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0019388; P:galactose catabolic process; IMP:SGD.
DR   GO; GO:0019255; P:glucose 1-phosphate metabolic process; IMP:SGD.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IGI:SGD.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IGI:SGD.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:SGD.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IMP:SGD.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IGI:SGD.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IGI:SGD.
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   1: Evidence at protein level;
KW   Acetylation; Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW   Glucose metabolism; Glycoprotein; Isomerase; Magnesium; Metal-binding;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..569
FT                   /note="Phosphoglucomutase 2"
FT                   /id="PRO_0000147797"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        119
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         119
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
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="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         294
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         294
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         359
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         380
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         391
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         111
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         117
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CONFLICT        27
FT                   /note="T -> G (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="D -> G (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="S -> A (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   569 AA;  63089 MW;  45B78AFF8197645E CRC64;
     MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE GSKGATLVVG
     GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS HIMRTYEEKC TGGIILTASH
     NPGGPENDMG IKYNLSNGGP APESVTNAIW EISKKLTSYK IIKDFPELDL GTIGKNKKYG
     PLLVDIIDIT KDYVNFLKEI FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD
     EFGLPADEVL QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG
     YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH GLNCYEVPTG
     WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW LNILAIYNKH HPENEASIKT
     IQNEFWAKYG RTFFTRYDFE KVETEKANKI VDQLRAYVTK SGVVNSAFPA DESLKVTDCG
     DFSYTDLDGS VSDHQGLYVK LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE
     EYLKPIINSV IKFLNFKQVL GTEEPTVRT
//