ID   KPYK1_YEAST             Reviewed;         500 AA.
AC   P00549; D6VPH8; Q2VQG5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   27-MAR-2024, entry version 228.
DE   RecName: Full=Pyruvate kinase 1;
DE            Short=PK 1;
DE            EC=2.7.1.40 {ECO:0000269|PubMed:10413488};
DE   AltName: Full=cell division cycle protein 19;
GN   Name=CDC19; Synonyms=PYK1; OrderedLocusNames=YAL038W;
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=2653861; DOI=10.1016/0014-5793(89)81359-6;
RA   McNally T., Purvis I.J., Fothergill-Gilmore L.A., Brown A.L.P.;
RT   "The yeast pyruvate kinase gene does not contain a string of non-preferred
RT   codons: revised nucleotide sequence.";
RL   FEBS Lett. 247:312-316(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6185493; DOI=10.1016/s0021-9258(18)32907-7;
RA   Burke R.L., Tekamp-Olson P., Najarian R.;
RT   "The isolation, characterization, and sequence of the pyruvate kinase gene
RT   of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 258:2193-2201(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 76625 / YPH499, Ba194, Bb32, Fy93, M1-2A, M2-8, M5-7A,
RC   M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15, MMW1-15h2,
RC   MMW1-2, MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, YPS396, YPS400, YPS598,
RC   YPS600, YPS602, YPS604, YPS606, YPS608, and YPS610;
RX   PubMed=16879422; DOI=10.1111/j.1567-1364.2006.00059.x;
RA   Aa E., Townsend J.P., Adams R.I., Nielsen K.M., Taylor J.W.;
RT   "Population structure and gene evolution in Saccharomyces cerevisiae.";
RL   FEMS Yeast Res. 6:702-715(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [5]
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   [6]
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   [7]
RP   CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF LYS-240.
RX   PubMed=10413488; DOI=10.1021/bi990690n;
RA   Bollenbach T.J., Mesecar A.D., Nowak T.;
RT   "Role of lysine 240 in the mechanism of yeast pyruvate kinase catalysis.";
RL   Biochemistry 38:9137-9145(1999).
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-478, AND
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-213, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-16; THR-31; SER-70;
RP   THR-184; SER-316; SER-450 AND THR-478, AND IDENTIFICATION BY MASS
RP   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   [14]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-204; LYS-255 AND LYS-446, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [15]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG;
RP   FRUCTOSE-1-6-DIPHOSPHATE; MANGANESE IONS AND POTASSIUM IONS.
RX   PubMed=9519410; DOI=10.1016/s0969-2126(98)00021-5;
RA   Jurica M.S., Mesecar A., Heath P.J., Shi W., Nowak T., Stoddard B.L.;
RT   "The allosteric regulation of pyruvate kinase by fructose-1,6-
RT   bisphosphate.";
RL   Structure 6:195-210(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=2.7.1.40; Evidence={ECO:0000269|PubMed:10413488};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10413488};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000305|PubMed:9519410};
CC   -!- ACTIVITY REGULATION: The activity is regulated by glucose levels.
CC       Activated by fructose-1,6-bisphosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.31 mM for phosphoenolpyruvate (with magnesium as divalent
CC         cation) {ECO:0000269|PubMed:10413488};
CC         KM=0.021 mM for phosphoenolpyruvate (with manganese as divalent
CC         cation) {ECO:0000269|PubMed:10413488};
CC         KM=1.1 mM for ADP (with magnesium as divalent cation)
CC         {ECO:0000269|PubMed:10413488};
CC         KM=0.24 mM for ADP (with manganese as divalent cation)
CC         {ECO:0000269|PubMed:10413488};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:10413488};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: Present with 291000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; V01321; CAA24631.1; -; Genomic_DNA.
DR   EMBL; X14400; CAA32573.1; -; Genomic_DNA.
DR   EMBL; AY949862; AAY27264.1; -; Genomic_DNA.
DR   EMBL; AY949863; AAY27265.1; -; Genomic_DNA.
DR   EMBL; AY949864; AAY27266.1; -; Genomic_DNA.
DR   EMBL; AY949865; AAY27267.1; -; Genomic_DNA.
DR   EMBL; AY949866; AAY27268.1; -; Genomic_DNA.
DR   EMBL; AY949867; AAY27269.1; -; Genomic_DNA.
DR   EMBL; AY949868; AAY27270.1; -; Genomic_DNA.
DR   EMBL; AY949869; AAY27271.1; -; Genomic_DNA.
DR   EMBL; AY949870; AAY27272.1; -; Genomic_DNA.
DR   EMBL; AY949871; AAY27273.1; -; Genomic_DNA.
DR   EMBL; AY949872; AAY27274.1; -; Genomic_DNA.
DR   EMBL; AY949873; AAY27275.1; -; Genomic_DNA.
DR   EMBL; AY949874; AAY27276.1; -; Genomic_DNA.
DR   EMBL; AY949875; AAY27277.1; -; Genomic_DNA.
DR   EMBL; AY949876; AAY27278.1; -; Genomic_DNA.
DR   EMBL; AY949877; AAY27279.1; -; Genomic_DNA.
DR   EMBL; AY949878; AAY27280.1; -; Genomic_DNA.
DR   EMBL; AY949879; AAY27281.1; -; Genomic_DNA.
DR   EMBL; AY949880; AAY27282.1; -; Genomic_DNA.
DR   EMBL; AY949881; AAY27283.1; -; Genomic_DNA.
DR   EMBL; AY949882; AAY27284.1; -; Genomic_DNA.
DR   EMBL; AY949883; AAY27285.1; -; Genomic_DNA.
DR   EMBL; AY949884; AAY27286.1; -; Genomic_DNA.
DR   EMBL; AY949885; AAY27287.1; -; Genomic_DNA.
DR   EMBL; AY949886; AAY27288.1; -; Genomic_DNA.
DR   EMBL; AY949887; AAY27289.1; -; Genomic_DNA.
DR   EMBL; AY949888; AAY27290.1; -; Genomic_DNA.
DR   EMBL; AY949889; AAY27291.1; -; Genomic_DNA.
DR   EMBL; AY949890; AAY27292.1; -; Genomic_DNA.
DR   EMBL; U12980; AAC04993.1; -; Genomic_DNA.
DR   EMBL; AY693107; AAT93126.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06948.1; -; Genomic_DNA.
DR   PIR; S05764; KIBYP.
DR   RefSeq; NP_009362.1; NM_001178183.1.
DR   PDB; 1A3W; X-ray; 3.00 A; A/B=1-500.
DR   PDB; 1A3X; X-ray; 3.00 A; A/B=1-500.
DR   PDBsum; 1A3W; -.
DR   PDBsum; 1A3X; -.
DR   AlphaFoldDB; P00549; -.
DR   SMR; P00549; -.
DR   BioGRID; 31727; 379.
DR   DIP; DIP-4124N; -.
DR   ELM; P00549; -.
DR   IntAct; P00549; 186.
DR   MINT; P00549; -.
DR   STRING; 4932.YAL038W; -.
DR   MoonProt; P00549; -.
DR   CarbonylDB; P00549; -.
DR   iPTMnet; P00549; -.
DR   MaxQB; P00549; -.
DR   PaxDb; 4932-YAL038W; -.
DR   PeptideAtlas; P00549; -.
DR   TopDownProteomics; P00549; -.
DR   EnsemblFungi; YAL038W_mRNA; YAL038W; YAL038W.
DR   GeneID; 851193; -.
DR   KEGG; sce:YAL038W; -.
DR   AGR; SGD:S000000036; -.
DR   SGD; S000000036; CDC19.
DR   VEuPathDB; FungiDB:YAL038W; -.
DR   eggNOG; KOG2323; Eukaryota.
DR   GeneTree; ENSGT00390000008859; -.
DR   HOGENOM; CLU_015439_0_1_1; -.
DR   InParanoid; P00549; -.
DR   OMA; RVHHIGE; -.
DR   OrthoDB; 312683at2759; -.
DR   BioCyc; YEAST:YAL038W-MONOMER; -.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-70171; Glycolysis.
DR   SABIO-RK; P00549; -.
DR   UniPathway; UPA00109; UER00188.
DR   BioGRID-ORCS; 851193; 7 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P00549; -.
DR   PRO; PR:P00549; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P00549; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IDA:SGD.
DR   GO; GO:0006096; P:glycolytic process; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IMP:SGD.
DR   CDD; cd00288; Pyruvate_Kinase; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
DR   COMPLUYEAST-2DPAGE; P00549; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Glycolysis;
KW   Isopeptide bond; Kinase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate;
KW   Reference proteome; Transferase; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   CHAIN           2..500
FT                   /note="Pyruvate kinase 1"
FT                   /id="PRO_0000112121"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3X"
FT   BINDING         51..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         51
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         53
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         84
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         85
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3X"
FT   BINDING         242
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         266
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         402..407
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W"
FT   BINDING         452
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         459
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   BINDING         484
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:9519410,
FT                   ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT   SITE            240
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000269|PubMed:10413488"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         31
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         184
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         478
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   CROSSLNK        204
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        255
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        446
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   MUTAGEN         240
FT                   /note="K->M: Reduces activity 1000-fold."
FT                   /evidence="ECO:0000269|PubMed:10413488"
FT   CONFLICT        382..386
FT                   /note="VAASA -> SLPR (in Ref. 1; CAA24631)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..8
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:1A3X"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           34..43
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           57..73
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          82..84
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   TURN            116..120
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           133..136
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   TURN            146..149
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:1A3X"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           193..205
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           218..232
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          235..241
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           245..248
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           250..256
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           264..270
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           276..290
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           302..305
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           312..324
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   TURN            333..337
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           341..355
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          357..359
FT                   /evidence="ECO:0007829|PDB:1A3X"
FT   HELIX           361..368
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           378..393
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          398..401
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          403..405
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           406..413
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          420..425
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           429..432
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           433..435
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          439..443
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   TURN            452..454
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   HELIX           455..469
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          478..483
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   TURN            487..489
FT                   /evidence="ECO:0007829|PDB:1A3W"
FT   STRAND          494..499
FT                   /evidence="ECO:0007829|PDB:1A3W"
SQ   SEQUENCE   500 AA;  54545 MW;  78D753FC410C5820 CRC64;
     MSRLERLTSL NVVAGSDLRR TSIIGTIGPK TNNPETLVAL RKAGLNIVRM NFSHGSYEYH
     KSVIDNARKS EELYPGRPLA IALDTKGPEI RTGTTTNDVD YPIPPNHEMI FTTDDKYAKA
     CDDKIMYVDY KNITKVISAG RIIYVDDGVL SFQVLEVVDD KTLKVKALNA GKICSHKGVN
     LPGTDVDLPA LSEKDKEDLR FGVKNGVHMV FASFIRTAND VLTIREVLGE QGKDVKIIVK
     IENQQGVNNF DEILKVTDGV MVARGDLGIE IPAPEVLAVQ KKLIAKSNLA GKPVICATQM
     LESMTYNPRP TRAEVSDVGN AILDGADCVM LSGETAKGNY PINAVTTMAE TAVIAEQAIA
     YLPNYDDMRN CTPKPTSTTE TVAASAVAAV FEQKAKAIIV LSTSGTTPRL VSKYRPNCPI
     ILVTRCPRAA RFSHLYRGVF PFVFEKEPVS DWTDDVEARI NFGIEKAKEF GILKKGDTYV
     SIQGFKAGAG HSNTLQVSTV
//