ID PFKA2_YEAST Reviewed; 959 AA. AC P16862; D6W030; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 218. DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit beta {ECO:0000255|HAMAP-Rule:MF_03184}; DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184}; DE AltName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184}; DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184}; DE Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184}; DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184}; GN Name=PFK2; OrderedLocusNames=YMR205C; ORFNames=YM8325.06C; 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=2528496; DOI=10.1016/0378-1119(89)90233-3; RA Heinisch J.J., Ritzel R.G., von Borstel R.C., Aguilera A., Rodicio R., RA Zimmermann F.K.; RT "The phosphofructokinase genes of yeast evolved from two duplication RT events."; RL Gene 78:309-321(1989). RN [2] 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 [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 PROTEIN SEQUENCE OF 2-12; 181-185 AND 193-197. RX PubMed=8223596; DOI=10.1111/j.1432-1033.1993.tb18273.x; RA Kopperschlaeger G., Baer J., Stellwagen E.; RT "Limited proteolysis of yeast phosphofructokinase. Sequence locations of RT cleavage sites created by the actions of different proteinases."; RL Eur. J. Biochem. 217:527-533(1993). RN [5] RP SUBUNIT. RX PubMed=145942; DOI=10.1111/j.1432-1033.1977.tb11954.x; RA Kopperschlaeger G., Baer J., Nissler K., Hofmann E.; RT "Physicochemical parameters and subunit composition of yeast RT phosphofructokinase."; RL Eur. J. Biochem. 81:317-325(1977). RN [6] RP ACTIVITY REGULATION. RX PubMed=19473; DOI=10.1016/s0021-9258(17)39970-2; RA Banuelos M., Gancedo C., Gancedo J.M.; RT "Activation by phosphate of yeast phosphofructokinase."; RL J. Biol. Chem. 252:6394-6398(1977). RN [7] RP FUNCTION. RX PubMed=40590; DOI=10.1021/bi00588a006; RA Navon G., Shulman R.G., Yamane T., Eccleshall T.R., Lam K.B., RA Baronofsky J.J., Marmur J.; RT "Phosphorus-31 nuclear magnetic resonance studies of wild-type and RT glycolytic pathway mutants of Saccharomyces cerevisiae."; RL Biochemistry 18:4487-4499(1979). RN [8] RP ACTIVITY REGULATION. RX PubMed=6458303; DOI=10.1016/0006-291x(81)91635-1; RA Avigad G.; RT "Stimulation of yeast phosphofructokinase activity by fructose 2,6- RT bisphosphate."; RL Biochem. Biophys. Res. Commun. 102:985-991(1981). RN [9] RP FUNCTION. RX PubMed=6211191; DOI=10.1021/bi00537a037; RA Clifton D., Fraenkel D.G.; RT "Mutant studies of yeast phosphofructokinase."; RL Biochemistry 21:1935-1942(1982). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=6219673; DOI=10.1016/s0006-291x(83)80150-8; RA Nissler K., Otto A., Schellenberger W., Hofmann E.; RT "Similarity of activation of yeast phosphofructokinase by AMP and fructose- RT 2,6-bisphosphate."; RL Biochem. Biophys. Res. Commun. 111:294-300(1983). RN [11] RP FUNCTION. RX PubMed=3000145; DOI=10.1016/0065-2571(85)90055-x; RA Hofmann E., Eschrich K., Schellenberger W.; RT "Temporal organization of the phosphofructokinase/fructose-1,6- RT biphosphatase cycle."; RL Adv. Enzyme Regul. 23:331-362(1985). RN [12] RP SUBUNIT. RX PubMed=2408613; RA Nissler K., Hofmann E., Stel'maschchuk V., Orlova E., Kiselev N.; RT "An electron microscopy study of the quarternary structure of yeast RT phosphofructokinase."; RL Biomed. Biochim. Acta 44:251-259(1985). RN [13] RP FUNCTION. RX PubMed=3007939; DOI=10.1007/bf00330520; RA Heinisch J.; RT "Isolation and characterization of the two structural genes coding for RT phosphofructokinase in yeast."; RL Mol. Gen. Genet. 202:75-82(1986). RN [14] RP FUNCTION, AND MUTAGENESIS OF ASP-301; ASP-348; ARG-439 AND HIS-481. RX PubMed=8132627; DOI=10.1016/s0021-9258(17)37054-0; RA Arvanitidis A., Heinisch J.J.; RT "Studies on the function of yeast phosphofructokinase subunits by in vitro RT mutagenesis."; RL J. Biol. Chem. 269:8911-8918(1994). RN [15] RP FUNCTION, AND MUTAGENESIS OF SER-718 AND HIS-853. RX PubMed=8663166; DOI=10.1074/jbc.271.27.15928; RA Heinisch J.J., Boles E., Timpel C.; RT "A yeast phosphofructokinase insensitive to the Fructose 2,6-bisphosphate; RT allosteric activator. Glycolysis/metabolic regulation/allosteric control."; RL J. Biol. Chem. 271:15928-15933(1996). RN [16] RP FUNCTION, AND MUTAGENESIS OF PRO-722. RX PubMed=11221662; DOI=10.1074/jbc.m007131200; RA Rodicio R., Strauss A., Heinisch J.J.; RT "Single point mutations in either gene encoding the subunits of the RT heterooctameric yeast phosphofructokinase abolish allosteric inhibition by RT ATP."; RL J. Biol. Chem. 275:40952-40960(2000). RN [17] 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 [18] 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 [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, 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 [21] 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 [22] RP SUBCELLULAR LOCATION. RX PubMed=18313953; DOI=10.1016/j.fgb.2008.01.003; RA Barnard E., McFerran N.V., Trudgett A., Nelson J., Timson D.J.; RT "Detection and localisation of protein-protein interactions in RT Saccharomyces cerevisiae using a split-GFP method."; RL Fungal Genet. Biol. 45:597-604(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152; SER-163 AND SER-171, 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 [25] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959 IN COMPLEX WITH SUBSTRATE RP FRUCTOSE 6-PHOSPHATE AND FRUCTOSE 2,6-BISPHOSPHATE; ALLOSTERIC ACTIVATOR. RX PubMed=21241708; DOI=10.1016/j.jmb.2011.01.019; RA Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T., RA Radermacher M., Kopperschlager G., Rypniewski W.; RT "The crystal structures of eukaryotic phosphofructokinases from baker's RT yeast and rabbit skeletal muscle."; RL J. Mol. Biol. 407:284-297(2011). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to CC fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184, CC ECO:0000269|PubMed:11221662, ECO:0000269|PubMed:3000145, CC ECO:0000269|PubMed:3007939, ECO:0000269|PubMed:40590, CC ECO:0000269|PubMed:6211191, ECO:0000269|PubMed:6219673, CC ECO:0000269|PubMed:8132627, ECO:0000269|PubMed:8663166}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03184, ECO:0000269|PubMed:6219673}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03184}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. CC {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:19473, CC ECO:0000269|PubMed:6219673, ECO:0000269|PubMed:6458303}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.24 mM for ATP (without effector) {ECO:0000269|PubMed:6219673}; CC KM=0.3 mM for ATP (with 1 mM AMP) {ECO:0000269|PubMed:6219673}; CC KM=0.31 mM for ATP (with 20 uM fructose 2,6-bisphosphate) CC {ECO:0000269|PubMed:6219673}; CC KM=1.65 mM for fructose 6-phosphate (without effector) CC {ECO:0000269|PubMed:6219673}; CC KM=0.51 mM for fructose 6-phosphate (with 1 mM AMP) CC {ECO:0000269|PubMed:6219673}; CC KM=0.11 mM for fructose 6-phosphate (with 20 uM fructose CC 2,6-bisphosphate) {ECO:0000269|PubMed:6219673}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_03184}. CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains. CC {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:145942, CC ECO:0000269|PubMed:21241708, ECO:0000269|PubMed:2408613}. CC -!- INTERACTION: CC P16862; P16861: PFK1; NbExp=7; IntAct=EBI-9435, EBI-9428; CC P16862; P39940: RSP5; NbExp=3; IntAct=EBI-9435, EBI-16219; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184, CC ECO:0000269|PubMed:18313953}. Mitochondrion outer membrane; Peripheral CC membrane protein; Cytoplasmic side {ECO:0000269|PubMed:16962558}. CC -!- MISCELLANEOUS: Present with 90200 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}. 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; M26944; AAA34860.1; -; Genomic_DNA. DR EMBL; Z48755; CAA88646.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10104.1; -; Genomic_DNA. DR PIR; S59446; JQ0017. DR RefSeq; NP_013932.1; NM_001182712.1. DR PDB; 3O8O; X-ray; 2.90 A; B/D/F/H=194-959. DR PDBsum; 3O8O; -. DR AlphaFoldDB; P16862; -. DR SMR; P16862; -. DR BioGRID; 35383; 433. DR ComplexPortal; CPX-554; 6-phosphofructokinase complex. DR DIP; DIP-2619N; -. DR IntAct; P16862; 104. DR MINT; P16862; -. DR STRING; 4932.YMR205C; -. DR CarbonylDB; P16862; -. DR iPTMnet; P16862; -. DR MaxQB; P16862; -. DR PaxDb; 4932-YMR205C; -. DR PeptideAtlas; P16862; -. DR EnsemblFungi; YMR205C_mRNA; YMR205C; YMR205C. DR GeneID; 855245; -. DR KEGG; sce:YMR205C; -. DR AGR; SGD:S000004818; -. DR SGD; S000004818; PFK2. DR VEuPathDB; FungiDB:YMR205C; -. DR eggNOG; KOG2440; Eukaryota. DR GeneTree; ENSGT00940000171778; -. DR HOGENOM; CLU_011053_0_0_1; -. DR InParanoid; P16862; -. DR OMA; EWQDQMC; -. DR OrthoDB; 374214at2759; -. DR BioCyc; MetaCyc:YMR205C-MONOMER; -. DR BioCyc; YEAST:YMR205C-MONOMER; -. DR BRENDA; 2.7.1.11; 984. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR Reactome; R-SCE-70171; Glycolysis. DR SABIO-RK; P16862; -. DR UniPathway; UPA00109; UER00182. DR BioGRID-ORCS; 855245; 1 hit in 10 CRISPR screens. DR PRO; PR:P16862; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P16862; Protein. DR GO; GO:0005945; C:6-phosphofructokinase complex; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016208; F:AMP binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IDA:SGD. DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:ComplexPortal. DR GO; GO:0006096; P:glycolytic process; IDA:SGD. DR GO; GO:1902600; P:proton transmembrane transport; IGI:UniProtKB. DR GO; GO:0051453; P:regulation of intracellular pH; IMP:SGD. DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD. DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IMP:SGD. DR Gene3D; 3.40.50.450; -; 2. DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2. DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1. DR InterPro; IPR009161; 6-Pfructokinase_euk. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR NCBIfam; TIGR02478; 6PF1K_euk; 1. DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1. DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1. DR Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; ATP_PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1. DR SUPFAM; SSF53784; Phosphofructokinase; 2. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; KW Direct protein sequencing; Glycolysis; Kinase; Magnesium; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion outer membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8223596" FT CHAIN 2..959 FT /note="ATP-dependent 6-phosphofructokinase subunit beta" FT /id="PRO_0000112046" FT REGION 2..573 FT /note="N-terminal catalytic PFK domain 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000305|PubMed:21241708" FT REGION 144..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 574..587 FT /note="Interdomain linker" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000305|PubMed:21241708" FT REGION 588..959 FT /note="C-terminal regulatory PFK domain 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000305|PubMed:21241708" FT ACT_SITE 348 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 206 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 270..271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 300..303 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 301 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 346..348 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /ligand_label="2" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 383 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /ligand_label="1" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 390..392 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /ligand_label="2" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 447 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /ligand_label="2" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 475 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /ligand_label="1" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 481..484 FT /ligand="beta-D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57634" FT /ligand_label="2" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 658 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_label="2" FT /ligand_note="allosteric activator; ligand shared with FT subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 716..720 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_label="2" FT /ligand_note="allosteric activator; ligand shared with FT subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 754 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_label="1" FT /ligand_note="allosteric activator; ligand shared with FT subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 761..763 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_label="2" FT /ligand_note="allosteric activator; ligand shared with FT subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 847 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_label="1" FT /ligand_note="allosteric activator; ligand shared with FT subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 853..856 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_label="2" FT /ligand_note="allosteric activator; ligand shared with FT subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT BINDING 935 FT /ligand="beta-D-fructose 2,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58579" FT /ligand_label="2" FT /ligand_note="allosteric activator; ligand shared with FT subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184, FT ECO:0000269|PubMed:21241708" FT MOD_RES 152 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 163 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 803 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MUTAGEN 301 FT /note="D->T: Reduces maximal activity of the holoenzyme by FT 30%." FT /evidence="ECO:0000269|PubMed:8132627" FT MUTAGEN 348 FT /note="D->S: Reduces maximal activity of the holoenzyme by FT 50%. Completely abolishes catalytic activity; when FT associated with 'T-309' or 'S-356' in subunit alpha." FT /evidence="ECO:0000269|PubMed:8132627" FT MUTAGEN 439 FT /note="R->V: Reduces maximal activity of the holoenzyme by FT less than 25%." FT /evidence="ECO:0000269|PubMed:8132627" FT MUTAGEN 481 FT /note="H->S: Increases the KM for fructose 6-phosphate 50 FT fold." FT /evidence="ECO:0000269|PubMed:8132627" FT MUTAGEN 718 FT /note="S->D: Abolishes sensitivity of the holoenzyme to FT fructose 2,6-bisphosphate activation; when associated with FT 'D-724' in subunit alpha." FT /evidence="ECO:0000269|PubMed:8663166" FT MUTAGEN 722 FT /note="P->L: Drastically reduces sensitivity of the FT holoenzyme to ATP inhibition." FT /evidence="ECO:0000269|PubMed:11221662" FT MUTAGEN 853 FT /note="H->S: Reduces sensitivity of the holoenzyme to FT fructose 2,6-bisphosphate activation; when associated with FT 'S-859' in subunit alpha." FT /evidence="ECO:0000269|PubMed:8663166" FT CONFLICT 137 FT /note="V -> G (in Ref. 1; AAA34860)" FT /evidence="ECO:0000305" FT CONFLICT 880 FT /note="K -> E (in Ref. 1; AAA34860)" FT /evidence="ECO:0000305" FT STRAND 198..206 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 211..225 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 235..240 FT /evidence="ECO:0007829|PDB:3O8O" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 247..250 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 277..289 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 294..299 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 301..322 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 329..334 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 339..345 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 360..380 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 384..389 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 396..405 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 408..411 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 421..435 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 441..446 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 459..468 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 474..478 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 480..483 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 490..509 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 517..524 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 526..530 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 531..546 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 550..556 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 561..573 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 581..584 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 588..596 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 601..615 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 618..622 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 625..632 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 635..637 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 640..643 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 646..648 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 661..664 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 666..676 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 679..686 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 687..697 FT /evidence="ECO:0007829|PDB:3O8O" FT TURN 698..702 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 704..706 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 712..715 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 730..751 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 752..760 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 767..776 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 779..782 FT /evidence="ECO:0007829|PDB:3O8O" FT TURN 784..786 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 790..807 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 815..820 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 821..823 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 829..840 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 845..850 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 852..856 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 862..881 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 884..889 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 890..894 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 901..904 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 907..911 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 913..915 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 918..921 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 922..928 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 932..934 FT /evidence="ECO:0007829|PDB:3O8O" FT STRAND 935..939 FT /evidence="ECO:0007829|PDB:3O8O" FT HELIX 943..952 FT /evidence="ECO:0007829|PDB:3O8O" SQ SEQUENCE 959 AA; 104618 MW; 82CE6402CEDBBCB2 CRC64; MTVTTPFVNG TSYCTVTAYS VQSYKAAIDF YTKFLSLENR SSPDENSTLL SNDSISLKIL LRPDEKINKN VEAHLKELNS ITKTQDWRSH ATQSLVFNTS DILAVKDTLN AMNAPLQGYP TELFPMQLYT LDPLGNVVGV TSTKNAVSTK PTPPPAPEAS AESGLSSKVH SYTDLAYRMK TTDTYPSLPK PLNRPQKAIA VMTSGGDAPG MNSNVRAIVR SAIFKGCRAF VVMEGYEGLV RGGPEYIKEF HWEDVRGWSA EGGTNIGTAR CMEFKKREGR LLGAQHLIEA GVDALIVCGG DGSLTGADLF RSEWPSLIEE LLKTNRISNE QYERMKHLNI CGTVGSIDND MSTTDATIGA YSALDRICKA IDYVEATANS HSRAFVVEVM GRNCGWLALL AGIATSADYI FIPEKPATSS EWQDQMCDIV SKHRSRGKRT TIVVVAEGAI AADLTPISPS DVHKVLVDRL GLDTRITTLG HVQRGGTAVA YDRILATLQG LEAVNAVLES TPDTPSPLIA VNENKIVRKP LMESVKLTKA VAEAIQAKDF KRAMSLRDTE FIEHLNNFMA INSADHNEPK LPKDKRLKIA IVNVGAPAGG INSAVYSMAT YCMSQGHRPY AIYNGWSGLA RHESVRSLNW KDMLGWQSRG GSEIGTNRVT PEEADLGMIA YYFQKYEFDG LIIVGGFEAF ESLHQLERAR ESYPAFRIPM VLIPATLSNN VPGTEYSLGS DTALNALMEY CDVVKQSASS TRGRAFVVDC QGGNSGYLAT YASLAVGAQV SYVPEEGISL EQLSEDIEYL AQSFEKAEGR GRFGKLILKS TNASKALSAT KLAEVITAEA DGRFDAKPAY PGHVQQGGLP SPIDRTRATR MAIKAVGFIK DNQAAIAEAR AAEENFNADD KTISDTAAVV GVKGSHVVYN SIRQLYDYET EVSMRMPKVI HWQATRLIAD HLVGRKRVD //