PFKA2_YEAST
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 03-AUG-2022, entry version 212.
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;
CC Evidence={ECO:0000255|HAMAP-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 2,6-
CC 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; 418.
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; P16862; -.
DR PRIDE; P16862; -.
DR EnsemblFungi; YMR205C_mRNA; YMR205C; YMR205C.
DR GeneID; 855245; -.
DR KEGG; sce:YMR205C; -.
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; FEAYHST; -.
DR BioCyc; MetaCyc:YMR205C-MON; -.
DR BioCyc; YEAST:YMR205C-MON; -.
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 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; 3.10.180.10; -; 1.
DR Gene3D; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
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
