F26_YEAST
ID F26_YEAST Reviewed; 452 AA.
AC P32604; D6VW32;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Fructose-2,6-bisphosphatase {ECO:0000305};
DE Short=FBPase 2 {ECO:0000303|PubMed:2831055};
DE EC=3.1.3.46 {ECO:0000305|PubMed:1322693, ECO:0000305|PubMed:2825652, ECO:0000305|PubMed:2831055};
GN Name=FBP26 {ECO:0000303|PubMed:1322693}; OrderedLocusNames=YJL155C;
GN ORFNames=J0575;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1322693; DOI=10.1021/bi00146a014;
RA Paravicini G., Kretschmer M.;
RT "The yeast FBP26 gene codes for a fructose-2,6-bisphosphatase.";
RL Biochemistry 31:7126-7133(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=2825652; DOI=10.1042/bj2460755;
RA Kretschmer M., Schellenberger W., Otto A., Kessler R., Hofmann E.;
RT "Fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase are separable in
RT yeast.";
RL Biochem. J. 246:755-759(1987).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=2831055; DOI=10.1111/j.1432-1033.1988.tb13830.x;
RA Francois J., Van Schaftigen E., Hers H.G.;
RT "Characterization of phosphofructokinase 2 and of enzymes involved in the
RT degradation of fructose 2,6-bisphosphate in yeast.";
RL Eur. J. Biochem. 171:599-608(1988).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-446, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Monofunctional, high-specificity fructose-2,6-bisphosphatase,
CC which releases phosphate from the 2-position of fructose 2,6-
CC bisphosphate. Has no detectable 6-phosphofructo-2-kinase activity.
CC {ECO:0000269|PubMed:1322693, ECO:0000305|PubMed:2825652,
CC ECO:0000305|PubMed:2831055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46;
CC Evidence={ECO:0000305|PubMed:1322693, ECO:0000305|PubMed:2825652,
CC ECO:0000305|PubMed:2831055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290;
CC Evidence={ECO:0000305|PubMed:1322693, ECO:0000305|PubMed:2825652,
CC ECO:0000305|PubMed:2831055};
CC -!- ACTIVITY REGULATION: Inhibited by fructose 6-P, activated by glycerol
CC 3-P. {ECO:0000305|PubMed:2825652, ECO:0000305|PubMed:2831055}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 uM for fructose 2,6-bisphosphate {ECO:0000305|PubMed:2825652};
CC KM=0.1 uM for fructose 2,6-bisphosphate {ECO:0000305|PubMed:2831055};
CC -!- INTERACTION:
CC P32604; Q06137: YLR345W; NbExp=3; IntAct=EBI-6749, EBI-33827;
CC -!- MISCELLANEOUS: Present with 1680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000305}.
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DR EMBL; S42124; AAB22823.1; -; Genomic_DNA.
DR EMBL; Z49430; CAA89450.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08648.1; -; Genomic_DNA.
DR PIR; S56938; S56938.
DR RefSeq; NP_012380.1; NM_001181588.1.
DR AlphaFoldDB; P32604; -.
DR SMR; P32604; -.
DR BioGRID; 33605; 85.
DR DIP; DIP-2593N; -.
DR IntAct; P32604; 6.
DR MINT; P32604; -.
DR STRING; 4932.YJL155C; -.
DR iPTMnet; P32604; -.
DR MaxQB; P32604; -.
DR PaxDb; P32604; -.
DR PRIDE; P32604; -.
DR EnsemblFungi; YJL155C_mRNA; YJL155C; YJL155C.
DR GeneID; 853286; -.
DR KEGG; sce:YJL155C; -.
DR SGD; S000003691; FBP26.
DR VEuPathDB; FungiDB:YJL155C; -.
DR eggNOG; KOG0234; Eukaryota.
DR GeneTree; ENSGT00950000182835; -.
DR HOGENOM; CLU_006383_1_0_1; -.
DR InParanoid; P32604; -.
DR OMA; AEDTRIC; -.
DR BioCyc; YEAST:YJL155C-MON; -.
DR Reactome; R-SCE-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR PRO; PR:P32604; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32604; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IMP:SGD.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IMP:SGD.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR10606; PTHR10606; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..452
FT /note="Fructose-2,6-bisphosphatase"
FT /id="PRO_0000179975"
FT REGION 1..223
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000250"
FT REGION 224..452
FT /note="Fructose-2,6-bisphosphatase"
FT ACT_SITE 104
FT /evidence="ECO:0000255"
FT ACT_SITE 232
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT ACT_SITE 302
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 53
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 78
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 106
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 112
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 143..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 169
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 173
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 231
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 238
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 244
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 313
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 324..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 327
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 331
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 342
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 368..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 368
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 372
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 231
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 238
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 367
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 199
FT /note="E -> Q (in Ref. 1; AAB22823)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="V -> E (in Ref. 1; AAB22823)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..449
FT /note="LE -> FQ (in Ref. 1; AAB22823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 52595 MW; 228766A302F32F82 CRC64;
MGYSTISNDN DIKVCVIMVG LPARGKSFIS QKIIRYLSWL SIKAKCFNVG NYRRDVSGNV
PMDAEFFNFE NTDNFKLREL AAQNAIKDIV NFFTKEDGSV AVFDATNSTR KRRKWLKDIC
EKNNIQPMFL ESWSNDHELI INNAKDIGST SPDYENSEPH VAEADFLERI RQYERFYEPL
DPQKDKDMTF IKLVNIIEEV VINKIRTYLE SRIVFYVMNI RPKPKYIWLS RHGESIYNVE
KKIGGDSSLS ERGFQYAKKL EQLVKESAGE INLTVWTSTL KRTQQTANYL PYKKLQWKAL
DELDAGVCDG MTYEEIEKEY PEDFKARDND KYEYRYRGGE SYRDVVIRLE PVIMELERQE
NVLIITHQAV LRCIYAYFMN VPQEESPWMS IPLHTLIKLE PRAYGTKVTK IKANIPAVST
YKEKGTSQVG ELSQSSTKLH QLLNDSPLED KF
