ID   F16P_YEAST              Reviewed;         348 AA.
AC   P09201; D6VZ13;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 201.
DE   RecName: Full=Fructose-1,6-bisphosphatase;
DE            Short=FBPase;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
GN   Name=FBP1; OrderedLocusNames=YLR377C; ORFNames=L8039.18;
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=2834361; DOI=10.1016/s0021-9258(18)68747-2;
RA   Rogers D.T., Hiller E., Mitsock L., Orr E.;
RT   "Characterization of the gene for fructose-1,6-bisphosphatase from
RT   Saccharomyces cerevisiae and Schizosaccharomyces pombe. Sequence, protein
RT   homology, and expression during growth on glucose.";
RL   J. Biol. Chem. 263:6051-6057(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2841162; DOI=10.1016/0014-5793(88)80313-2;
RA   Entian K.-D., Vogel R.F., Rose M., Hofmann L., Mecke D.;
RT   "Isolation and primary structure of the gene encoding fructose-1,6-
RT   bisphosphatase from Saccharomyces cerevisiae.";
RL   FEBS Lett. 236:195-200(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871; DOI=10.1038/387s087;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-16; 83-97; 256-280; 289-306 AND 327-346.
RX   PubMed=3008716; DOI=10.1016/0006-291x(86)90005-7;
RA   Marcus F., Gontero B., Harrsch P.B., Rittenhouse J.;
RT   "Amino acid sequence homology among fructose-1,6-bisphosphatases.";
RL   Biochem. Biophys. Res. Commun. 135:374-381(1986).
RN   [7]
RP   PROTEASOMAL DEGRADATION.
RX   PubMed=12686616; DOI=10.1091/mbc.e02-08-0456;
RA   Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D.,
RA   Thumm M., Wolf D.H.;
RT   "Catabolite degradation of fructose-1,6-bisphosphatase in the yeast
RT   Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID
RT   genes and indicates the existence of two degradation pathways.";
RL   Mol. Biol. Cell 14:1652-1663(2003).
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   PROTEASOMAL DEGRADATION.
RX   PubMed=18508925; DOI=10.1091/mbc.e08-03-0328;
RA   Santt O., Pfirrmann T., Braun B., Juretschke J., Kimmig P., Scheel H.,
RA   Hofmann K., Thumm M., Wolf D.H.;
RT   "The yeast GID complex, a novel ubiquitin ligase (E3) involved in the
RT   regulation of carbohydrate metabolism.";
RL   Mol. Biol. Cell 19:3323-3333(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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).
RN   [11]
RP   UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
RX   PubMed=22645139; DOI=10.1074/jbc.m112.363762;
RA   Menssen R., Schweiggert J., Schreiner J., Kusevic D., Reuther J., Braun B.,
RA   Wolf D.H.;
RT   "Exploring the topology of the Gid complex, the E3 ubiquitin ligase
RT   involved in catabolite-induced degradation of gluconeogenic enzymes.";
RL   J. Biol. Chem. 287:25602-25614(2012).
RN   [12]
RP   DOMAIN, PROTEASOMAL DEGRADATION, AND MUTAGENESIS OF PRO-2.
RX   PubMed=28126757; DOI=10.1126/science.aal3655;
RA   Chen S.J., Wu X., Wadas B., Oh J.H., Varshavsky A.;
RT   "An N-end rule pathway that recognizes proline and destroys gluconeogenic
RT   enzymes.";
RL   Science 355:0-0(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P00636};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P00636};
CC   -!- ACTIVITY REGULATION: Subject to complex allosteric regulation. The
CC       enzyme can assume an active R-state, or an inactive T-state.
CC       Intermediate conformations may exist. AMP acts as allosteric inhibitor.
CC       AMP binding affects the turnover of bound substrate and not the
CC       affinity for substrate (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00636}.
CC   -!- DOMAIN: The Pro/N-degron targets the protein for proteasomal
CC       degradation when cells are shifted to glucose-containing growth medium.
CC       {ECO:0000269|PubMed:28126757}.
CC   -!- PTM: Ubiquitinated (PubMed:22645139). Targeted for proteasomal
CC       degradation when cells are shifted to glucose-containing growth medium
CC       (PubMed:12686616, PubMed:18508925, PubMed:22645139, PubMed:28126757).
CC       {ECO:0000269|PubMed:12686616, ECO:0000269|PubMed:18508925,
CC       ECO:0000269|PubMed:22645139, ECO:0000269|PubMed:28126757}.
CC   -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR   EMBL; Y00754; CAA68723.1; -; Genomic_DNA.
DR   EMBL; J03207; AAA34603.1; -; Genomic_DNA.
DR   EMBL; U19103; AAB67579.1; -; Genomic_DNA.
DR   EMBL; AY692816; AAT92835.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09679.1; -; Genomic_DNA.
DR   PIR; S01127; PABY.
DR   RefSeq; NP_013481.3; NM_001182266.3.
DR   PDB; 7NS5; X-ray; 1.95 A; A/B/C/D=1-348.
DR   AlphaFoldDB; P09201; -.
DR   SMR; P09201; -.
DR   BioGRID; 31636; 98.
DR   DIP; DIP-3986N; -.
DR   FunCoup; P09201; 772.
DR   IntAct; P09201; 4.
DR   MINT; P09201; -.
DR   STRING; 4932.YLR377C; -.
DR   iPTMnet; P09201; -.
DR   PaxDb; 4932-YLR377C; -.
DR   PeptideAtlas; P09201; -.
DR   EnsemblFungi; YLR377C_mRNA; YLR377C; YLR377C.
DR   GeneID; 851092; -.
DR   KEGG; sce:YLR377C; -.
DR   AGR; SGD:S000004369; -.
DR   SGD; S000004369; FBP1.
DR   VEuPathDB; FungiDB:YLR377C; -.
DR   eggNOG; KOG1458; Eukaryota.
DR   HOGENOM; CLU_039977_1_0_1; -.
DR   InParanoid; P09201; -.
DR   OMA; YIPENCP; -.
DR   OrthoDB; 10256725at2759; -.
DR   BioCyc; YEAST:YLR377C-MONOMER; -.
DR   BRENDA; 3.1.3.11; 984.
DR   Reactome; R-SCE-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   BioGRID-ORCS; 851092; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P09201; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P09201; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0042597; C:periplasmic space; IDA:SGD.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:SGD.
DR   GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:SGD.
DR   CDD; cd00354; FBPase; 1.
DR   FunFam; 3.30.540.10:FF:000009; Fructose-1,6-bisphosphatase; 1.
DR   FunFam; 3.40.190.80:FF:000001; Fructose-1,6-bisphosphatase class 1; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   HAMAP; MF_01855; FBPase_class1; 1.
DR   InterPro; IPR044015; FBPase_C_dom.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR   NCBIfam; NF006778; PRK09293.1-1; 1.
DR   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11556:SF1; FRUCTOSE-BISPHOSPHATASE; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   Pfam; PF18913; FBPase_C; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00124; FBPASE; 1.
DR   PDBsum; 7NS5; -.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Carbohydrate metabolism;
KW   Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3008716"
FT   CHAIN           2..348
FT                   /note="Fructose-1,6-bisphosphatase"
FT                   /id="PRO_0000200511"
FT   MOTIF           2..5
FT                   /note="Pro/N-degron"
FT                   /evidence="ECO:0000269|PubMed:28126757"
FT   BINDING         27..31
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         38..42
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         122..123
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         131..134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         150
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         222..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         255..260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         286..288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P00636"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         2
FT                   /note="P->S: Loss of proteasomal degradation in response to
FT                   shift to glucose-containing growth medium."
FT                   /evidence="ECO:0000269|PubMed:28126757"
FT   CONFLICT        278
FT                   /note="C -> D (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           23..31
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           40..61
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           84..98
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          123..131
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           133..138
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          142..150
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          170..189
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          192..197
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   TURN            198..201
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           223..228
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           231..240
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           260..270
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          273..276
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          286..288
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           289..293
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           294..302
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   STRAND          329..332
FT                   /evidence="ECO:0007829|PDB:7NS5"
FT   HELIX           334..347
FT                   /evidence="ECO:0007829|PDB:7NS5"
SQ   SEQUENCE   348 AA;  38263 MW;  BCFC0984A086094B CRC64;
     MPTLVNGPRR DSTEGFDTDI ITLPRFIIEH QKQFKNATGD FTLVLNALQF AFKFVSHTIR
     RAELVNLVGL AGASNFTGDQ QKKLDVLGDE IFINAMRASG IIKVLVSEEQ EDLIVFPTNT
     GSYAVCCDPI DGSSNLDAGV SVGTIASIFR LLPDSSGTIN DVLRCGKEMV AACYAMYGSS
     THLVLTLGDG VDGFTLDTNL GEFILTHPNL RIPPQKAIYS INEGNTLYWN ETIRTFIEKV
     KQPQADNNNK PFSARYVGSM VADVHRTFLY GGLFAYPCDK KSPNGKLRLL YEAFPMAFLM
     EQAGGKAVND RGERILDLVP SHIHDKSSIW LGSSGEIDKF LDHIGKSQ
//