F16P_YEAST
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 03-AUG-2022, entry version 187.
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;
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 PDBsum; 7NS5; -.
DR AlphaFoldDB; P09201; -.
DR SMR; P09201; -.
DR BioGRID; 31636; 95.
DR DIP; DIP-3986N; -.
DR IntAct; P09201; 4.
DR MINT; P09201; -.
DR STRING; 4932.YLR377C; -.
DR iPTMnet; P09201; -.
DR PaxDb; P09201; -.
DR PRIDE; P09201; -.
DR EnsemblFungi; YLR377C_mRNA; YLR377C; YLR377C.
DR GeneID; 851092; -.
DR KEGG; sce:YLR377C; -.
DR SGD; S000004369; FBP1.
DR VEuPathDB; FungiDB:YLR377C; -.
DR eggNOG; KOG1458; Eukaryota.
DR GeneTree; ENSGT00390000015513; -.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; P09201; -.
DR OMA; YIPENCP; -.
DR BioCyc; YEAST:YLR377C-MON; -.
DR BRENDA; 3.1.3.11; 984.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR PRO; PR:P09201; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P09201; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:SGD.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 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 PANTHER; PTHR11556; PTHR11556; 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 PROSITE; PS00124; FBPASE; 1.
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 TURN 289..292
FT /evidence="ECO:0007829|PDB:7NS5"
FT HELIX 293..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
