F16P1_SHEEP
ID F16P1_SHEEP Reviewed; 337 AA.
AC P09199;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Fructose-1,6-bisphosphatase 1;
DE Short=FBPase 1;
DE EC=3.1.3.11 {ECO:0000250|UniProtKB:P19112};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1;
DE AltName: Full=Liver FBPase;
GN Name=FBP1; Synonyms=FBP;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE OF 2-337, ACETYLATION AT THR-2, AND PHOSPHORYLATION AT
RP SER-208.
RX PubMed=6316885; DOI=10.1071/bi9830235;
RA Fisher W.K., Thompson E.O.P.;
RT "Amino acid sequence studies on sheep liver fructose-bisphosphatase. II.
RT The complete sequence.";
RL Aust. J. Biol. Sci. 36:235-250(1983).
RN [2]
RP PROTEIN SEQUENCE OF 2-61, AND ACETYLATION AT THR-2.
RX PubMed=6264908; DOI=10.1071/bi9800665;
RA Fisher W.K., Thompson E.O.P.;
RT "Amino acid sequence studies on sheep liver fructose-bisphosphatase. I. The
RT S-peptide.";
RL Aust. J. Biol. Sci. 33:665-674(1980).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate in the presence of divalent cations, acting as a
CC rate-limiting enzyme in gluconeogenesis. Plays a role in regulating
CC glucose sensing and insulin secretion of pancreatic beta-cells. Appears
CC to modulate glycerol gluconeogenesis in liver. Important regulator of
CC appetite and adiposity; increased expression of the protein in liver
CC after nutrient excess increases circulating satiety hormones and
CC reduces appetite-stimulating neuropeptides and thus seems to provide a
CC feedback mechanism to limit weight gain.
CC {ECO:0000250|UniProtKB:P09467}.
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 Evidence={ECO:0000250|UniProtKB:P19112};
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. Fructose 2,6-bisphosphate acts as competitive
CC inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects
CC (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00636}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR PIR; A05318; A05318.
DR AlphaFoldDB; P09199; -.
DR SMR; P09199; -.
DR STRING; 9940.ENSOARP00000009283; -.
DR iPTMnet; P09199; -.
DR eggNOG; KOG1458; Eukaryota.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; ISS:UniProtKB.
DR GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
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 Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW Direct protein sequencing; Gluconeogenesis; Hydrolase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6264908,
FT ECO:0000269|PubMed:6316885"
FT CHAIN 2..337
FT /note="Fructose-1,6-bisphosphatase 1"
FT /id="PRO_0000200503"
FT BINDING 18..22
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 28..32
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 113..114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 122..125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 244..249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 275..277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:6264908,
FT ECO:0000269|PubMed:6316885"
FT MOD_RES 151
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD6"
FT MOD_RES 208
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:6316885"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD6"
FT MOD_RES 245
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD6"
FT MOD_RES 265
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09467"
SQ SEQUENCE 337 AA; 36675 MW; 4477539DA1AF9334 CRC64;
MTDEAPFDTN IVTVTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI
AGTTNVTGDQ VKKLDVLSND LVVNVLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP
LDGSSNIDCL VSIGTIFGIY KKISKDDPSE KDALQPGRNL VAAGYALYGS ATMLVLAMVN
GVNCFMLDPA IGEFILVDRD VKIKKKGSIY SLNEGYAKDF DPALTEYVQR KKFPPDNSAP
YGSRYVGSMV ADVHRTLVYG GIFMYPADKK SPSGKLRLLY ECDPMAYVIE KAGGMATTGK
EAVLDIVPTD IHQKVPIILG SPEDVTEFLE IKKYTAK
