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Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase)

 F16P1_SHEEP             Reviewed;         337 AA.
P09199;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
15-MAR-2017, entry version 108.
RecName: Full=Fructose-1,6-bisphosphatase 1;
Short=FBPase 1;
EC=3.1.3.11;
AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1;
AltName: Full=Liver FBPase;
Name=FBP1; Synonyms=FBP;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
PROTEIN SEQUENCE OF 2-337, ACETYLATION AT THR-2, AND PHOSPHORYLATION
AT SER-208.
PubMed=6316885; DOI=10.1071/BI9830235;
Fisher W.K., Thompson E.O.P.;
"Amino acid sequence studies on sheep liver fructose-bisphosphatase.
II. The complete sequence.";
Aust. J. Biol. Sci. 36:235-250(1983).
[2]
PROTEIN SEQUENCE OF 2-61, AND ACETYLATION AT THR-2.
PubMed=6264908; DOI=10.1071/BI9800665;
Fisher W.K., Thompson E.O.P.;
"Amino acid sequence studies on sheep liver fructose-bisphosphatase.
I. The S-peptide.";
Aust. J. Biol. Sci. 33:665-674(1980).
-!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
fructose 6-phosphate in the presence of divalent cations, acting
as a rate-limiting enzyme in gluconeogenesis. Plays a role in
regulating glucose sensing and insulin secretion of pancreatic
beta-cells. Appears to modulate glycerol gluconeogenesis in liver.
Important regulator of appetite and adiposity; increased
expression of the protein in liver after nutrient excess increases
circulating satiety hormones and reduces appetite-stimulating
neuropeptides and thus seems to provide a feedback mechanism to
limit weight gain (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
fructose 6-phosphate + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Subject to complex allosteric regulation. The
enzyme can assume an active R-state, or an inactive T-state.
Intermediate conformations may exist. AMP acts as allosteric
inhibitor. AMP binding affects the turnover of bound substrate and
not the affinity for substrate. Fructose 2,6-bisphosphate acts as
competitive inhibitor. Fructose 2,6-bisphosphate and AMP have
synergistic effects (By similarity). {ECO:0000250}.
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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PIR; A05318; A05318.
ProteinModelPortal; P09199; -.
SMR; P09199; -.
iPTMnet; P09199; -.
PRIDE; P09199; -.
HOVERGEN; HBG005627; -.
UniPathway; UPA00138; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
GO; GO:0048029; F:monosaccharide binding; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
CDD; cd00354; FBPase; 1.
HAMAP; MF_01855; FBPase_class1; 1.
InterPro; IPR000146; FBPase_class-1.
InterPro; IPR033391; FBPase_N.
InterPro; IPR028343; FBPtase.
InterPro; IPR020548; Fructose_bisphosphatase_AS.
PANTHER; PTHR11556; PTHR11556; 1.
Pfam; PF00316; FBPase; 1.
PIRSF; PIRSF500210; FBPtase; 1.
PIRSF; PIRSF000904; FBPtase_SBPase; 1.
PRINTS; PR00115; F16BPHPHTASE.
PROSITE; PS00124; FBPASE; 1.
1: Evidence at protein level;
Acetylation; Allosteric enzyme; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Gluconeogenesis;
Hydrolase; Magnesium; Metal-binding; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6264908,
ECO:0000269|PubMed:6316885}.
CHAIN 2 337 Fructose-1,6-bisphosphatase 1.
/FTId=PRO_0000200503.
NP_BIND 18 22 AMP. {ECO:0000250}.
NP_BIND 28 32 AMP. {ECO:0000250}.
NP_BIND 113 114 AMP. {ECO:0000250}.
REGION 122 125 Substrate binding. {ECO:0000250}.
REGION 213 216 Substrate binding. {ECO:0000250}.
REGION 244 249 Substrate binding. {ECO:0000250}.
REGION 275 277 Substrate binding. {ECO:0000250}.
METAL 69 69 Magnesium 1. {ECO:0000250}.
METAL 98 98 Magnesium 1. {ECO:0000250}.
METAL 98 98 Magnesium 2. {ECO:0000250}.
METAL 119 119 Magnesium 2. {ECO:0000250}.
METAL 119 119 Magnesium 3. {ECO:0000250}.
METAL 121 121 Magnesium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 122 122 Magnesium 3. {ECO:0000250}.
METAL 281 281 Magnesium 3. {ECO:0000250}.
BINDING 141 141 AMP. {ECO:0000250}.
BINDING 265 265 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000269|PubMed:6264908,
ECO:0000269|PubMed:6316885}.
MOD_RES 151 151 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 208 208 Phosphoserine; by PKA.
{ECO:0000269|PubMed:6316885}.
MOD_RES 216 216 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 245 245 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 265 265 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09467}.
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


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