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Protein

Fructose-1,6-bisphosphatase 1

Gene

Fbp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Enzyme regulationi

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.1 Publication

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Magnesium 1By similarity
Metal bindingi98 – 981Magnesium 1By similarity
Metal bindingi98 – 981Magnesium 2By similarity
Metal bindingi119 – 1191Magnesium 2By similarity
Metal bindingi119 – 1191Magnesium 3By similarity
Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygenBy similarity
Metal bindingi122 – 1221Magnesium 3By similarity
Binding sitei141 – 1411AMPBy similarity
Binding sitei265 – 2651SubstrateBy similarity
Metal bindingi281 – 2811Magnesium 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 225AMPBy similarity
Nucleotide bindingi28 – 325AMPBy similarity
Nucleotide bindingi113 – 1142AMPBy similarity

GO - Molecular functioni

  • AMP binding Source: UniProtKB
  • fructose 1,6-bisphosphate 1-phosphatase activity Source: RGD
  • metal ion binding Source: UniProtKB
  • monosaccharide binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKP19112.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
Short name:
FBPase 1
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Liver FBPase
Gene namesi
Name:Fbp1
Synonyms:Fbp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2595. Fbp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi275 – 2751K → A: Reduces affinity for substrate 20-fold, and decreases affinity for the competitive inhibitor fructose 2,6-bisphosphate 500-fold. 1 Publication

Chemistry

ChEMBLiCHEMBL4391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 363362Fructose-1,6-bisphosphatase 1PRO_0000200502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylvaline1 Publication
Modified residuei151 – 1511N6-succinyllysineBy similarity
Modified residuei216 – 2161PhosphotyrosineCombined sources
Modified residuei245 – 2451PhosphotyrosineBy similarity
Modified residuei265 – 2651PhosphotyrosineBy similarity
Modified residuei339 – 3391PhosphoserineCombined sources
Modified residuei353 – 3531PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP19112.

PTM databases

iPTMnetiP19112.
PhosphoSiteiP19112.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

MINTiMINT-4565506.

Chemistry

BindingDBiP19112.

Structurei

3D structure databases

ProteinModelPortaliP19112.
SMRiP19112. Positions 7-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1254Substrate bindingBy similarity
Regioni213 – 2164Substrate bindingBy similarity
Regioni244 – 2496Substrate bindingBy similarity
Regioni275 – 2773Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP19112.
KOiK03841.
PhylomeDBiP19112.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDHAPFETD ISTLTRFVLE EGRKAGGTGE MTQLLNSLCT AIKAISSAVR
60 70 80 90 100
QAGIAQLYGI AGSTNVTGDQ VKKLDILSND LVINMLKSSY ATCVLVSEED
110 120 130 140 150
THAIIIEPEK RGKYVVCFDP LDGSSNIDCL ASIGTIFGIY RKTSANEPSE
160 170 180 190 200
KDALQPGRNL VAAGYALYGS ATMLVLAMNC GVNCFMLDPS IGEFILVDRD
210 220 230 240 250
VKIKKKGNIY SINEGYAKDF DPAINEYIQR KKFPPDNSAP YGARYVGSMV
260 270 280 290 300
ADVHRTLVYG GIFLYPANKK NPSGKLRLLY ECNPIAYVME KAGGLATTGN
310 320 330 340 350
EDILDIVPTE IHQKAPVIMG STEDVQEFLE IYNKDKAKSR PSLPLPQSRA
360
RESPVHSICD ELF
Length:363
Mass (Da):39,609
Last modified:January 23, 2007 - v2
Checksum:i0470F1A2EA917D6F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481P → A in AAA41131 (PubMed:1846613).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04112 mRNA. Translation: AAA60739.1.
M57284
, M57274, M57279, M57278, M57282, M57281 Genomic DNA. Translation: AAA41131.1.
M86240 mRNA. Translation: AAA86425.1.
BC078894 mRNA. Translation: AAH78894.1.
BC078895 mRNA. Translation: AAH78895.1.
PIRiA31342.
RefSeqiNP_036690.2. NM_012558.3.
UniGeneiRn.33703.

Genome annotation databases

GeneIDi24362.
KEGGirno:24362.
UCSCiRGD:2595. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04112 mRNA. Translation: AAA60739.1.
M57284
, M57274, M57279, M57278, M57282, M57281 Genomic DNA. Translation: AAA41131.1.
M86240 mRNA. Translation: AAA86425.1.
BC078894 mRNA. Translation: AAH78894.1.
BC078895 mRNA. Translation: AAH78895.1.
PIRiA31342.
RefSeqiNP_036690.2. NM_012558.3.
UniGeneiRn.33703.

3D structure databases

ProteinModelPortaliP19112.
SMRiP19112. Positions 7-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4565506.

Chemistry

BindingDBiP19112.
ChEMBLiCHEMBL4391.

PTM databases

iPTMnetiP19112.
PhosphoSiteiP19112.

Proteomic databases

PRIDEiP19112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24362.
KEGGirno:24362.
UCSCiRGD:2595. rat.

Organism-specific databases

CTDi2203.
RGDi2595. Fbp1.

Phylogenomic databases

HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP19112.
KOiK03841.
PhylomeDBiP19112.

Enzyme and pathway databases

UniPathwayiUPA00138.
SABIO-RKP19112.

Miscellaneous databases

NextBioi603091.
PROiP19112.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence of rat liver fructose-1,6-bisphosphatase and evidence for down-regulation of its mRNA by insulin."
    El-Maghrabi M.R., Pilkis J., Marker A.J., Colosia A.D., D'Angelo G., Fraser B.A., Pilkis S.J.
    Proc. Natl. Acad. Sci. U.S.A. 85:8430-8434(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The rat fructose-1,6-bisphosphatase gene. Structure and regulation of expression."
    El-Maghrabi M.R., Lange A.J., Kummel L., Pilkis S.J.
    J. Biol. Chem. 266:2115-2120(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  3. "Liver fructose-1,6-bisphosphatase cDNA: trans-complementation of fission yeast and characterization of two human transcripts."
    Bertolotti R., Armbruster-Hilbert L., Okayama H.
    Differentiation 59:51-60(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. "Amino acid sequence of the COOH-terminal region of fructose-1,6-bisphosphatases in relation to cyclic AMP-dependent phosphorylation."
    Rittenhouse J., Chatterjee T., Marcus F., Reardon I., Heinrikson R.L.
    J. Biol. Chem. 258:7648-7652(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 320-362.
    Tissue: Liver.
  6. "Lysine 274 is essential for fructose 2,6-bisphosphate inhibition of fructose-1,6-bisphosphatase."
    el-Maghrabi M.R., Austin L.R., Correia J.J., Pilkis S.J.
    J. Biol. Chem. 267:6526-6530(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-275, ENZYME REGULATION.
  7. "Identification of novel protein targets regulated by maternal dietary fatty acid composition in neonatal rat liver."
    Novak E.M., Lee E.K., Innis S.M., Keller B.O.
    J. Proteomics 73:41-49(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT VAL-2.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216; SER-339 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF16P1_RAT
AccessioniPrimary (citable) accession number: P19112
Secondary accession number(s): Q64594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.