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Protein

Fructose-1,6-bisphosphatase 1

Gene

Fbp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi69Magnesium 1By similarity1
Metal bindingi98Magnesium 1By similarity1
Metal bindingi98Magnesium 2By similarity1
Metal bindingi119Magnesium 2By similarity1
Metal bindingi119Magnesium 3By similarity1
Metal bindingi121Magnesium 2; via carbonyl oxygenBy similarity1
Metal bindingi122Magnesium 3By similarity1
Binding sitei141AMPBy similarity1
Binding sitei265SubstrateBy similarity1
Metal bindingi281Magnesium 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 22AMPBy similarity5
Nucleotide bindingi28 – 32AMPBy similarity5
Nucleotide bindingi113 – 114AMPBy similarity2

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

Keywordsi

Molecular functionAllosteric enzyme, Hydrolase
Biological processCarbohydrate metabolism, Gluconeogenesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKiP19112
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2595 Fbp1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi275K → A: Reduces affinity for substrate 20-fold, and decreases affinity for the competitive inhibitor fructose 2,6-bisphosphate 500-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4391

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002005022 – 363Fructose-1,6-bisphosphatase 1Add BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylvaline1 Publication1
Modified residuei151N6-succinyllysineBy similarity1
Modified residuei216PhosphotyrosineCombined sources1
Modified residuei245PhosphotyrosineBy similarity1
Modified residuei265PhosphotyrosineBy similarity1
Modified residuei339PhosphoserineCombined sources1
Modified residuei353PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP19112

PTM databases

iPTMnetiP19112
PhosphoSitePlusiP19112

Interactioni

Subunit structurei

Homotetramer.By similarity

Chemistry databases

BindingDBiP19112

Structurei

3D structure databases

ProteinModelPortaliP19112
SMRiP19112
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni122 – 125Substrate bindingBy similarity4
Regioni213 – 216Substrate bindingBy similarity4
Regioni244 – 249Substrate bindingBy similarity6
Regioni275 – 277Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

HOGENOMiHOG000191265
HOVERGENiHBG005627
InParanoidiP19112
KOiK03841
PhylomeDBiP19112

Family and domain databases

CDDicd00354 FBPase, 1 hit
HAMAPiMF_01855 FBPase_class1, 1 hit
InterProiView protein in InterPro
IPR000146 FBPase_class-1
IPR033391 FBPase_N
IPR028343 FBPtase
IPR020548 Fructose_bisphosphatase_AS
PANTHERiPTHR11556 PTHR11556, 1 hit
PfamiView protein in Pfam
PF00316 FBPase, 1 hit
PIRSFiPIRSF500210 FBPtase, 1 hit
PIRSF000904 FBPtase_SBPase, 1 hit
PRINTSiPR00115 F16BPHPHTASE
PROSITEiView protein in PROSITE
PS00124 FBPASE, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti148P → A in AAA41131 (PubMed:1846613).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiF16P1_RAT
AccessioniPrimary (citable) accession number: P19112
Secondary accession number(s): Q64594
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 146 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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
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