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Protein

Fructose-1,6-bisphosphatase isozyme 2

Gene

Fbp2

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 and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate.

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. Fructose 2,6-bisphosphate acts as competitive inhibitor. Strongly inhibited by Ca2+ (By similarity).By similarity

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
Binding sitei18AMP; via carbonyl oxygenBy similarity1
Sitei33Important for the conversion from active R-state to inactive T-state in the presence of AMPBy similarity1
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 sitei122SubstrateBy similarity1
Binding sitei141AMPBy similarity1
Binding sitei265SubstrateBy similarity1
Binding sitei275SubstrateBy similarity1
Metal bindingi281Magnesium 3By similarity1

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-RNO-70263 Gluconeogenesis
SABIO-RKiQ9Z1N1
UniPathwayiUPA00138

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase isozyme 2 (EC:3.1.3.11)
Short name:
FBPase 2
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 2
Muscle FBPase
Gene namesi
Name:Fbp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi620930 Fbp2

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

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002005071 – 339Fructose-1,6-bisphosphatase isozyme 2Add BLAST339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei216PhosphotyrosineCombined sources1
Modified residuei219PhosphotyrosineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z1N1
PRIDEiQ9Z1N1

PTM databases

iPTMnetiQ9Z1N1
PhosphoSitePlusiQ9Z1N1

Expressioni

Gene expression databases

BgeeiENSRNOG00000017637
GenevisibleiQ9Z1N1 RN

Interactioni

Subunit structurei

Homotetramer. Interacts with ALDOA; the interaction blocks inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+. Interacts with alpha-actinin and F-actin (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023865

Structurei

3D structure databases

ProteinModelPortaliQ9Z1N1
SMRiQ9Z1N1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 10Important for interaction with ALDOABy similarity8
Regioni213 – 216Substrate bindingBy similarity4
Regioni245 – 249Substrate bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi204 – 208Nuclear localization signalBy similarity5

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

eggNOGiKOG1458 Eukaryota
COG0158 LUCA
GeneTreeiENSGT00390000015513
HOGENOMiHOG000191265
HOVERGENiHBG005627
InParanoidiQ9Z1N1
KOiK03841
OMAiHEKSECY
OrthoDBiEOG091G0AZP
PhylomeDBiQ9Z1N1
TreeFamiTF314824

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.

Q9Z1N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR
60 70 80 90 100
KAGLANLYGI AGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN
110 120 130 140 150
KEAVITAKER RGKYVVCFDP LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE
160 170 180 190 200
KDALQPGRNI VAAGYALYGS ATLVALSTGQ GVDLFMLDPA LGEFVLVEKD
210 220 230 240 250
IRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSAP YGARYVGSMV
260 270 280 290 300
ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT
310 320 330
QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR
Length:339
Mass (Da):36,887
Last modified:May 1, 1999 - v1
Checksum:i13096E40E96095D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005046 mRNA Translation: CAA06313.1
RefSeqiNP_446168.1, NM_053716.1
UniGeneiRn.15319

Genome annotation databases

EnsembliENSRNOT00000023865; ENSRNOP00000023865; ENSRNOG00000017637
GeneIDi114508
KEGGirno:114508
UCSCiRGD:620930 rat

Similar proteinsi

Entry informationi

Entry nameiF16P2_RAT
AccessioniPrimary (citable) accession number: Q9Z1N1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: May 1, 1999
Last modified: March 28, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health