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Reviewed, UniProtKB/Swiss-Prot Q9Z1N1 (F16P2_RAT)

Last modified January 19, 2010. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fructose-1,6-bisphosphatase isozyme 2
      Short name=FBPase 2
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 2
Gene names
Name: Fbp2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 3 magnesium ions per subunit By similarity.

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. Fructose-2,6-biphosphate acts as competitive inhibitor By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the FBPase class 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Gluconeogenesis
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from direct assay. Source: RGD

   Molecular functionfructose 1,6-bisphosphate 1-phosphatase activity

Inferred from direct assay. Source: RGD

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Fructose-1,6-bisphosphatase isozyme 2
PRO_0000200507

Regions

Nucleotide binding18 – 225AMP By similarity
Nucleotide binding28 – 325AMP By similarity
Nucleotide binding113 – 1142AMP By similarity
Region122 – 1254Substrate binding By similarity
Region213 – 2164Substrate binding By similarity
Region244 – 2496Substrate binding By similarity
Region275 – 2773Substrate binding By similarity

Sites

Metal binding691Magnesium 1 By similarity
Metal binding981Magnesium 1 By similarity
Metal binding981Magnesium 2 By similarity
Metal binding1191Magnesium 2 By similarity
Metal binding1191Magnesium 3 By similarity
Metal binding1211Magnesium 2; via carbonyl oxygen By similarity
Metal binding1221Magnesium 3 By similarity
Metal binding2811Magnesium 3 By similarity
Binding site1411AMP By similarity
Binding site2651Substrate By similarity

Amino acid modifications

Modified residue2161Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z1N1-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 13096E40E96095D8

FASTA33936,887
        10         20         30         40         50         60 
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLANLYGI 

        70         80         90        100        110        120 
AGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN KEAVITAKER RGKYVVCFDP 

       130        140        150        160        170        180 
LDGSSNIDCL ASIGTIFAIY RKTTEDEPSE KDALQPGRNI VAAGYALYGS ATLVALSTGQ 

       190        200        210        220        230        240 
GVDLFMLDPA LGEFVLVEKD IRIKKKGKIF SLNEGYAKYF DAATAEYVQK KKFPEDGSAP 

       250        260        270        280        290        300 
YGARYVGSMV ADVHRTLVYG GIFMYPANQK SPNGKLRLLY ECNPVAYIIE QAGGMATTGT 

       310        320        330 
QPVLDVKPES IHQRVPLILG SPEDVQEYLS CVQRNQAGR 

« Hide

References

[1]"Cloning and expression of rat muscle fructose-1,6-bisphosphatase cDNA."
Al-Robaiy S., Eschrich K.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005046 mRNA. Translation: CAA06313.1.
IPIIPI00209038.
RefSeqNP_446168.1.
UniGeneRn.15319

3D structure databases

SMRQ9Z1N1. Positions 7-337.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9Z1N1.

Genome annotation databases

EnsemblENSRNOT00000023865; ENSRNOP00000023865; ENSRNOG00000017637; Rattus norvegicus. [Genome view]
GeneID114508.
KEGGrno:114508.
UCSCNM_053716. rat.

Organism-specific databases

CTD114508.
RGD620930. Fbp2.

Phylogenomic databases

eggNOGroNOG08567.
HOVERGENQ9Z1N1.
InParanoidQ9Z1N1.
PhylomeDBQ9Z1N1.

Enzyme and pathway databases

BRENDA3.1.3.11. 248.

Gene expression databases

ArrayExpressQ9Z1N1.
GenevestigatorQ9Z1N1.
GermOnlineENSRNOG00000017637. Rattus norvegicus.

Family and domain databases

InterProIPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio618609.

Entry information

Entry nameF16P2_RAT
AccessionPrimary (citable) accession number: Q9Z1N1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: May 1, 1999
Last modified: January 19, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents