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Reviewed, UniProtKB/Swiss-Prot Q9N0J6 (F16P2_RABIT)

Last modified September 22, 2009. Version 48. 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
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 electronic annotation. Source: UniProtKB-KW

   Molecular functionfructose 1,6-bisphosphate 1-phosphatase activity

Inferred from electronic annotation. Source: EC

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_0000200506

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
Q9N0J6-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C1D65B70F8763872

FASTA33936,816
        10         20         30         40         50         60 
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLAHLYGI 

        70         80         90        100        110        120 
AGTVNVTGDE VKKLDVLSNA LVINMLQSSY STCVLVSEEN KEAIITAKER RGKYVVCFDP 

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

       190        200        210        220        230        240 
GVDLFMLDPA LGEFVLVEKD VKIKKKGKIF SLNEGYAKYF DAATTEYVQK KKFPEDGSAP 

       250        260        270        280        290        300 
YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT 

       310        320        330 
QPVLDVKPES IHQRVPLILG SPDDVQEYLA CVQKNQAGR 

« Hide

References

[1]"Fructose-1,6-bisphosphatase genes in animals."
Tillmann H., Bernhard D., Eschrich K.
Gene 291:57-66(2002) [PubMed: 12095679] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

Cross-references

Sequence databases

AJ272520 mRNA. Translation: CAB76202.1.
RefSeqNP_001075597.1.
UniGeneOcu.6263

3D structure databases

HSSPHSSP built from PDB template 1FTA based on UniProtKB P09467.
SMRQ9N0J6. Positions 9-335.
ModBaseSearch...

Genome annotation databases

GeneID100008853.

Organism-specific databases

CTD100008853.

Phylogenomic databases

HOVERGENQ9N0J6.

Enzyme and pathway databases

BRENDA3.1.3.11. 255.

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.
ProDomPD001491. In_FB_phphtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16P2_RABIT
AccessionPrimary (citable) accession number: Q9N0J6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: October 1, 2000
Last modified: September 22, 2009
This is version 48 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