Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8RW99 (F16P2_PEA)

Last modified September 22, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Fructose-1,6-bisphosphatase, cytosolic
      Short name=FBPase
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Hide | Top

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Hide | Top

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.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

In plants there are two FBPase isozymes: one in the cytosol and the other in the chloroplast.

Sequence similarities

Belongs to the FBPase class 1 family.

Hide | Top

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Fructose-1,6-bisphosphatase, cytosolic
PRO_0000200518

Regions

Region124 – 1274Substrate binding By similarity

Sites

Metal binding711Magnesium 1 By similarity
Metal binding1001Magnesium 1 By similarity
Metal binding1001Magnesium 2 By similarity
Metal binding1211Magnesium 2 By similarity
Metal binding1211Magnesium 3 By similarity
Metal binding1231Magnesium 2; via carbonyl oxygen By similarity
Metal binding1241Magnesium 3 By similarity
Metal binding2831Magnesium 3 By similarity
Binding site2151Substrate By similarity
Binding site2471Substrate By similarity
Binding site2671Substrate By similarity
Binding site2771Substrate By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q8RW99-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 44A14ED36EDC96B6

FASTA34137,330
        10         20         30         40         50         60 
MDHAGDAMRT DLMTITRYVL NEQSKRPESR GDFTILLSHI VLGCKFVCSA VNKAGLAKLI 

        70         80         90        100        110        120 
GLAGETNIQG EEQKKLDVLS NEVFVKALTS SGRTCILVSE EDEEATFIEP SLRGKYCVVF 

       130        140        150        160        170        180 
DPLDGSFNID CGVSIGTIFG IYMVKDFETA TLEDVLQPGK NMVAAGYCMY GSSCTLVLST 

       190        200        210        220        230        240 
GSGVNGFTLD PSLGEYILTH PDIKIPNKGK IYSVNEGNAK NWDGPTTKYV EKCKFPTDGS 

       250        260        270        280        290        300 
SPKSLRYIES MVANVHRTLL YGGIFLYPGD KKSPNGKLRV LYEVFPMSFL MEQAGGQAFT 

       310        320        330        340 
GKQRALDLIP TKIHERSPVF LGSYDDVEDI KALYAAQEKT A

« Hide

Hide | Top

References

[1]Hahn T.-R., Son T.-J., Jang H.-K., Lee S.-W.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Hide | Top

Cross-references

Sequence databases

AY093594 mRNA. Translation: AAM14744.1.

3D structure databases

HSSPHSSP built from PDB template 1DBZ based on UniProtKB P46275.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.11. 287.

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...

Hide | Top

Entry information

Entry nameF16P2_PEA
AccessionPrimary (citable) accession number: Q8RW99
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2002
Last modified: September 22, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

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