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Reviewed, UniProtKB/Swiss-Prot P46276 (F16P2_SOLTU)

Last modified September 22, 2009. Version 54. 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

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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
    CY-F1
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

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Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Fructose-1,6-bisphosphatase, cytosolic
PRO_0000200520

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

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Sequences

Sequence LengthMass (Da)Tools
P46276-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C470B55B35E6BFF6

FASTA34037,311
        10         20         30         40         50         60 
MDHAADRHRT DLMTITRFVL NEQTKHPESR GDFSILLSHI VLGCKFVCTA VNKAGLAKLL 

        70         80         90        100        110        120 
GLAGETNVQG EDQKKLDVLS NEVFIKALVS SNRTCILVSE EDEEATFVRP ANRGKYCVVF 

       130        140        150        160        170        180 
DPLDGSSNID CGVSIGTIFG IYMIKDGHEP TLDDVLQPGM NMLAAGYCMY GSSCTLVLST 

       190        200        210        220        230        240 
GSGVNGFTLD PSLGEFILTH PDIKIPKKGK IYSVNEGNAK NWDSPTSKYV QSCKYPADGS 

       250        260        270        280        290        300 
SPKSLRYIGS MVADVHRTLL YGGIFLYPGD KKSPNGKLRV LYEVFPMSFL MEQAGGQAFT 

       310        320        330        340 
GKQRALDLVP EKIHERSPIF LGSYDDVEEI KKLYAAEEQN

« Hide

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References

[1]"Reduction of the cytosolic fructose-1,6-bisphosphatase in transgenic potato plants limits photosynthetic sucrose biosynthesis with no impact on plant growth and tuber yield."
Zrenner R., Krause K.P., Apel P., Sonnewald U.
Plant J. 9:671-681(1996) [PubMed: 8653116] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Desiree.
Tissue: Leaf.

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Cross-references

Sequence databases

X76946 mRNA. Translation: CAA54265.1.
PIRS41287.

3D structure databases

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

Enzyme and pathway databases

BRENDA3.1.3.11. 296.

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...

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Entry information

Entry nameF16P2_SOLTU
AccessionPrimary (citable) accession number: P46276
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 22, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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