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Reviewed, UniProtKB/Swiss-Prot P14766 (F16P2_SPIOL)

Last modified September 22, 2009. Version 65. 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
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

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Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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
   Technical termDirect protein sequencing
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 – 341341Fructose-1,6-bisphosphatase, cytosolic
PRO_0000200521

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

Experimental info

Sequence conflict1231L → F AA sequence Ref.2
Sequence conflict1771V → Y AA sequence Ref.2
Sequence conflict181 – 19010Missing AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P14766-1 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: BD079A41D975CA95

FASTA34137,199
        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 
DPLDGSSNID CGVSIGTIFG IYMVKDFETA TLEDVLQPGK NMVAAGYCMY GSSCTLVLST 

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

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

       310        320        330        340 
GKQRALDLIP TKIHERSPVF LGSYDDVEDI KALYAAQEKT A

« Hide

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References

[1]"Isolation and characterization of a cDNA encoding cytosolic fructose-1,6-bisphosphatase from spinach."
Hur Y., Unger E.A., Vasconcelos A.C.
Plant Mol. Biol. 18:799-802(1992) [PubMed: 1313712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
[2]"Spinach cytosolic fructose-1,6-bisphosphatase. Purification, enzyme properties and structural comparisons."
Ladror U.S., Latshaw S.P., Marcus F.
Eur. J. Biochem. 189:89-94(1990) [PubMed: 2158892] [Abstract]
Cited for: PROTEIN SEQUENCE OF 10-341.
Tissue: Leaf.

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Cross-references

Sequence databases

X61690 mRNA. Translation: CAA43860.1.
PIRPASPY. S20852.

3D structure databases

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

Enzyme and pathway databases

BRENDA3.1.3.11. 286.

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_SPIOL
AccessionPrimary (citable) accession number: P14766
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 1, 1992
Last modified: September 22, 2009
This is version 65 of the entry and version 2 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