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Reviewed, UniProtKB/Swiss-Prot P46267 (F16P2_BRANA)

Last modified September 22, 2009. Version 51. 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
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Brassica

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Protein attributes

Sequence length339 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 – 339339Fructose-1,6-bisphosphatase, cytosolic
PRO_0000200514

Regions

Region123 – 1264Substrate binding By similarity

Sites

Metal binding701Magnesium 1 By similarity
Metal binding991Magnesium 1 By similarity
Metal binding991Magnesium 2 By similarity
Metal binding1201Magnesium 2 By similarity
Metal binding1201Magnesium 3 By similarity
Metal binding1221Magnesium 2; via carbonyl oxygen By similarity
Metal binding1231Magnesium 3 By similarity
Metal binding2821Magnesium 3 By similarity
Binding site2141Substrate By similarity
Binding site2461Substrate By similarity
Binding site2661Substrate By similarity
Binding site2761Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
P46267-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3844CD90F3C6DD33

FASTA33937,156
        10         20         30         40         50         60 
MDHEADAFRD LMTITRFVLN EQSKYPESRG DFTILLSNIV LGCKFVCSAV NKAGLAKLIG 

        70         80         90        100        110        120 
LAGDTNIQGE EQKKLDVLSN DVFVKALVSS GRTSVLVSEE DEEATFVESS KCGKYCVVFD 

       130        140        150        160        170        180 
PLDGSSNIDC GVSIGTIFGI YTMEHSDEPT TKDVLKPGNE MVAAGYCMYG SSCMLVLSTG 

       190        200        210        220        230        240 
TGVHGFTLDP SLGEFILTHP DIKIPKKGNI YSVNEGNAQN WDGPTTKYVE RCKYPKDGSP 

       250        260        270        280        290        300 
AKSLRYVGSM VADVHRTLLY GGIFLYPADK KSPNGKLRVL YEVFPMAFLM EQAGGQAFTG 

       310        320        330 
KKRALDLVPK KIHERSPIFL GSYDDVEEIK ALYAEEEKN

« Hide

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References

[1]"Isolation and characterization of an oilseed rape fructose-1,6-bisphosphatase cDNA."
Laroche A., Frick M.M., Kazala C., Weselake R.J., Thomas J.E.
Plant Physiol. 108:1335-1336(1995) [PubMed: 7630967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cotyledon.

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Cross-references

Sequence databases

U20179 mRNA. Translation: AAA82750.1.
PIRT07853.

3D structure databases

HSSPHSSP built from PDB template 1BK4 based on UniProtKB P00637.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.11. 393.

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_BRANA
AccessionPrimary (citable) accession number: P46267
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 22, 2009
This is version 51 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