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Reviewed, UniProtKB/Swiss-Prot Q07204 (F16P1_BRANA)

Last modified June 16, 2009. Version 59. 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, chloroplastic
      Short name=FBPase
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase
Gene names
Name: FBP
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeBrassica

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Homotetramer By similarity.

Subcellular location

Plastidchloroplast stroma.

Induction

Light activation through pH changes, Mg2+ levels and also by light-modulated reduction of essential disulfide groups via the ferredoxin-thioredoxin f system 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.

Ontologies

Keywords
   Biological processCalvin cycle
Carbohydrate metabolism
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processreductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast stroma

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Chloroplast By similarity
Chain54 – 411358Fructose-1,6-bisphosphatase, chloroplastic
PRO_0000008815

Regions

Region186 – 1894Substrate binding By similarity

Sites

Metal binding1331Magnesium 1 By similarity
Metal binding1621Magnesium 1 By similarity
Metal binding1621Magnesium 2 By similarity
Metal binding1831Magnesium 2 By similarity
Metal binding1831Magnesium 3 By similarity
Metal binding1851Magnesium 2; via carbonyl oxygen By similarity
Metal binding1861Magnesium 3 By similarity
Metal binding3591Magnesium 3 By similarity
Binding site2911Substrate By similarity
Binding site3231Substrate By similarity
Binding site3411Substrate By similarity
Binding site3431Substrate By similarity
Binding site3531Substrate By similarity

Amino acid modifications

Disulfide bond227 ↔ 232Redox-active (light-modulated) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07204-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 83AC46D39EA7CECF

FASTA41144,446
        10         20         30         40         50         60 
MAATAGATPS SHLLLSSSRH VAASPQPRIL FPSLSGKRVA VGKNHHATGV RCMAVAADAT 

        70         80         90        100        110        120 
AETKPAAKKK SGYELQTLTS WLLRQEMKGE IDTELTIVMS SIAMACKQIA SLVQRAGISN 

       130        140        150        160        170        180 
LTGVQGAVNI QGEDQKKLDV VSNEVFSNCL RSSGRTGIIA SEEEDVPVAV EESYSGNYVV 

       190        200        210        220        230        240 
VFDPLDGSSN IDAAVSTGSI FGIYSPNDEC LPDSDDTSAL GSEEERCIVN VCQPGNNLLA 

       250        260        270        280        290        300 
AGYCMYSSSV IFVLTLGKGV FAFTLDPMYG EFVLTQENIE IPKAGKIYSF NEGNYQMWDE 

       310        320        330        340        350        360 
NLKKYIDDLK DPGPSGKPYS ARYIGSLVGD FHRTLLYGGI YGYPRDAKSK NGKLRLLYEC 

       370        380        390        400        410 
APMSFIVEQA GGKGSDGHHR VLDIQPTEIH QRVPLYIGSK EEVEKLEKYL A 

« Hide

References

[1]"Sequence of a cDNA encoding chloroplast fructose-1,6-bisphosphatase from rapeseed."
Rodriguez-Suarez R.J., Wolosiuk R.A.
Plant Physiol. 103:1453-1454(1993) [PubMed: 8290637] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

L15303 mRNA. Translation: AAB88708.1.
PIRT07987.

3D structure databases

HSSPHSSP built from PDB template 1D9Q based on UniProtKB P46275.
SMRQ07204. Positions 73-411.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.11. 393.

Family and domain databases

InterProIPR000146. Fructose_bisphosphatase.
IPR017955. IMPase/FBPase.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. FBPHPHTASE.
PR00377. INFBPHPHTASE.
ProDomPD001491. In_FB_phphtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16P1_BRANA
AccessionPrimary (citable) accession number: Q07204
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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