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Reviewed, UniProtKB/Swiss-Prot P46275 (F16P1_PEA)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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, chloroplastic
      Short name=FBPase
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase
Gene names
Name: FBP
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

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Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Homotetramer.

Subcellular location

Plastid › chloroplast 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.

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Ontologies

Keywords
   Biological processCalvin cycle
Carbohydrate metabolism
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Chloroplast
Chain51 – 407357Fructose-1,6-bisphosphatase, chloroplastic
PRO_0000008817

Regions

Region179 – 1824Substrate binding By similarity

Sites

Metal binding1261Magnesium 1 By similarity
Metal binding1551Magnesium 1 By similarity
Metal binding1551Magnesium 2 By similarity
Metal binding1761Magnesium 2 By similarity
Metal binding1761Magnesium 3 By similarity
Metal binding1781Magnesium 2; via carbonyl oxygen By similarity
Metal binding1791Magnesium 3 By similarity
Metal binding3551Magnesium 3 By similarity
Binding site2871Substrate By similarity
Binding site3191Substrate By similarity
Binding site3371Substrate By similarity
Binding site3391Substrate By similarity
Binding site3491Substrate By similarity

Amino acid modifications

Disulfide bond203 ↔ 223

Experimental info

Sequence conflict821G → P in CAA48719. Ref.2
Sequence conflict1601A → P in CAA48719. Ref.2
Sequence conflict2471A → I in CAA48719. Ref.2
Sequence conflict2821E → K in CAA48719. Ref.2

Secondary structure

1 ...................................................... 407
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P46275-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B60E9164F1F6FE9D

FASTA40744,511
        10         20         30         40         50         60 
MAAATASSQL IFSKPYSPSR LCPFQLCVFD AKSVLSSSRR KHVNGSGVRC MAVKEATSET 

        70         80         90        100        110        120 
KKRSGYEIIT LTSWLLQQEQ KGIIDAELTI VLSSISMACK QIASLVQRAN ISNLTGTQGA 

       130        140        150        160        170        180 
VNIQGEDQKK LDVISNEVFS NCLRSSGRTG IIASEEEDVA VAVEESYSGN YIVVFDPLDG 

       190        200        210        220        230        240 
SSNLDAAVST GSIFGIYSPN DECLPDFGDD SDDNTLGTEE QRCIVNVCQP GSNLLAAGYC 

       250        260        270        280        290        300 
MYSSSVAFVL TIGKGVFVFT LDPLYGEFVL TQENLQIPKS GEIYSFNEGN YKLWDENLKK 

       310        320        330        340        350        360 
YIDDLKEPGP SGKPYSARYI GSLVGDFHRT LLYGGIYGYP RDKKSKNGKL RLLYECAPMS 

       370        380        390        400 
FIVEQAGGKG SDGHQRVLDI QPTEIHQRVP LYIGSTEEVE KVEKYLA

« Hide

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References

[1]"Nucleotide sequence analysis of a cDNA encoding chloroplastic fructose-1,6-bisphosphatase from pea (Pisum sativum l.)."
Dong S.M., Rhim J.H., Hahn T.R.
Plant Physiol. 107:313-314(1995) [PubMed: 7870839] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Giant.
Tissue: Leaf.
[2]"Cloning, structure and expression of a pea cDNA clone coding for a photosynthetic fructose-1,6-bisphosphatase with some features different from those of the leaf chloroplast enzyme."
Carrasco J.L., Chueca A., Prado F.E., Hermoso R., Lazaro J.J., Ramos J.L., Sahrawy M., Lopez Gorge J.
Planta 193:494-501(1994) [PubMed: 7764999] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-407.
Strain: cv. Lincoln.
Tissue: Leaf.
[3]"Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase."
Chiadmi M., Navaza A., Miginiac-Maslow M., Jacquot J.-P., Cherfils J.
EMBO J. 18:6809-6815(1999) [PubMed: 10581254] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-407.

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Cross-references

Sequence databases

L34806 mRNA. Translation: AAD10213.1.
X68826 mRNA. Translation: CAA48719.1.
PIRS29560.
T06408.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1D9QX-ray2.40A/B/C/D51-407[»]
1DBZX-ray2.65A/B/C/D51-407[»]
1DCUX-ray2.20A/B/C/D51-407[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.11. 287.

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...

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Entry information

Entry nameF16P1_PEA
AccessionPrimary (citable) accession number: P46275
Secondary accession number(s): Q37263
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 66 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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