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Reviewed, UniProtKB/Swiss-Prot P22418 (F16P1_SPIOL)

Last modified June 16, 2009. Version 72. 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
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 length415 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.

Induction

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

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
Direct protein sequencing
Gene Ontology (GO)
   Biological processreductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

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 – 5757Chloroplast Ref.2
Chain58 – 415358Fructose-1,6-bisphosphatase, chloroplastic
PRO_0000008818

Regions

Region188 – 1914Substrate binding By similarity
Region207 – 23226Involved in light regulation Potential

Sites

Metal binding1351Magnesium 1 By similarity
Metal binding1641Magnesium 1 By similarity
Metal binding1641Magnesium 2 By similarity
Metal binding1851Magnesium 2 By similarity
Metal binding1851Magnesium 3 By similarity
Metal binding1871Magnesium 2; via carbonyl oxygen By similarity
Metal binding1881Magnesium 3 By similarity
Metal binding3631Magnesium 3 By similarity
Binding site2951Substrate By similarity
Binding site3271Substrate By similarity
Binding site3451Substrate By similarity
Binding site3471Substrate By similarity
Binding site3571Substrate By similarity

Amino acid modifications

Disulfide bond231 ↔ 236Redox-active (light-modulated) By similarity

Experimental info

Sequence conflict661E → Q AA sequence Ref.2
Sequence conflict881E → P AA sequence Ref.2
Sequence conflict3031D → P AA sequence Ref.2

Secondary structure

1 ................................................. 415
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P22418-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: A23465129F54A5A1

FASTA41545,230
        10         20         30         40         50         60 
MASIGPATTT AVKLRSSIFN PQSSTLSPSQ QCITFTKSLH SFPTATRHNV ASGVRCMAAV 

        70         80         90        100        110        120 
GEAATETKAR TRSKYEIETL TGWLLKQEMA GVIDAELTIV LSSISLACKQ IASLVQRAGI 

       130        140        150        160        170        180 
SNLTGIQGAV NIQGEDQKKL DVVSNEVFSS CLRSSGRTGI IASEEEDVPV AVEESYSGNY 

       190        200        210        220        230        240 
IVVFDPLDGS SNIDAAVSTG SIFGIYSPND ECIVDSDHDD ESQLSAEEQR CVVNVCQPGD 

       250        260        270        280        290        300 
NLLAAGYCMY SSSVIFVLTI GKGVYAFTLD PMYGEFVLTS EKIQIPKAGK IYSFNEGNYK 

       310        320        330        340        350        360 
MWDDKLKKYM DDLKEPGESQ KPYSSRYIGS LVGDFHRTLL YGGIYGYPRD AKSKNGKLRL 

       370        380        390        400        410 
LYECAPMSFI VEQAGGKGSD GHQRILDIQP TEIHQRVPLY IGSVEEVEKL EKYLA

« Hide

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References

[1]"Higher-plant chloroplast and cytosolic fructose-1,6-bisphosphatase isoenzymes: origins via duplication rather than prokaryote-eukaryote divergence."
Martin W., Mustafa A.Z., Henze K., Schnarrenberger C.
Plant Mol. Biol. 32:485-491(1996) [PubMed: 8980497] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Seedling.
[2]"Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase."
Marcus F., Harrsch P.B.
Arch. Biochem. Biophys. 279:151-157(1990) [PubMed: 2159755] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-415.
[3]"Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography."
Villeret V., Huang S., Zhang Y., Lipscomb W.N.
Biochemistry 34:4307-4315(1995) [PubMed: 7703244] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

L76555 mRNA. Translation: AAD10207.1.
PIRT09085.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1SPIX-ray2.80A/B/C/D58-415[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.11. 286.

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_SPIOL
AccessionPrimary (citable) accession number: P22418
Secondary accession number(s): O20251
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 15, 1998
Last modified: June 16, 2009
This is version 72 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