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Reviewed, UniProtKB/Swiss-Prot Q42796 (F16P1_SOYBN)

Last modified February 9, 2010. Version 67. 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
OrganismGlycine max (Soybean)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycine

Protein attributes

Sequence length402 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.

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

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 – 5050Chloroplast Potential
Chain51 – 402352Fructose-1,6-bisphosphatase, chloroplastic
PRO_0000008819

Regions

Region180 – 1834Substrate binding By similarity

Sites

Metal binding1271Magnesium 1 By similarity
Metal binding1561Magnesium 1 By similarity
Metal binding1561Magnesium 2 By similarity
Metal binding1771Magnesium 2 By similarity
Metal binding1771Magnesium 3 By similarity
Metal binding1791Magnesium 2; via carbonyl oxygen By similarity
Metal binding1801Magnesium 3 By similarity
Metal binding3531Magnesium 3 By similarity
Binding site2851Substrate By similarity
Binding site3171Substrate By similarity
Binding site3351Substrate By similarity
Binding site3371Substrate By similarity
Binding site3471Substrate By similarity

Amino acid modifications

Disulfide bond221 ↔ 226Redox-active (light-modulated) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q42796-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2EC4876454C59A3B

FASTA40243,897
        10         20         30         40         50         60 
MAAATASTQL IFSKPCSPSR LCPFQLCVFD TKQVLSSGRR RHVGGSGVRC MAVGEAATTG 

        70         80         90        100        110        120 
TKKRSGYELQ TLTSWLLKQE QAGVIDAELT IVLSSISMAC KQIASLVQRA NISNLTGVQG 

       130        140        150        160        170        180 
AVNVQGEDQK KLDVVSNEVF SNCLRSSGRT GIIASEEEDV PVAVEESYSG NYIVVFDPLD 

       190        200        210        220        230        240 
GSSNIDAAAS TGSNFWIYSP NDECLADIDD DPTLDTTEQR CIVNVCQPGS NLLAAGYCMY 

       250        260        270        280        290        300 
SSSIIFVLTL GNGVFVFTLD PMYGEFVLTQ ENLQIPRAGK IYAFNEGNYQ LWDEKLKKYI 

       310        320        330        340        350        360 
DDLKDPGQSG KPYSARYIGS LVGDFHRTLL YGGIYGYPRD KKSKNGKLRL LYECAPINFI 

       370        380        390        400 
VEQAGGKGTD GLQVLRLQGT EIHQRVPLYI GEEVEKVEKY LA 

« Hide

References

[1]"Molecular characterization of a cDNA encoding chloroplastic fructose-1,6-bisphosphatase from soybean (Glycine max L.)."
Jeon Y.H., Bhoo S.H., Hahn T.R.
Mol. Cells 8:113-116(1998) [PubMed: 9571641] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Jinhung.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34841 mRNA. Translation: AAA33956.1.
PIRT07134.
UniGeneGma.33674

3D structure databases

SMRQ42796. Positions 63-402.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.11. 299.

Gene expression databases

GenevestigatorQ42796.

Family and domain databases

InterProIPR000146. Fructose_bisphosphatase.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16P1_SOYBN
AccessionPrimary (citable) accession number: Q42796
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 67 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