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Protein

Fructose-1,6-bisphosphatase, chloroplastic

Gene

FBP

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi126Magnesium 1By similarity1
Metal bindingi155Magnesium 1By similarity1
Metal bindingi155Magnesium 2By similarity1
Metal bindingi176Magnesium 2By similarity1
Metal bindingi176Magnesium 3By similarity1
Metal bindingi178Magnesium 2; via carbonyl oxygenBy similarity1
Metal bindingi179Magnesium 3By similarity1
Binding sitei287SubstrateBy similarity1
Binding sitei319SubstrateBy similarity1
Binding sitei337SubstrateBy similarity1
Binding sitei339SubstrateBy similarity1
Binding sitei349SubstrateBy similarity1
Metal bindingi355Magnesium 3By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calvin cycle, Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKP46275.
UniPathwayiUPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase, chloroplastic (EC:3.1.3.11)
Short name:
FBPase
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase
Gene namesi
Name:FBP
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50ChloroplastAdd BLAST50
ChainiPRO_000000881751 – 407Fructose-1,6-bisphosphatase, chloroplasticAdd BLAST357

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi203 ↔ 223

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP46275.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1407
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi71 – 80Combined sources10
Helixi86 – 112Combined sources27
Turni113 – 115Combined sources3
Helixi127 – 142Combined sources16
Turni143 – 146Combined sources4
Beta strandi147 – 152Combined sources6
Beta strandi155 – 157Combined sources3
Beta strandi161 – 166Combined sources6
Beta strandi172 – 179Combined sources8
Helixi184 – 186Combined sources3
Beta strandi190 – 197Combined sources8
Helixi218 – 227Combined sources10
Turni230 – 232Combined sources3
Beta strandi233 – 254Combined sources22
Beta strandi256 – 262Combined sources7
Turni263 – 266Combined sources4
Beta strandi267 – 274Combined sources8
Beta strandi282 – 285Combined sources4
Helixi288 – 293Combined sources6
Helixi296 – 306Combined sources11
Beta strandi310 – 312Combined sources3
Helixi323 – 333Combined sources11
Beta strandi336 – 339Combined sources4
Beta strandi343 – 345Combined sources3
Beta strandi349 – 351Combined sources3
Turni352 – 355Combined sources4
Helixi356 – 365Combined sources10
Beta strandi369 – 376Combined sources8
Helixi377 – 379Combined sources3
Beta strandi391 – 394Combined sources4
Helixi396 – 406Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D9QX-ray2.40A/B/C/D51-407[»]
1DBZX-ray2.65A/B/C/D51-407[»]
1DCUX-ray2.20A/B/C/D51-407[»]
ProteinModelPortaliP46275.
SMRiP46275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46275.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni179 – 182Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

CDDicd00354. FBPase. 1 hit.
HAMAPiMF_01855. FBPase_class1. 1 hit.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATASSQL IFSKPYSPSR LCPFQLCVFD AKSVLSSSRR KHVNGSGVRC
60 70 80 90 100
MAVKEATSET KKRSGYEIIT LTSWLLQQEQ KGIIDAELTI VLSSISMACK
110 120 130 140 150
QIASLVQRAN ISNLTGTQGA VNIQGEDQKK LDVISNEVFS NCLRSSGRTG
160 170 180 190 200
IIASEEEDVA VAVEESYSGN YIVVFDPLDG SSNLDAAVST GSIFGIYSPN
210 220 230 240 250
DECLPDFGDD SDDNTLGTEE QRCIVNVCQP GSNLLAAGYC MYSSSVAFVL
260 270 280 290 300
TIGKGVFVFT LDPLYGEFVL TQENLQIPKS GEIYSFNEGN YKLWDENLKK
310 320 330 340 350
YIDDLKEPGP SGKPYSARYI GSLVGDFHRT LLYGGIYGYP RDKKSKNGKL
360 370 380 390 400
RLLYECAPMS FIVEQAGGKG SDGHQRVLDI QPTEIHQRVP LYIGSTEEVE

KVEKYLA
Length:407
Mass (Da):44,511
Last modified:November 1, 1997 - v2
Checksum:iB60E9164F1F6FE9D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82G → P in CAA48719 (PubMed:7764999).Curated1
Sequence conflicti160A → P in CAA48719 (PubMed:7764999).Curated1
Sequence conflicti247A → I in CAA48719 (PubMed:7764999).Curated1
Sequence conflicti282E → K in CAA48719 (PubMed:7764999).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34806 mRNA. Translation: AAD10213.1.
X68826 mRNA. Translation: CAA48719.1.
PIRiS29560.
T06408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34806 mRNA. Translation: AAD10213.1.
X68826 mRNA. Translation: CAA48719.1.
PIRiS29560.
T06408.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D9QX-ray2.40A/B/C/D51-407[»]
1DBZX-ray2.65A/B/C/D51-407[»]
1DCUX-ray2.20A/B/C/D51-407[»]
ProteinModelPortaliP46275.
SMRiP46275.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP46275.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00116.
SABIO-RKP46275.

Miscellaneous databases

EvolutionaryTraceiP46275.

Family and domain databases

CDDicd00354. FBPase. 1 hit.
HAMAPiMF_01855. FBPase_class1. 1 hit.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiF16P1_PEA
AccessioniPrimary (citable) accession number: P46275
Secondary accession number(s): Q37263
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

In plants there are two FBPase isozymes: one in the cytosol and the other in the chloroplast.

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.