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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261Magnesium 1By similarity
Metal bindingi155 – 1551Magnesium 1By similarity
Metal bindingi155 – 1551Magnesium 2By similarity
Metal bindingi176 – 1761Magnesium 2By similarity
Metal bindingi176 – 1761Magnesium 3By similarity
Metal bindingi178 – 1781Magnesium 2; via carbonyl oxygenBy similarity
Metal bindingi179 – 1791Magnesium 3By similarity
Binding sitei287 – 2871SubstrateBy similarity
Binding sitei319 – 3191SubstrateBy similarity
Binding sitei337 – 3371SubstrateBy similarity
Binding sitei339 – 3391SubstrateBy similarity
Binding sitei349 – 3491SubstrateBy similarity
Metal bindingi355 – 3551Magnesium 3By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050ChloroplastAdd
BLAST
Chaini51 – 407357Fructose-1,6-bisphosphatase, chloroplasticPRO_0000008817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi203 ↔ 223

Keywords - PTMi

Disulfide bond

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

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi71 – 8010Combined sources
Helixi86 – 11227Combined sources
Turni113 – 1153Combined sources
Helixi127 – 14216Combined sources
Turni143 – 1464Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi172 – 1798Combined sources
Helixi184 – 1863Combined sources
Beta strandi190 – 1978Combined sources
Helixi218 – 22710Combined sources
Turni230 – 2323Combined sources
Beta strandi233 – 25422Combined sources
Beta strandi256 – 2627Combined sources
Turni263 – 2664Combined sources
Beta strandi267 – 2748Combined sources
Beta strandi282 – 2854Combined sources
Helixi288 – 2936Combined sources
Helixi296 – 30611Combined sources
Beta strandi310 – 3123Combined sources
Helixi323 – 33311Combined sources
Beta strandi336 – 3394Combined sources
Beta strandi343 – 3453Combined sources
Beta strandi349 – 3513Combined sources
Turni352 – 3554Combined sources
Helixi356 – 36510Combined sources
Beta strandi369 – 3768Combined sources
Helixi377 – 3793Combined sources
Beta strandi391 – 3944Combined sources
Helixi396 – 40611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 66-407.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46275.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni179 – 1824Substrate bindingBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821G → P in CAA48719 (PubMed:7764999).Curated
Sequence conflicti160 – 1601A → P in CAA48719 (PubMed:7764999).Curated
Sequence conflicti247 – 2471A → I in CAA48719 (PubMed:7764999).Curated
Sequence conflicti282 – 2821E → K in CAA48719 (PubMed:7764999).Curated

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
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. Positions 66-407.
ModBaseiSearch...
MobiDBiSearch...

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: September 7, 2016
This is version 96 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.