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Protein

Fructose-1,6-bisphosphatase, chloroplastic

Gene

FBP

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 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 bindingi138 – 1381Magnesium 1By similarity
Metal bindingi167 – 1671Magnesium 1By similarity
Metal bindingi167 – 1671Magnesium 2By similarity
Metal bindingi188 – 1881Magnesium 2By similarity
Metal bindingi188 – 1881Magnesium 3By similarity
Metal bindingi190 – 1901Magnesium 2; via carbonyl oxygenBy similarity
Metal bindingi191 – 1911Magnesium 3By similarity
Binding sitei297 – 2971SubstrateBy similarity
Binding sitei329 – 3291SubstrateBy similarity
Binding sitei347 – 3471SubstrateBy similarity
Binding sitei349 – 3491SubstrateBy similarity
Binding sitei359 – 3591SubstrateBy similarity
Metal bindingi365 – 3651Magnesium 3By similarity

GO - Molecular functioni

  • fructose 1,6-bisphosphate 1-phosphatase activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • fructose 1,6-bisphosphate metabolic process Source: TAIR
  • photosynthesis Source: TAIR
  • photosynthetic electron transport in photosystem I Source: TAIR
  • reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
  • response to cold Source: TAIR
  • response to cytokinin Source: TAIR
  • sucrose metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calvin cycle, Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G54050-MONOMER.
ARA:GQT-118-MONOMER.
MetaCyc:AT3G54050-WS-MONOMER.
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
Ordered Locus Names:At3g54050
ORF Names:F24B22.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G54050.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • stromule Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5959ChloroplastSequence analysisCombined sourcesAdd
BLAST
Chaini60 – 417358Fructose-1,6-bisphosphatase, chloroplasticPRO_0000008814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N-acetylalanineCombined sources
Disulfide bondi233 ↔ 238Redox-active (light-modulated)By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP25851.
PRIDEiP25851.

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

Gene expression databases

GenevisibleiP25851. AT.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi9889. 2 interactions.
IntActiP25851. 1 interaction.
STRINGi3702.AT3G54050.1.

Structurei

3D structure databases

ProteinModelPortaliP25851.
SMRiP25851. Positions 78-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
HOGENOMiHOG000191265.
InParanoidiP25851.
KOiK03841.
OMAiYTTRYIG.
PhylomeDBiP25851.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
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.

P25851-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAATTTS SHLLLSSSRH VASSSQPSIL SPRSLFSNNG KRAPTGVRNH
60 70 80 90 100
QYASGVRCMA VAADAAETKT AARKKSGYEL QTLTGWLLRQ EMKGEIDAEL
110 120 130 140 150
TIVMSSISLA CKQIASLVQR AGISNLTGVQ GAVNIQGEDQ KKLDVISNEV
160 170 180 190 200
FSNCLRSSGR TGIIASEEED VPVAVEESYS GNYVVVFDPL DGSSNIDAAV
210 220 230 240 250
STGSIFGIYS PNDECIVDDS DDISALGSEE QRCIVNVCQP GNNLLAAGYC
260 270 280 290 300
MYSSSVIFVL TLGKGVFSFT LDPMYGEFVL TQENIEIPKA GRIYSFNEGN
310 320 330 340 350
YQMWDDKLKK YIDDLKDPGP TGKPYSARYI GSLVGDFHRT LLYGGIYGYP
360 370 380 390 400
RDAKSKNGKL RLLYECAPMS FIVEQAGGKG SDGHSRVLDI QPTEIHQRVP
410
LYIGSTEEVE KLEKYLA
Length:417
Mass (Da):45,162
Last modified:June 6, 2002 - v2
Checksum:iCEB17F65468746D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → S in CAA41154 (PubMed:1651131).Curated
Sequence conflicti66 – 661A → S in CAA41154 (PubMed:1651131).Curated
Sequence conflicti133 – 1331V → I in CAA41154 (PubMed:1651131).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58148 mRNA. Translation: CAA41154.1.
AL132957 Genomic DNA. Translation: CAB70979.1.
CP002686 Genomic DNA. Translation: AEE79179.1.
CP002686 Genomic DNA. Translation: AEE79180.1.
AF428326 mRNA. Translation: AAL16256.1.
AY039934 mRNA. Translation: AAK64038.1.
AY150450 mRNA. Translation: AAN12891.1.
BT000743 mRNA. Translation: AAN31884.1.
PIRiS16582.
T47564.
RefSeqiNP_001190083.1. NM_001203154.1.
NP_190973.1. NM_115265.4.
UniGeneiAt.22619.
At.51003.

Genome annotation databases

EnsemblPlantsiAT3G54050.1; AT3G54050.1; AT3G54050.
AT3G54050.2; AT3G54050.2; AT3G54050.
GeneIDi824572.
GrameneiAT3G54050.1; AT3G54050.1; AT3G54050.
AT3G54050.2; AT3G54050.2; AT3G54050.
KEGGiath:AT3G54050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58148 mRNA. Translation: CAA41154.1.
AL132957 Genomic DNA. Translation: CAB70979.1.
CP002686 Genomic DNA. Translation: AEE79179.1.
CP002686 Genomic DNA. Translation: AEE79180.1.
AF428326 mRNA. Translation: AAL16256.1.
AY039934 mRNA. Translation: AAK64038.1.
AY150450 mRNA. Translation: AAN12891.1.
BT000743 mRNA. Translation: AAN31884.1.
PIRiS16582.
T47564.
RefSeqiNP_001190083.1. NM_001203154.1.
NP_190973.1. NM_115265.4.
UniGeneiAt.22619.
At.51003.

3D structure databases

ProteinModelPortaliP25851.
SMRiP25851. Positions 78-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9889. 2 interactions.
IntActiP25851. 1 interaction.
STRINGi3702.AT3G54050.1.

Proteomic databases

PaxDbiP25851.
PRIDEiP25851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G54050.1; AT3G54050.1; AT3G54050.
AT3G54050.2; AT3G54050.2; AT3G54050.
GeneIDi824572.
GrameneiAT3G54050.1; AT3G54050.1; AT3G54050.
AT3G54050.2; AT3G54050.2; AT3G54050.
KEGGiath:AT3G54050.

Organism-specific databases

TAIRiAT3G54050.

Phylogenomic databases

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
HOGENOMiHOG000191265.
InParanoidiP25851.
KOiK03841.
OMAiYTTRYIG.
PhylomeDBiP25851.

Enzyme and pathway databases

UniPathwayiUPA00116.
BioCyciARA:AT3G54050-MONOMER.
ARA:GQT-118-MONOMER.
MetaCyc:AT3G54050-WS-MONOMER.

Miscellaneous databases

PROiP25851.

Gene expression databases

GenevisibleiP25851. AT.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA clone encoding chloroplast fructose-1,6-bisphosphatase from Arabidopsis thaliana."
    Horsnell P.R., Raines C.A.
    Plant Mol. Biol. 17:185-186(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-60, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER MET-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF16P1_ARATH
AccessioniPrimary (citable) accession number: P25851
Secondary accession number(s): Q9M398
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 6, 2002
Last modified: July 6, 2016
This is version 132 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.