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Protein

Sedoheptulose-1,7-bisphosphatase, chloroplastic

Gene

At3g55800

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate.

Cofactori

Mg2+CuratedNote: Binds 3 Mg2+ ions per subunit.Curated

Enzyme regulationi

In continuous light, by inorganic phosphate, sed7P, glycerate and ribulose 1,5-bisphosphate.

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 bindingi127Magnesium 1Sequence analysis1
Metal bindingi156Magnesium 1Sequence analysis1
Metal bindingi156Magnesium 2Sequence analysis1
Metal bindingi177Magnesium 2Sequence analysis1
Metal bindingi177Magnesium 3Sequence analysis1
Metal bindingi179Magnesium 2; via carbonyl oxygenSequence analysis1
Metal bindingi180Magnesium 3Sequence analysis1
Binding sitei291SubstrateBy similarity1
Binding sitei321SubstrateBy similarity1
Metal bindingi327Magnesium 3By similarity1

GO - Molecular functioni

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

GO - Biological processi

  • carbohydrate biosynthetic process Source: TAIR
  • defense response to bacterium Source: TAIR
  • fructose 1,6-bisphosphate metabolic process Source: GO_Central
  • fructose 6-phosphate metabolic process Source: GO_Central
  • fructose metabolic process Source: GO_Central
  • gluconeogenesis Source: GO_Central
  • reductive pentose-phosphate cycle Source: TAIR
  • starch biosynthetic process Source: TAIR
  • sucrose biosynthetic process Source: TAIR

Keywordsi

Molecular functionHydrolase
Biological processCalvin cycle, Carbohydrate metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G55800-MONOMER
UniPathwayiUPA00116

Names & Taxonomyi

Protein namesi
Recommended name:
Sedoheptulose-1,7-bisphosphatase, chloroplastic (EC:3.1.3.37)
Alternative name(s):
SED(1,7)P2ase
Sedoheptulose bisphosphatase
Short name:
SBPase
Gene namesi
Ordered Locus Names:At3g55800
ORF Names:F1I16_210
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

AraportiAT3G55800
TAIRilocus:2078941 AT3G55800

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 74ChloroplastCuratedAdd BLAST74
ChainiPRO_000000882175 – 393Sedoheptulose-1,7-bisphosphatase, chloroplasticAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi116 ↔ 121Redox-active (light-modulated)Sequence analysis

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP46283
PRIDEiP46283
ProMEXiP46283

2D gel databases

SWISS-2DPAGEiP46283
World-2DPAGEi0003:P46283

PTM databases

iPTMnetiP46283

Expressioni

Tissue specificityi

Expressed in all tissues examined except root. Highest levels found in leaves and flowers.

Inductioni

Light activation through pH changes, Mg2+ levels and also by light-modulated reduction of essential disulfide groups via the ferredoxin-thioredoxin f system. In etiolated seedlings, induction occurs only after 8 hours of illumination.

Gene expression databases

ExpressionAtlasiP46283 baseline and differential
GenevisibleiP46283 AT

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

BioGridi10062, 1 interactor
IntActiP46283, 2 interactors
STRINGi3702.AT3G55800.1

Structurei

3D structure databases

ProteinModelPortaliP46283
SMRiP46283
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni180 – 183Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1458 Eukaryota
COG0158 LUCA
HOGENOMiHOG000191263
InParanoidiP46283
KOiK01100
OMAiNWTVGTI
OrthoDBiEOG09360B47
PhylomeDBiP46283

Family and domain databases

CDDicd00354 FBPase, 1 hit
HAMAPiMF_01855 FBPase_class1, 1 hit
InterProiView protein in InterPro
IPR000146 FBPase_class-1
IPR033391 FBPase_N
IPR020548 Fructose_bisphosphatase_AS
IPR023079 SBPase
PANTHERiPTHR11556 PTHR11556, 1 hit
PfamiView protein in Pfam
PF00316 FBPase, 1 hit
PIRSFiPIRSF000904 FBPtase_SBPase, 1 hit
PRINTSiPR01958 S17BPHPHTASE
PROSITEiView protein in PROSITE
PS00124 FBPASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

P46283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METSIACYSR GILPPSVSSQ RSSTLVSPPS YSTSSSFKRL KSSSIFGDSL
60 70 80 90 100
RLAPKSQLKA TKAKSNGAST VTKCEIGQSL EEFLAQATPD KGLRTLLMCM
110 120 130 140 150
GEALRTIAFK VRTASCGGTA CVNSFGDEQL AVDMLADKLL FEALQYSHVC
160 170 180 190 200
KYACSEEVPE LQDMGGPVEG GFSVAFDPLD GSSIVDTNFT VGTIFGVWPG
210 220 230 240 250
DKLTGITGGD QVAAAMGIYG PRTTYVLAVK GFPGTHEFLL LDEGKWQHVK
260 270 280 290 300
ETTEIAEGKM FSPGNLRATF DNSEYSKLID YYVKEKYTLR YTGGMVPDVN
310 320 330 340 350
QIIVKEKGIF TNVTSPTAKA KLRLLFEVAP LGLLIENAGG FSSDGHKSVL
360 370 380 390
DKTIINLDDR TQVAYGSKNE IIRFEETLYG TSRLKNVPIG VTA
Length:393
Mass (Da):42,414
Last modified:November 1, 1995 - v1
Checksum:iED398496A7357345
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145Q → R in AAM91137 (PubMed:14593172).Curated1
Sequence conflicti145Q → R in AAK96860 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74719 Genomic DNA Translation: AAB33001.1
AL161667 Genomic DNA Translation: CAB81605.1
CP002686 Genomic DNA Translation: AEE79443.1
AY054669 mRNA Translation: AAK96860.1
AY128737 mRNA Translation: AAM91137.1
PIRiS51838
RefSeqiNP_191139.1, NM_115438.4
UniGeneiAt.21157

Genome annotation databases

EnsemblPlantsiAT3G55800.1; AT3G55800.1; AT3G55800
GeneIDi824746
GrameneiAT3G55800.1; AT3G55800.1; AT3G55800
KEGGiath:AT3G55800

Similar proteinsi

Entry informationi

Entry nameiS17P_ARATH
AccessioniPrimary (citable) accession number: P46283
Secondary accession number(s): Q940F8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 25, 2018
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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