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Protein

Sedoheptulose-1,7-bisphosphatase, chloroplastic

Gene

At3g55800

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271Magnesium 1Sequence analysis
Metal bindingi156 – 1561Magnesium 1Sequence analysis
Metal bindingi156 – 1561Magnesium 2Sequence analysis
Metal bindingi177 – 1771Magnesium 2Sequence analysis
Metal bindingi177 – 1771Magnesium 3Sequence analysis
Metal bindingi179 – 1791Magnesium 2; via carbonyl oxygenSequence analysis
Metal bindingi180 – 1801Magnesium 3Sequence analysis
Binding sitei291 – 2911SubstrateBy similarity
Binding sitei321 – 3211SubstrateBy similarity
Metal bindingi327 – 3271Magnesium 3By similarity

GO - Molecular functioni

  • fructose 1,6-bisphosphate 1-phosphatase activity Source: InterPro
  • 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
  • reductive pentose-phosphate cycle Source: TAIR
  • starch biosynthetic process Source: TAIR
  • sucrose biosynthetic 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: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

TAIRiAT3G55800.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5959ChloroplastSequence analysisAdd
BLAST
Chaini60 – 393334Sedoheptulose-1,7-bisphosphatase, chloroplasticPRO_0000008821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi116 ↔ 121Redox-active (light-modulated)Sequence analysis

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP46283.
PRIDEiP46283.
ProMEXiP46283.

2D gel databases

SWISS-2DPAGEP46283.
World-2DPAGE0003: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

GenevisibleiP46283. AT.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

BioGridi10062. 1 interaction.
IntActiP46283. 2 interactions.
STRINGi3702.AT3G55800.1.

Structurei

3D structure databases

ProteinModelPortaliP46283.
SMRiP46283. Positions 79-382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni180 – 1834Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
HOGENOMiHOG000191263.
InParanoidiP46283.
KOiK01100.
OMAiHEKSECY.
PhylomeDBiP46283.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR020548. Fructose_bisphosphatase_AS.
IPR023079. SBPase.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSiPR01958. S17BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451Q → R in AAM91137 (PubMed:14593172).Curated
Sequence conflicti145 – 1451Q → R in AAK96860 (PubMed:14593172).Curated

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_115438.3.
UniGeneiAt.21157.

Genome annotation databases

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

Cross-referencesi

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_115438.3.
UniGeneiAt.21157.

3D structure databases

ProteinModelPortaliP46283.
SMRiP46283. Positions 79-382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10062. 1 interaction.
IntActiP46283. 2 interactions.
STRINGi3702.AT3G55800.1.

PTM databases

iPTMnetiP46283.

2D gel databases

SWISS-2DPAGEP46283.
World-2DPAGE0003:P46283.

Proteomic databases

PaxDbiP46283.
PRIDEiP46283.
ProMEXiP46283.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G55800.

Phylogenomic databases

eggNOGiKOG1458. Eukaryota.
COG0158. LUCA.
HOGENOMiHOG000191263.
InParanoidiP46283.
KOiK01100.
OMAiHEKSECY.
PhylomeDBiP46283.

Enzyme and pathway databases

UniPathwayiUPA00116.
BioCyciARA:AT3G55800-MONOMER.

Miscellaneous databases

PROiP46283.

Gene expression databases

GenevisibleiP46283. AT.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR020548. Fructose_bisphosphatase_AS.
IPR023079. SBPase.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSiPR01958. S17BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the Arabidopsis thaliana sedoheptulose-1,7-biphosphatase gene and expression studies in wheat and Arabidopsis thaliana."
    Willingham N.M., Lloyd J.C., Raines C.A.
    Plant Mol. Biol. 26:1191-1200(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. C24 and cv. Landsberg erecta.
    Tissue: Leaf.
  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.

Entry informationi

Entry nameiS17P_ARATH
AccessioniPrimary (citable) accession number: P46283
Secondary accession number(s): Q940F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.