Skip Header

Contribute Send feedback
Read comments (?) or add your own

P46283 (S17P_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sedoheptulose-1,7-bisphosphatase, chloroplastic
EC=3.1.3.37
Alternative name(s):
SED(1,7)P2ase
Sedoheptulose bisphosphatase
Short name=SBPase
Gene names
Ordered Locus Names:At3g55800
ORF Names:F1I16_210
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 3 magnesium ions per subunit Potential.

Enzyme regulation

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

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Homodimer Potential.

Subcellular location

Plastid › chloroplast.

Tissue specificity

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

Induction

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.

Sequence similarities

Belongs to the FBPase class 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5959Chloroplast Potential
Chain60 – 393334Sedoheptulose-1,7-bisphosphatase, chloroplastic
PRO_0000008821

Regions

Region180 – 1834Substrate binding By similarity

Sites

Metal binding1271Magnesium 1 Potential
Metal binding1561Magnesium 1 Potential
Metal binding1561Magnesium 2 Potential
Metal binding1771Magnesium 2 Potential
Metal binding1771Magnesium 3 Potential
Metal binding1791Magnesium 2; via carbonyl oxygen Potential
Metal binding1801Magnesium 3 Potential
Metal binding3271Magnesium 3 By similarity
Binding site2911Substrate By similarity
Binding site3211Substrate By similarity

Amino acid modifications

Disulfide bond116 ↔ 121Redox-active (light-modulated) Potential

Experimental info

Sequence conflict1451Q → R in AAM91137. Ref.4
Sequence conflict1451Q → R in AAK96860. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P46283 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: ED398496A7357345

FASTA39342,414
        10         20         30         40         50         60 
METSIACYSR GILPPSVSSQ RSSTLVSPPS YSTSSSFKRL KSSSIFGDSL RLAPKSQLKA 

        70         80         90        100        110        120 
TKAKSNGAST VTKCEIGQSL EEFLAQATPD KGLRTLLMCM GEALRTIAFK VRTASCGGTA 

       130        140        150        160        170        180 
CVNSFGDEQL AVDMLADKLL FEALQYSHVC KYACSEEVPE LQDMGGPVEG GFSVAFDPLD 

       190        200        210        220        230        240 
GSSIVDTNFT VGTIFGVWPG DKLTGITGGD QVAAAMGIYG PRTTYVLAVK GFPGTHEFLL 

       250        260        270        280        290        300 
LDEGKWQHVK ETTEIAEGKM FSPGNLRATF DNSEYSKLID YYVKEKYTLR YTGGMVPDVN 

       310        320        330        340        350        360 
QIIVKEKGIF TNVTSPTAKA KLRLLFEVAP LGLLIENAGG FSSDGHKSVL DKTIINLDDR 

       370        380        390 
TQVAYGSKNE IIRFEETLYG TSRLKNVPIG VTA

« Hide

References

« Hide 'large scale' references
[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: 7811976] [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. expand/collapse author list , 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: 11130713] [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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00544876.
PIRS51838.
RefSeqNP_191139.1. NM_115438.3.
UniGeneAt.21157.

3D structure databases

ProteinModelPortalP46283.
SMRP46283. Positions 72-381.
ModBaseSearch...

Protein-protein interaction databases

IntActP46283. 2 interactions.
STRINGP46283.

2D gel databases

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

Proteomic databases

PRIDEP46283.
ProMEXP46283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G55800.1; AT3G55800.1; AT3G55800.
GeneID824746.
GenomeReviewsGene locus AT3G55800 in contig BA000014_GR.
KEGGath:AT3G55800.
NMPDRfig|3702.1.peg.16902.

Organism-specific databases

TAIRAt3g55800.

Phylogenomic databases

eggNOGKOG1458.
HOGENOMHBG731261.
InParanoidP46283.
OMAHANIVIE.
PhylomeDBP46283.
ProtClustDBPLN02462.

Gene expression databases

GenevestigatorP46283.
GermOnlineAT3G55800. Arabidopsis thaliana.

Family and domain databases

InterProIPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
IPR023079. SBPase.
[Graphical view]
KOK01100.
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR01958. S17BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameS17P_ARATH
AccessionPrimary (citable) accession number: P46283
Secondary accession number(s): Q940F8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents