Reviewed, UniProtKB/Swiss-Prot P46283 (S17P_ARATH)

Names and origin

Protein names

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 names

Ordered Locus Names:	At3g55800
ORF Names:	F1I16_210

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Calvin cycle Carbohydrate metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from expression pattern. Source: TAIR reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW starch biosynthetic process Inferred from direct assay. Source: TAIR sucrose biosynthetic process Inferred from direct assay. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR thylakoid Inferred from direct assay. Source: TAIR
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct sedoheptulose-bisphosphatase activity Inferred from mutant phenotype. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P93397	2	EBI-449184,EBI-1750986	From a different organism.
TRX3	Q42403	1	EBI-449184,EBI-449157

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 393		Sedoheptulose-1,7-bisphosphatase, chloroplastic		PRO_0000008821
Regions
	Region	180 – 183	4	Substrate binding By similarity
Sites
	Metal binding	127	1	Magnesium 1 Potential
	Metal binding	156	1	Magnesium 1 Potential
	Metal binding	156	1	Magnesium 2 Potential
	Metal binding	177	1	Magnesium 2 Potential
	Metal binding	177	1	Magnesium 3 Potential
	Metal binding	179	1	Magnesium 2; via carbonyl oxygen Potential
	Metal binding	180	1	Magnesium 3 Potential
	Metal binding	327	1	Magnesium 3 By similarity
	Binding site	291	1	Substrate By similarity
	Binding site	321	1	Substrate By similarity
Amino acid modifications
	Disulfide bond	116 ↔ 121		Redox-active (light-modulated) Potential

Sequences

	Sequence		Length	Mass (Da)
	P46283-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: ED398496A7357345	FASTA	393	42,414
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S74719 Genomic DNA. Translation: AAB33001.1. AL161667 Genomic DNA. Translation: CAB81605.1.
IPI	IPI00544876.
PIR	S51838.
RefSeq	NP_191139.1.
UniGene	At.21157
3D structure databases
HSSP	HSSP built from PDB template 1FJ9 based on UniProtKB P00636.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46283. 2 interactions.
2-D gel databases
SWISS-2DPAGE	P46283.
Proteomic databases
PRIDE	P46283.
ProMEX	P46283.
Genome annotation databases
GeneID	824746.
GenomeReviews	Gene locus AT3G55800 in contig BA000014_GR.
KEGG	ath:AT3G55800.
NMPDR	fig|3702.1.peg.16902.
Organism-specific databases
TAIR	At3g55800.
Phylogenomic databases
OMA	P46283. HANIVIE.
Enzyme and pathway databases
BRENDA	3.1.3.37. 302.
Gene expression databases
GermOnline	AT3G55800. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000146. Fructose_bisphosphatase. IPR017955. IMPase/FBPase. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. FBPHPHTASE. PR00377. INFBPHPHTASE.
ProDom	PD001491. In_FB_phphtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

S17P_ARATH

Accession

Primary (citable) accession number: P46283

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)