P46275 (F16P1_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-1,6-bisphosphatase, chloroplastic
Short name=FBPase
EC=3.1.3.11

Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase

Gene names

Name:

FBP

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	407 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	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Pathway	Carbohydrate biosynthesis; Calvin cycle.
Subunit structure	Homotetramer.
Subcellular location	Plastid › chloroplast stroma.
Induction	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.
Miscellaneous	In plants there are two FBPase isozymes: one in the cytosol and the other in the chloroplast.
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	3D-structure
Gene Ontology (GO)
Biological process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 50

50

Chloroplast

Chain

51 – 407

357

Fructose-1,6-bisphosphatase, chloroplastic

PRO_0000008817

Regions

Region

179 – 182

4

Substrate binding By similarity

Sites

Metal binding

126

1

Magnesium 1 By similarity

Metal binding

155

1

Magnesium 1 By similarity

Metal binding

155

1

Magnesium 2 By similarity

Metal binding

176

1

Magnesium 2 By similarity

Metal binding

176

1

Magnesium 3 By similarity

Metal binding

178

1

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

179

1

Magnesium 3 By similarity

Metal binding

355

1

Magnesium 3 By similarity

Binding site

287

1

Substrate By similarity

Binding site

319

1

Substrate By similarity

Binding site

337

1

Substrate By similarity

Binding site

339

1

Substrate By similarity

Binding site

349

1

Substrate By similarity

Amino acid modifications

Disulfide bond

203 ↔ 223

Experimental info

Sequence conflict

82

1

G → P in CAA48719. Ref.2

Sequence conflict

160

1

A → P in CAA48719. Ref.2

Sequence conflict

247

1

A → I in CAA48719. Ref.2

Sequence conflict

282

1

E → K in CAA48719. Ref.2

Secondary structure

1

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407

Helix Strand Turn

Details...

Helix

71 – 80

10

Helix

86 – 107

22

Helix

109 – 112

4

Turn

113 – 115

3

Helix

130 – 142

13

Turn

143 – 146

4

Beta strand

147 – 152

6

Beta strand

155 – 157

3

Beta strand

161 – 166

6

Beta strand

172 – 179

8

Turn

183 – 186

4

Beta strand

190 – 197

8

Helix

218 – 227

10

Turn

230 – 232

3

Beta strand

233 – 254

22

Beta strand

257 – 262

6

Turn

263 – 266

4

Beta strand

267 – 274

8

Beta strand

282 – 285

4

Helix

288 – 293

6

Helix

296 – 305

10

Beta strand

310 – 312

3

Helix

323 – 333

11

Beta strand

336 – 339

4

Beta strand

349 – 351

3

Turn

352 – 355

4

Helix

356 – 365

10

Beta strand

369 – 376

8

Helix

377 – 379

3

Beta strand

391 – 394

4

Helix

396 – 405

10

Sequences

	Sequence		Length	Mass (Da)
	P46275 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: B60E9164F1F6FE9D	FASTA	407	44,511
	10 20 30 40 50 60 MAAATASSQL IFSKPYSPSR LCPFQLCVFD AKSVLSSSRR KHVNGSGVRC MAVKEATSET 70 80 90 100 110 120 KKRSGYEIIT LTSWLLQQEQ KGIIDAELTI VLSSISMACK QIASLVQRAN ISNLTGTQGA 130 140 150 160 170 180 VNIQGEDQKK LDVISNEVFS NCLRSSGRTG IIASEEEDVA VAVEESYSGN YIVVFDPLDG 190 200 210 220 230 240 SSNLDAAVST GSIFGIYSPN DECLPDFGDD SDDNTLGTEE QRCIVNVCQP GSNLLAAGYC 250 260 270 280 290 300 MYSSSVAFVL TIGKGVFVFT LDPLYGEFVL TQENLQIPKS GEIYSFNEGN YKLWDENLKK 310 320 330 340 350 360 YIDDLKEPGP SGKPYSARYI GSLVGDFHRT LLYGGIYGYP RDKKSKNGKL RLLYECAPMS 370 380 390 400 FIVEQAGGKG SDGHQRVLDI QPTEIHQRVP LYIGSTEEVE KVEKYLA

References

[1]	"Nucleotide sequence analysis of a cDNA encoding chloroplastic fructose-1,6-bisphosphatase from pea (Pisum sativum l.)." Dong S.M., Rhim J.H., Hahn T.R. Plant Physiol. 107:313-314(1995) [PubMed: 7870839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Giant. Tissue: Leaf.
[2]	"Cloning, structure and expression of a pea cDNA clone coding for a photosynthetic fructose-1,6-bisphosphatase with some features different from those of the leaf chloroplast enzyme." Carrasco J.L., Chueca A., Prado F.E., Hermoso R., Lazaro J.J., Ramos J.L., Sahrawy M., Lopez Gorge J. Planta 193:494-501(1994) [PubMed: 7764999] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-407. Strain: cv. Lincoln. Tissue: Leaf.
[3]	"Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase." Chiadmi M., Navaza A., Miginiac-Maslow M., Jacquot J.-P., Cherfils J. EMBO J. 18:6809-6815(1999) [PubMed: 10581254] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-407.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L34806 mRNA. Translation: AAD10213.1.
X68826 mRNA. Translation: CAA48719.1.

PIR

S29560.
T06408.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D9Q	X-ray	2.40	A/B/C/D	51-407	[»]
1DBZ	X-ray	2.65	A/B/C/D	51-407	[»]
1DCU	X-ray	2.20	A/B/C/D	51-407	[»]

ProteinModelPortal

P46275.

SMR

P46275. Positions 66-407.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]

PANTHER

PTHR11556. In_FB_phphtase. 1 hit.

Pfam

PF00316. FBPase. 1 hit.
[Graphical view]

PIRSF

PIRSF000904. FBPtase_SBPase. 1 hit.

PRINTS

PR00115. F16BPHPHTASE.

PROSITE

PS00124. FBPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

F16P1_PEA

Accession

Primary (citable) accession number: P46275
Secondary accession number(s): Q37263

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1997
Last modified:	July 27, 2011
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program