Reviewed, UniProtKB/Swiss-Prot P09195 (F16P1_WHEAT)

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

Triticum aestivum (Wheat)

Taxonomic identifier

4565 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Subcellular location	Plastid › chloroplast.
Tissue specificity	In photosynthetically active tissues, and in the shoot and root apical meristems. Ref.2
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
Gene Ontology (GO)
Biological process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC magnesium 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 – 49	49	Chloroplast Potential
	Chain	50 – 409	360	Fructose-1,6-bisphosphatase, chloroplastic		PRO_0000008820
Regions
	Region	184 – 187	4	Substrate binding By similarity
Sites
	Metal binding	131	1	Magnesium 1 By similarity
	Metal binding	160	1	Magnesium 1 By similarity
	Metal binding	160	1	Magnesium 2 By similarity
	Metal binding	181	1	Magnesium 2 By similarity
	Metal binding	181	1	Magnesium 3 By similarity
	Metal binding	183	1	Magnesium 2; via carbonyl oxygen By similarity
	Metal binding	184	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	223 ↔ 228		Redox-active (light-modulated) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P09195-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 607ECCC0B5E66745	FASTA	409	44,218
	10 20 30 40 50 60 MAAATTTTSR PLLLSRQQAA ASSLQCRLPR RPGSSLFAGQ GQASTPNVRC MAVVDTASAP 70 80 90 100 110 120 APAAARKRSS YDMITLTTWL LKQEQEGVID NEMTIVLSSI STACKQIASL VQRAPISNLT 130 140 150 160 170 180 GVQGATNVQG EDQKKLDVIS NEVFSNCLRW SGRTGVIASE EEDVPVAVEE SYSGNYIVVF 190 200 210 220 230 240 DPLDGSSNID AAVSTGSIFG IYSPSDECHI GDDATLDEVT QMCIVNVCQP GSNLLAAGYC 250 260 270 280 290 300 MYSSSVIFVL TIGTGVYVFT LDPMYGEFVL TQEKVQIPKS GKIYSFNEGN YALWDDKLKK 310 320 330 340 350 360 YMDSLKEPGT SGKPYSARYI GSLVGDFHRT MLYGGIYGYP SDQKSKNGKL RLLYECAPMS 370 380 390 400 FIAEQAGGKG SDGHQRVLDI MPTAVHQRVP LYVGSVEEVE KVEKFLSSE

References

[1]	"Chloroplast fructose-1,6-bisphosphatase: the product of a mosaic gene." Raines C.A., Lloyd J.C., Longstaff M., Bradley D., Dyer T.A. Nucleic Acids Res. 16:7931-7942(1988) [PubMed: 2843806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY LIGHT. Strain: cv. Mardler.
[2]	"The chloroplast FBPase gene of wheat: structure and expression of the promoter in photosynthetic and meristematic cells of transgenic tobacco plants." Lloyd J.C., Raines C.A., John U.P., Dyer T.A. Mol. Gen. Genet. 225:209-216(1991) [PubMed: 1848650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: cv. Chinese Spring. Tissue: Etiolated shoot.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X07780 mRNA. Translation: CAA30612.1. X53957 Genomic DNA. Translation: CAA37908.1.
PIR	PAWTF. S14060.
UniGene	Ta.439
3D structure databases
HSSP	HSSP built from PDB template 1D9Q based on UniProtKB P46275.
SMR	P09195. Positions 71-407.
ModBase	Search...
Organism-specific databases
Gramene	P09195.
Enzyme and pathway databases
BRENDA	3.1.3.11. 253.
Family and domain databases
InterPro	IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. F16BPHPHTASE.
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

F16P1_WHEAT

Accession

Primary (citable) accession number: P09195

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	September 22, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)