[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Seedling; DOI=10.1007/BF00019100; PubMed=8980497 [NCBI, ExPASy, EBI, Israel, Japan] Martin W., Mustafa A.Z., Henze K., Schnarrenberger C.; "Higher-plant chloroplast and cytosolic fructose-1,6-bisphosphatase isoenzymes: origins via duplication rather than prokaryote-eukaryote divergence."; Plant Mol. Biol. 32:485-491(1996).
[2]	PROTEIN SEQUENCE OF 58-415. DOI=10.1016/0003-9861(90)90475-E; PubMed=2159755 [NCBI, ExPASy, EBI, Israel, Japan] Marcus F., Harrsch P.B.; "Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase."; Arch. Biochem. Biophys. 279:151-157(1990).
[3]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1021/bi00013a020; PubMed=7703244 [NCBI, ExPASy, EBI, Israel, Japan] Villeret V., Huang S., Zhang Y., Lipscomb W.N.; "Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography."; Biochemistry 34:4307-4315(1995).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
PATHWAY: Carbohydrate biosynthesis; Calvin cycle .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Plastid, chloroplast.
INDUCTION: Light activation through pH changes, Mg(2+) levels and also by light-modulated reduction of essential disulfide groups via the ferredoxin-thioredoxin f system.
MISCELLANEOUS: In plants there are two FBPase isozymes: one in the cytosol and the other in the chloroplast.
SIMILARITY: Belongs to the FBPase class 1 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L76555; AAD10207.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09085; T09085.

3D structure databases

PDB

1SPI; X-ray; 2.80 A; A/B/C/D=58-415.

[ExPASy / RCSB / EBI]

PDBsum

1SPI; -.

ModBase

P22418.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0042132;	Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity (inferred from electronic annotation from EC).
GO:0019253;	Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000146; In_FB_phphtase.
Graphical view of domain structure.

PANTHER

PTHR11556; In_FB_phphtase; 1.

Pfam

PF00316; FBPase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00115; FBPHPHTASE.
PR00377; INFBPHPHTASE.

ProDom

PD001491; In_FB_phphtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PS00124; FBPASE; 1.

Other

P22418; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calvin cycle; Carbohydrate metabolism; Chloroplast; Direct protein sequencing; Hydrolase; Plastid; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 57`	`57`	`Chloroplast.`
`CHAIN`	`58 415`	`358`	`Fructose-1,6-bisphosphatase, chloroplastic.`	`PRO_0000008818`
`REGION`	`207 232`	`26`	`Involved in light regulation (Potential).`
`ACT_SITE`	`357 357`		`By similarity.`
`DISULFID`	`231 236`		`Redox-active (light-modulated) (By similarity).`
`CONFLICT`	`66 66`		`E -> Q (in Ref. 2; AA sequence).`
`CONFLICT`	`88 88`		`E -> P (in Ref. 2; AA sequence).`
`CONFLICT`	`303 303`		`D -> P (in Ref. 2; AA sequence).`
`HELIX`	`80 86`	`7`
`HELIX`	`96 116`	`21`
`HELIX`	`140 142`	`3`
`HELIX`	`145 152`	`8`
`STRAND`	`158 162`	`5`
`STRAND`	`181 185`	`5`
`HELIX`	`190 193`	`4`
`STRAND`	`202 206`	`5`
`STRAND`	`239 260`	`22`
`STRAND`	`263 270`	`8`
`TURN`	`271 274`	`4`
`STRAND`	`275 282`	`8`
`STRAND`	`291 293`	`3`
`HELIX`	`296 298`	`3`
`HELIX`	`304 313`	`10`
`STRAND`	`317 320`	`4`
`HELIX`	`331 341`	`11`
`STRAND`	`344 347`	`4`
`STRAND`	`349 353`	`5`
`STRAND`	`356 359`	`4`
`TURN`	`360 363`	`4`
`HELIX`	`364 374`	`11`
`STRAND`	`377 388`	`12`
`STRAND`	`391 394`	`4`
`STRAND`	`399 402`	`4`
`HELIX`	`405 411`	`7`

Sequence information

Length: 415 AA [This is the length of the unprocessed precursor]

Molecular weight: 45230 Da [This is the MW of the unprocessed precursor]

CRC64: A23465129F54A5A1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASIGPATTT AVKLRSSIFN PQSSTLSPSQ QCITFTKSLH SFPTATRHNV ASGVRCMAAV 

        70         80         90        100        110        120 
GEAATETKAR TRSKYEIETL TGWLLKQEMA GVIDAELTIV LSSISLACKQ IASLVQRAGI 

       130        140        150        160        170        180 
SNLTGIQGAV NIQGEDQKKL DVVSNEVFSS CLRSSGRTGI IASEEEDVPV AVEESYSGNY 

       190        200        210        220        230        240 
IVVFDPLDGS SNIDAAVSTG SIFGIYSPND ECIVDSDHDD ESQLSAEEQR CVVNVCQPGD 

       250        260        270        280        290        300 
NLLAAGYCMY SSSVIFVLTI GKGVYAFTLD PMYGEFVLTS EKIQIPKAGK IYSFNEGNYK 

       310        320        330        340        350        360 
MWDDKLKKYM DDLKEPGESQ KPYSSRYIGS LVGDFHRTLL YGGIYGYPRD AKSKNGKLRL 

       370        380        390        400        410 
LYECAPMSFI VEQAGGKGSD GHQRILDIQP TEIHQRVPLY IGSVEEVEKL EKYLA

P22418 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools