[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00487a014; PubMed=2175647 [NCBI, ExPASy, EBI, Israel, Japan] Gibson J.L., Chen J.-H., Tower P.A., Tabita F.R.; "The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form part of a large operon in Rhodobacter sphaeroides: primary structure and insertional mutagenesis analysis."; Biochemistry 29:8085-8093(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. STRAIN=HR; PubMed=7961502 [NCBI, ExPASy, EBI, Israel, Japan] Xu H.H., Tabita F.R.; "Positive and negative regulation of sequences upstream of the form II cbb CO2 fixation operon of Rhodobacter sphaeroides."; J. Bacteriol. 176:7299-7308(1994).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
ENZYME REGULATION: Fructose-1,6-bisphosphatase II is not light-activated.
PATHWAY: Carbohydrate biosynthesis; Calvin cycle .
MISCELLANEOUS: There are two genes for FBPase in R.sphaeroides.
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

J02922; AAA26105.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U12430; AAA65078.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35819; A35819.

3D structure databases

HSSP

P46275; 1DBZ. [HSSP ENTRY / PDB]

ModBase

P22780.

Ontologies

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

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

Keywords

Calvin cycle; Carbohydrate metabolism; Hydrolase; Photosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 331`	`331`	`Fructose-1,6-bisphosphatase II.`	`PRO_0000200488`
`ACT_SITE`	`255 255`		`By similarity.`

Sequence information

Length: 331 AA [This is the length of the unprocessed precursor]

Molecular weight: 35256 Da [This is the MW of the unprocessed precursor]

CRC64: 500EB63E9BBECD13 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIELEDLGL SPDVADVMQR LARVGAGIAR IISRNGLERD LGAGVGTNAG GDGQKALDVI 

        70         80         90        100        110        120 
ADDAFRAALE GSAVAYYASE EQDEVVTLGE GSLALAIDPL DGSSNIDVNV SIGTIFSIFP 

       130        140        150        160        170        180 
AAAGPEASFL RPGTEQIAGG YIIYGPQCAL VCSFGQGVQH WVLDLDAGIF RRMPDIRPLP 

       190        200        210        220        230        240 
AETSEFAINA SNYRHWPQPI RAFVDDLVAG AEGPRGKNFN MRWIASLVAE THRILMRGGV 

       250        260        270        280        290        300 
FLYPGDERKG YERGRLRHVY ECAPIAFLIA NVGGGATDGC ADILTALPDR LHARTPFVFG 

       310        320        330 
CASKVARVAA YHDLACEETS ALFGSRGLFR S

P22780 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