NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ismej.2007.46; PubMed=18059494 [NCBI, ExPASy, EBI, Israel, Japan]
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses.";
ISME J. 1:703-713(2007).

Comments

FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-phosphate and sedoheptulose 7-phosphate, respectively (By similarity).
CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
CATALYTIC ACTIVITY: Sedoheptulose 1,7-bisphosphate + H₂O = sedoheptulose 7-phosphate + phosphate.
PATHWAY: Carbohydrate biosynthesis; Calvin cycle .
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the FBPase class 2 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

CP000239; ABC98759.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_474022.1; -.

3D structure databases

ModBase

Q2JWU7.

Ontologies

GO:0042132;	Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity (inferred from electronic annotation from EC).
GO:0050278;	Molecular function: sedoheptulose-bisphosphatase activity (inferred from electronic annotation from EC).
GO:0006071;	Biological process: glycerol metabolic process (inferred from electronic annotation from InterPro).
GO:0019253;	Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR004464; GlpX.
Graphical view of domain structure.

Pfam

PF03320; FBPase_glpX; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF004532; GlpX; 1.

ProDom

PD007014; GlpX; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00330; glpX; 1.

ProtoNet

Q2JWU7.

Genome annotation databases

GeneID

3897417; -.

GenomeReviews

CP000239_GR; CYA_0542.

KEGG

cya:CYA_0542; -.

TIGR

CYA_0542; -.

Other

UniRef

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

Keywords

Calvin cycle; Carbohydrate metabolism; Complete proteome; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 347`	`347`		`D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase.`	`PRO_0000342731`

Sequence information

Length: 347 AA [This is the length of the unprocessed precursor]

Molecular weight: 37716 Da [This is the MW of the unprocessed precursor]

CRC64: 79495F4F197169C1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDNKLGLEII EVVEQAAIAA ARWMGKGDNK TADQVAVEAM REKLNQIPMR GRIVIGEGTR 

        70         80         90        100        110        120 
DEAPMLYIGE EVGICTRPDA EQFCRVEELV EIDIAVDPCE GTNLVAKGQN GSMAVLAISE 

       130        140        150        160        170        180 
KGGLLHAPDI YMQKLAAPPQ AKGKVHLDYP PEKNLQIIAE SLDREVSDLT VVVMDRKRHV 

       190        200        210        220        230        240 
DLIRQIREAG ARVKLITDGD ISAALSAGFN GTGIHALMGI GAAPEGVISA AALRCLGAHF 

       250        260        270        280        290        300 
QGRLIYDPEV VQAGTYLPPV EETRRQLKEQ GIEDPDKVWE CEELASGKEV LFAATGITDG 

       310        320        330        340 
DLMRGVRFFG GGARTETLVI SSQSRTVRFV DTIHMKDGQQ PRSLQLR

Q2JWU7 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