NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PCC 7421;
DOI=10.1093/dnares/10.4.137; PubMed=14621292 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids.";
DNA Res. 10:137-145(2003).

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

BA000045; BAC91283.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_926288.1; -.

3D structure databases

ModBase

Q7NG31.

Enzyme and pathway databases

BioCyc

GVIO251221:GLR3342-MON; -.

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: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]

TIGR00330; glpX; 1.

Genome annotation databases

GeneID

2601745; -.

GenomeReviews

BA000045_GR; glr3342.

KEGG

gvi:glr3342; -.

NMPDR

fig|251221.1.peg.3342; -.

CMR

Q7NG31; glr3342.

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`	`1 346`	`346`		`D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase.`	`PRO_0000342711`

Sequence information

Length: 346 AA [This is the length of the unprocessed precursor]

Molecular weight: 37030 Da [This is the MW of the unprocessed precursor]

CRC64: 6E6D758437BF68CD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKTLGLEII EVVEQAAIAS ARLMGKGLRN EADGVAVKAM RDRMNQIYMR GRIVIGEGER 

        70         80         90        100        110        120 
DDAPMLYIGE QVGICTQPNA AQMCSIDELL EIDIAVDPCE GTNLVAEGRQ GSMAVLAISE 

       130        140        150        160        170        180 
KGGLLGAPDL YMKKLAAPPQ AKGKVHIDYP ATKNLQIIAE CLDRAIEDLV VIVMKRDRHK 

       190        200        210        220        230        240 
DLISEIRSTG ARVRFIDDGD ISAALSAGIN GTGVHALMGI GAAPEGVISA AALRCLGSHF 

       250        260        270        280        290        300 
QGQLIYDPDV VQTGLLKGTK AEIEEQLKAQ GVEQPDKVWE AEELASGKNV LFAACGITDG 

       310        320        330        340 
DFIKGVRFFT GSARTETMVI SSQSNTVRFV DTVHILDPAH HASLVI

Q7NG31 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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