NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of Synechococcus sp. CC9605.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.

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

CP000110; ABB35008.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_381563.1; -.

3D structure databases

ModBase

Q3AK74.

Enzyme and pathway databases

BioCyc

SSP1131:SYNCC9605_1253-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: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

Q3AK74.

Genome annotation databases

GeneID

3736457; -.

GenomeReviews

CP000110_GR; Syncc9605_1253.

KEGG

syd:Syncc9605_1253; -.

NMPDR

fig|110662.3.peg.222; -.

CMR

Q3AK74; Syncc9605_1253.

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`	`1 334`	`334`		`D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase.`	`PRO_0000342728`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 35307 Da [This is the MW of the unprocessed precursor]

CRC64: BB2C4102553FE7A2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDQTLIQEIL EIVEQAAIAS ASLSGKGLKD EADALAVDAM RKRMNQIQMQ GRIVIGEGER 

        70         80         90        100        110        120 
DEAPMLYIGE EVGTGTGPGV DFAVDPCEGT NLCAFNQRGS MAVLAASDRG GLFNAPDFYM 

       130        140        150        160        170        180 
KKLAAPPAAK GKVDIRKSAT ENIKILSECL GLPVDELNIV VMDRARHKDL IAEIRGTGAR 

       190        200        210        220        230        240 
IQPISDGDVQ AAIACGFAGT GTHCLMGIGA APEGVISAAA MRALGGHFQG QLVYDPAIAQ 

       250        260        270        280        290        300 
TSEWADMTKE GNLARLAEMG IADPDKVYEA EELACGEHVC FAGSGITDGL LFNGVKFEKD 

       310        320        330 
CTRTSSLVIS NLDNTCRFTN TVHIKEDAQS IALS

Q3AK74 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