NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1907281 [NCBI, ExPASy, EBI, Israel, Japan]
Gibson J.L., Falcone D.L., Tabita F.R.;
"Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides.";
J. Biol. Chem. 266:14646-14653(1991).

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

M64624; AAA26112.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40767; PARFAS.

3D structure databases

HSSP

P46275; 1DBZ. [HSSP ENTRY / PDB]

ModBase

P27994.

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`	`1 333`	`333`	`Fructose-1,6-bisphosphatase I.`	`PRO_0000200487`
`ACT_SITE`	`257 257`		`By similarity.`

Sequence information

Length: 333 AA [This is the length of the unprocessed precursor]

Molecular weight: 35997 Da [This is the MW of the unprocessed precursor]

CRC64: 7274A0D4C8FC8426 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPFPTHPDA IPAELQDVMD RLGSVAIEVA NRIARGGIDE DLAGLCGTNT DGDGQKALDV 

        70         80         90        100        110        120 
IADDAFRVAL EGSAVRFYAS EEQDTAVTLN EAGTLALAID PLDGSSNIDT NLSVGTTFAI 

       130        140        150        160        170        180 
WPAAPRPNPS FLRLGSELIA AGYVIYGPQV CMMVSFGKGT QKYVLDPGSR SFVLVDRAVK 

       190        200        210        220        230        240 
VPPSSTEFAI NASNYRHWPK PIRAYIDDCV AGTEGPRGRN FNMRWLASLV AETHRILARG 

       250        260        270        280        290        300 
GVFLYPRDSR KGYEQGRLRY LYECAPIAFV ITQAGGGATD GENPILGQTP SRLHARTPFV 

       310        320        330 
FGSAEKVARI TAYHDLPEQE TSALFGNRGL FRS

P27994 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