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Reviewed, UniProtKB/Swiss-Prot A4WW38 (F16A1_RHOS5)

Last modified November 3, 2009. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fructose-1,6-bisphosphatase class 1 1
      Short name=FBPase class 1 1
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 1
Gene names
Name: fbp1
Ordered Locus Names: Rsph17025_2715
OrganismRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP]
Taxonomic identifier349102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. HAMAP MF_01855

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Pathway

Carbohydrate biosynthesis; Calvin cycle. HAMAP MF_01855

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the FBPase class 1 family.

Ontologies

Keywords
   Biological processCalvin cycle
Carbohydrate metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processreductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionfructose 1,6-bisphosphate 1-phosphatase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855
PRO_0000364668

Regions

Region103 – 1064Substrate binding By similarity

Sites

Metal binding811Magnesium 1 By similarity
Metal binding1001Magnesium 1 By similarity
Metal binding1001Magnesium 2 By similarity
Metal binding1021Magnesium 1; via carbonyl oxygen By similarity
Metal binding1031Magnesium 2 By similarity
Metal binding2631Magnesium 2 By similarity
Binding site1911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WW38-1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: DA12E6B8F7D6F247

FASTA33335,775
        10         20         30         40         50         60 
MKPFATHPDA IPADLQDVMD RLGSVAIEVA TRIARGGIDE DLAGLCGTNT DGDGQKALDV 

        70         80         90        100        110        120 
IADDAFRAAL EGSAVRFYAS EEQEEAVTLN EAGTLALAID PLDGSSNIDT NLSVGTIFAI 

       130        140        150        160        170        180 
WPAAATAETS FLRPGSDLIA GGYIIYGPQV CLMVSFGQGT QKYVLDPGSR SFVLVDRAVK 

       190        200        210        220        230        240 
VPPASTEFAI NASNYRHWSK PIRAYIDDCV AGTEGPRGRN FNMRWLASLV AETHRILARG 

       250        260        270        280        290        300 
GVFLYPRDGR KGYEQGRLRY LYECAPIAFV ITQAGGGATD GENPILGQTP ARLHARTPFI 

       310        320        330 
FGSAEKVARI TAYHDLPEQE TSALFGNRGL FRS 

« Hide

References

[1]"Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000661 Genomic DNA. Translation: ABP71602.1.
RefSeqYP_001168907.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4WW38.

Genome annotation databases

GeneID5085293.
GenomeReviewsGene locus Rsph17025_2715 in contig CP000661_GR.
KEGGrsq:Rsph17025_2715.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAAACARIS.

Family and domain databases

HAMAPMF_01855.
[Tree]
InterProIPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
ProDomPD001491. In_FB_phphtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16A1_RHOS5
AccessionPrimary (citable) accession number: A4WW38
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: May 29, 2007
Last modified: November 3, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents