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Reviewed, UniProtKB/Swiss-Prot Q3IYB9 (F16A1_RHOS4)

Last modified November 3, 2009. Version 30. 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

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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: RHOS4_28970
ORF Names: RSP_1285
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Complete proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

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Protein attributes

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

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855
PRO_0000364666

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

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Sequences

Sequence LengthMass (Da)Tools
Q3IYB9-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: E4C702EE381F1E38

FASTA33335,891
        10         20         30         40         50         60 
MKPFPTHPDA IPAELQDVMD RLGSVAIEVA NRIARGGIDE DLAGLCGTNT DGDGQKALDV 

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

       130        140        150        160        170        180 
WPAAATAEAS 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

« Hide

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References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000143 Genomic DNA. Translation: ABA80465.1.
RefSeqYP_354366.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IYB9.

Genome annotation databases

GeneID3718199.
GenomeReviewsGene locus RHOS4_28970 in contig CP000143_GR.
KEGGrsp:RSP_1285.
NMPDRfig|272943.3.peg.2896.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3IYB9.
OMAVNKGALA.

Enzyme and pathway databases

BioCycRSPH272943:RSP_1285-MON.

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...

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Entry information

Entry nameF16A1_RHOS4
AccessionPrimary (citable) accession number: Q3IYB9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: November 8, 2005
Last modified: November 3, 2009
This is version 30 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)

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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