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B3QB72 (F16PA_RHOPT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fructose-1,6-bisphosphatase class 1
Short name=FBPase class 1
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
Gene names
Name:fbp
Ordered Locus Names:Rpal_5126
OrganismRhodopseudomonas palustris (strain TIE-1) [Complete proteome] [HAMAP]
Taxonomic identifier395960 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
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. HAMAP MF_01855

Pathway

Carbohydrate biosynthesis; Calvin cycle. HAMAP MF_01855

Subunit structure

Homotetramer By similarity. HAMAP MF_01855

Subcellular location

Cytoplasm Potential HAMAP MF_01855.

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: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364679

Regions

Region112 – 1154Substrate binding By similarity

Sites

Metal binding901Magnesium 1 By similarity
Metal binding1091Magnesium 1 By similarity
Metal binding1091Magnesium 2 By similarity
Metal binding1111Magnesium 1; via carbonyl oxygen By similarity
Metal binding1121Magnesium 2 By similarity
Metal binding2711Magnesium 2 By similarity
Binding site1991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B3QB72 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 4C0B5D61C5841B5B

FASTA34336,633
        10         20         30         40         50         60 
MDQGQTLSVL LDSYAVDPQK KAVAAAVGAI AAGSIEISEL IGQGALAGIT GAAHGGSNAD 

        70         80         90        100        110        120 
GDVQKDLDVK AEQIIVKSLK DVPYAALASE ESDTLLDGDP NAPISIAYDP LDGSSNIDTN 

       130        140        150        160        170        180 
MTVGTIFSII PNQPGVKPFT AAGSCQIAAG FVVYGPQTSL VLTLGDGVNI FTLDRKAKVY 

       190        200        210        220        230        240 
RLIRERVKVP ADTAEYAVNA SNHRHWEQPI RDFVDECIAG ADGPRAKDFN MRWIGSLVAE 

       250        260        270        280        290        300 
VYRILTRGGV FLYPGDNRPG YGNGRLRLLY ETHPMSFVME QAGGAASTGR ERVLDLTAKT 

       310        320        330        340 
IHQRSPLIMG SIDKVKRIEL LHTDPSAASR SAPLFARRGL FRV

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris TIE-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Emerson D., Newman D.K., Roden E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TIE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001096 Genomic DNA. Translation: ACF03615.1.
RefSeqYP_001994090.1. NC_011004.1.

3D structure databases

ProteinModelPortalB3QB72.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3QB72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6412820.
GenomeReviewsGene locus Rpal_5126 in contig CP001096_GR.
KEGGrpt:Rpal_5126.
PATRIC23314843. VBIRhoPal88240_5201.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731261.
OMAHWEAPVQ.
ProtClustDBPRK09293.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
[Tree]
InterProIPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
KOK03841.
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16PA_RHOPT
AccessionPrimary (citable) accession number: B3QB72
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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