Skip Header

Contribute Send feedback
Read comments (?) or add your own

A3PRW1 (F16A2_RHOS1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-1,6-bisphosphatase class 1 2

Short name=FBPase class 1 2
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 2
Gene names
Name:fbp2
Ordered Locus Names:Rsph17029_3999
OrganismRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) [Complete proteome] [HAMAP]
Taxonomic identifier349101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length331 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 – 331331Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855
PRO_0000364671

Regions

Region101 – 1044Substrate binding By similarity

Sites

Metal binding801Magnesium 1 By similarity
Metal binding981Magnesium 1 By similarity
Metal binding981Magnesium 2 By similarity
Metal binding1001Magnesium 1; via carbonyl oxygen By similarity
Metal binding1011Magnesium 2 By similarity
Metal binding2611Magnesium 2 By similarity
Binding site1891Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PRW1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 451BB62B8EBECD13

FASTA33135,355
        10         20         30         40         50         60 
MAIELEDLGL SPDVADVMQR LARVGAGIAR IISRNGLERD LGAGVGTNAG GDGQKALDVI 

        70         80         90        100        110        120 
ADDAFRAALE GSAVAYYASE EQDEVVTLGE GSLALAIDPL DGSSNIDVNV SIGTIFSIFP 

       130        140        150        160        170        180 
AAAGPEASFL RPGTEQIAGG YIIYGPQCAL VCSFGQGVQH WVLDLDAGIF RRMPDIRPLP 

       190        200        210        220        230        240 
AETSEFAINA SNYRHWPQPI RAFVDDLVAG AEGPRGKNFN MRWIASLVAE THRILMRGGV 

       250        260        270        280        290        300 
FLYPGDERKG YERGRLRHVY ECAPIAFLIA NVGGRATDGC ADILTALPDR LHARTPFVFG 

       310        320        330 
CASKVARVAA YHDLACEETS ALFGSRGLFR S 

« Hide

References

[1]"Complete sequence of chromosome 2 of Rhodobacter sphaeroides ATCC 17029."
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17029 / ATH 2.4.9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000578 Genomic DNA. Translation: ABN79077.1.
RefSeqYP_001045849.1. NC_009050.1.

3D structure databases

ProteinModelPortalA3PRW1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3PRW1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4898844.
GenomeReviewsGene locus Rsph17029_3999 in contig CP000578_GR.
KEGGrsh:Rsph17029_3999.
PATRIC23176047. VBIRhoSph114483_4284.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMARNTDGDV.
ProtClustDBCLSK841466.

Enzyme and pathway databases

BioCycRSPH349101:RSPH17029_3999-MONOMER.

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 nameF16A2_RHOS1
AccessionPrimary (citable) accession number: A3PRW1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 41 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