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Reviewed, UniProtKB/Swiss-Prot A1VNR3 (F16A2_POLNA)

Last modified January 19, 2010. Version 27. 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 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: Pnap_1982
OrganismPolaromonas naphthalenivorans (strain CJ2) [Complete proteome] [HAMAP]
Taxonomic identifier365044 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length364 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; gluconeogenesis. 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 processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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 – 364364Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855
PRO_0000364629

Regions

Region124 – 1274Substrate binding By similarity

Sites

Metal binding991Magnesium 1 By similarity
Metal binding1211Magnesium 1 By similarity
Metal binding1211Magnesium 2 By similarity
Metal binding1231Magnesium 1; via carbonyl oxygen By similarity
Metal binding1241Magnesium 2 By similarity
Metal binding2921Magnesium 2 By similarity
Binding site2201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1VNR3-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 97599F184FFF6B28

FASTA36440,284
        10         20         30         40         50         60 
MPLNKRFTLT QYLIQERRRF PDARGDFNAL ILDVALACKA IARAVAFGEL GGMLGNHDAD 

        70         80         90        100        110        120 
AGGSINVQGE TQKKLDVISN QYFTRMNEWG GHLAGMASEE MDDAYQIPAE HPRGKYLLVF 

       130        140        150        160        170        180 
DPLDGSSNID VNVSVGSIFS ILRAPQEAVE SGRDVVEADF FQPGAEQVAA GYALYGPTTM 

       190        200        210        220        230        240 
LVLSVGNGVA GFTLDPMLGE FMLTHDKLQV PENTQEFAIN ASNSRFWEPP VKRYVDECLA 

       250        260        270        280        290        300 
GKTGPRDKDF NMRWIASMVA EAHRILMRGG VFLYPRDSKD AAKPGRLRLL YEANPIGFIM 

       310        320        330        340        350        360 
EQAGGRASTG REPMLGVQPT SLHQRIGLIF GSKNEVERIE RYHAEPARAE MHNPLFAERS 


LFRS 

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References

[1]"Complete sequence of chromosome 1 of Polaromonas naphthalenivorans CJ2."
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., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Madsen E.L., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000529 Genomic DNA. Translation: ABM37291.1.
RefSeqYP_982212.1.

3D structure databases

SMRA1VNR3. Positions 7-344.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1VNR3.

Genome annotation databases

GeneID4688089.
GenomeReviewsGene locus Pnap_1982 in contig CP000529_GR.
KEGGpna:Pnap_1982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMADGDGQKA.
PhylomeDBA1VNR3.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
[Tree]
InterProIPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16A2_POLNA
AccessionPrimary (citable) accession number: A1VNR3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: February 6, 2007
Last modified: January 19, 2010
This is version 27 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