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Reviewed, UniProtKB/Swiss-Prot A5FWQ8 (F16PA_ACICJ)

Last modified November 3, 2009. Version 22. 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
      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: Acry_0821
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length355 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; gluconeogenesis. HAMAP MF_01855

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm Potential.

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 – 355355Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364443

Regions

Region112 – 1154Substrate binding By similarity
Region256 – 2583Substrate 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 binding2761Magnesium 2 By similarity
Binding site2041Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FWQ8-1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 20B4591F918C72DF

FASTA35537,722
        10         20         30         40         50         60 
MSDALRLDTC LDQIASQLPA LTASCRVVEA LAGAARQIAH LLARGPLSGD LGAVIGESLD 

        70         80         90        100        110        120 
GDGQKALDAI THALVREAVI ASGAAAFASE EAAAPEWLDP VGEVAVAVDP LDGSSNIDTL 

       130        140        150        160        170        180 
APVGTIFSIL PARHASGADP ASPFLQTGRR QLAAGFFIYG PRTALAVTFG NGTRIFTLDP 

       190        200        210        220        230        240 
VSGAFLAPAP PATVPAATRE YAINGSNLRH WEEPIRDYIV ELKQGRNGPR GIDFNTRWLA 

       250        260        270        280        290        300 
SMVGDAFRIL GRGGIYLYPA DERQGYEAGR LRLVYEANPI AFLMEQAGAS ATDGRIPILD 

       310        320        330        340        350 
LQPAHIHQRC PLVFGSADEV RRVAQAYERA GQPSSPLFRR RSLFRSTSNV AELFA 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
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., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000697 Genomic DNA. Translation: ABQ30040.1.
RefSeqYP_001233959.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5FWQ8.

Genome annotation databases

GeneID5161624.
GenomeReviewsGene locus Acry_0821 in contig CP000697_GR.
KEGGacr:Acry_0821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMALFGQRGL.

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 nameF16PA_ACICJ
AccessionPrimary (citable) accession number: A5FWQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: June 12, 2007
Last modified: November 3, 2009
This is version 22 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