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Reviewed, UniProtKB/Swiss-Prot Q47A13 (F16A1_DECAR)

Last modified January 19, 2010. Version 37. 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: Daro_3589
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Dechloromonas

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Protein attributes

Sequence length338 AA.
Sequence statusComplete.
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. 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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855
PRO_0000364534

Regions

Region117 – 1204Substrate binding By similarity

Sites

Metal binding921Magnesium 1 By similarity
Metal binding1141Magnesium 1 By similarity
Metal binding1141Magnesium 2 By similarity
Metal binding1161Magnesium 1; via carbonyl oxygen By similarity
Metal binding1171Magnesium 2 By similarity
Metal binding2851Magnesium 2 By similarity
Binding site2131Substrate By similarity
Binding site2791Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q47A13-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: F292D5A9087CAB5A

FASTA33836,728
        10         20         30         40         50         60 
MTQQRTLARY LTEEQRNKGV ITGDLKLLIE VVSRACQAIS IAIGKGGLGG VLGEAGSDNV 

        70         80         90        100        110        120 
QGEAQKKLDV LSNDILLDAN EWGGHLAAMA SEEMDLPHLV PHRFPKGEYL LTFDPLDGSS 

       130        140        150        160        170        180 
NIDVNVSIGT IFSVLKCPEG ADLSTPEAAE QAFLQPGTAQ VAAGYAVYGP TTLLVLTVGD 

       190        200        210        220        230        240 
GVAVFTLDRE QGQFILTLEN VQIPADTKEF AINMSNQRFW EAPVQRYVAE MQVGKEGPLG 

       250        260        270        280        290        300 
KDYNMRWVAS MVADVHRIMT RGGIFMYPMD SKIKGQGGKL RLMYEANPMA MLIEQAGGAA 

       310        320        330 
TTGRQRILDI QPEKLHQRVP VILGSKNEVE RVTGYHSA

« Hide

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References

[1]"Complete sequence of Dechloromonas aromatica RCB."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000089 Genomic DNA. Translation: AAZ48318.1.
RefSeqYP_286788.1.

3D structure databases

HSSPHSSP built from PDB template 2FIE based on UniProtKB P09467.
SMRQ47A13. Positions 2-337.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ47A13.

Genome annotation databases

GeneID3567899.
GenomeReviewsGene locus Daro_3589 in contig CP000089_GR.
KEGGdar:Daro_3589.
NMPDRfig|159087.4.peg.2911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMACEETSAL.

Enzyme and pathway databases

BioCycDARO159087:DARO_3589-MONOMER.

Family and domain databases

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

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Entry information

Entry nameF16A1_DECAR
AccessionPrimary (citable) accession number: Q47A13
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 13, 2005
Last modified: January 19, 2010
This is version 37 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