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Reviewed, UniProtKB/Swiss-Prot P27994 (F16A1_RHOSH)

Last modified June 16, 2009. Version 45. 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
Synonyms: fbpA
OrganismRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifier1063 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

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Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Enzyme regulation

Fructose-1,6-bisphosphatase II is not light-activated. HAMAP MF_01855

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_01855

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm Potential.

Miscellaneous

There are two genes for FBPase in R.sphaeroides. 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
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 – 333333Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855
PRO_0000200487

Regions

Region103 – 1064Substrate binding By similarity

Sites

Metal binding811Magnesium 1 By similarity
Metal binding1001Magnesium 1 By similarity
Metal binding1001Magnesium 2 By similarity
Metal binding1021Magnesium 1; via carbonyl oxygen By similarity
Metal binding1031Magnesium 2 By similarity
Metal binding2631Magnesium 2 By similarity
Binding site1911Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
P27994-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 7274A0D4C8FC8426

FASTA33335,997
        10         20         30         40         50         60 
MKPFPTHPDA IPAELQDVMD RLGSVAIEVA NRIARGGIDE DLAGLCGTNT DGDGQKALDV 

        70         80         90        100        110        120 
IADDAFRVAL EGSAVRFYAS EEQDTAVTLN EAGTLALAID PLDGSSNIDT NLSVGTTFAI 

       130        140        150        160        170        180 
WPAAPRPNPS FLRLGSELIA AGYVIYGPQV CMMVSFGKGT QKYVLDPGSR SFVLVDRAVK 

       190        200        210        220        230        240 
VPPSSTEFAI NASNYRHWPK PIRAYIDDCV AGTEGPRGRN FNMRWLASLV AETHRILARG 

       250        260        270        280        290        300 
GVFLYPRDSR KGYEQGRLRY LYECAPIAFV ITQAGGGATD GENPILGQTP SRLHARTPFV 

       310        320        330 
FGSAEKVARI TAYHDLPEQE TSALFGNRGL FRS

« Hide

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References

[1]"Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides."
Gibson J.L., Falcone D.L., Tabita F.R.
J. Biol. Chem. 266:14646-14653(1991) [PubMed: 1907281] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

M64624 Genomic DNA. Translation: AAA26112.1.
PIRPARFAS. A40767.

3D structure databases

HSSPHSSP built from PDB template 1DBZ based on UniProtKB P46275.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.11. 2796.

Family and domain databases

HAMAPMF_01855.
[Tree]
InterProIPR000146. Fructose_bisphosphatase.
IPR017955. IMPase/FBPase.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. FBPHPHTASE.
PR00377. INFBPHPHTASE.
ProDomPD001491. In_FB_phphtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameF16A1_RHOSH
AccessionPrimary (citable) accession number: P27994
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 45 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