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B4SDN7 (F16PA_PELPB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Ppha_2207
OrganismPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) [Complete proteome] [HAMAP]
Taxonomic identifier324925 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Pelodictyon

Protein attributes

Sequence length333 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 – 333333Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364625

Regions

Region116 – 1194Substrate binding By similarity

Sites

Metal binding921Magnesium 1 By similarity
Metal binding1131Magnesium 1 By similarity
Metal binding1131Magnesium 2 By similarity
Metal binding1151Magnesium 1; via carbonyl oxygen By similarity
Metal binding1161Magnesium 2 By similarity
Metal binding2781Magnesium 2 By similarity
Binding site2091Substrate By similarity
Binding site2421Substrate By similarity
Binding site2721Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4SDN7 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: EE1A20FBCAB4D497

FASTA33336,864
        10         20         30         40         50         60 
MSNLITIERH ILEQQKFFPD AQGELTDLLN DVAFAAKLVR REVVRAGLVD ILGFTGSTNV 

        70         80         90        100        110        120 
QGEEVKKLDL FANEKIISAI GQHGRFAIMG SEENEGVIIP PKNESGNYAL LFDPLDGSSN 

       130        140        150        160        170        180 
IDVNVSVGTI FSIYKLKGDD PGKASLSDCL QHGYEQVAAG YVIYGSSVVM VYTTGHGVHG 

       190        200        210        220        230        240 
FTYDPTIGEF LLSHENIITP KSGKYYSINE GSYAQFNEGT KRYLDYIKEE DPATNRPYST 

       250        260        270        280        290        300 
RYIGSLVADF HRNLLTGGVF VYPPTTKHLK GKLRLMYEAN PLAFICEQAG GRATNGRDRI 

       310        320        330 
LDIQPLELHQ RTPLYIGSVD DVILAEEFEQ GIR

« Hide

References

[1]"Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5477 / BU-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001110 Genomic DNA. Translation: ACF44405.1.
RefSeqYP_002019022.1. NC_011060.1.

3D structure databases

ProteinModelPortalB4SDN7.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4SDN7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6461068.
GenomeReviewsGene locus Ppha_2207 in contig CP001110_GR.
KEGGpph:Ppha_2207.
PATRIC22905175. VBIPelPha134556_2353.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731261.
OMAVMVYTTG.
ProtClustDBPRK09293.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
[Tree]
InterProIPR000146. FBPase_class-1/SBPase.
[Graphical view]
KOK03841.
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16PA_PELPB
AccessionPrimary (citable) accession number: B4SDN7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 29 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

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