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B3EGL2 (F16PA_CHLL2) 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:Clim_0557
OrganismChlorobium limicola (strain DSM 245 / NBRC 103803) [Complete proteome] [HAMAP]
Taxonomic identifier290315 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Chlorobium

Protein attributes

Sequence length332 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 – 332332Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364522

Regions

Region115 – 1184Substrate binding By similarity

Sites

Metal binding911Magnesium 1 By similarity
Metal binding1121Magnesium 1 By similarity
Metal binding1121Magnesium 2 By similarity
Metal binding1141Magnesium 1; via carbonyl oxygen By similarity
Metal binding1151Magnesium 2 By similarity
Metal binding2771Magnesium 2 By similarity
Binding site2081Substrate By similarity
Binding site2411Substrate By similarity
Binding site2711Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B3EGL2 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: FE66CA85A4D5E916

FASTA33236,447
        10         20         30         40         50         60 
MNLVTIERHI LEQQKFFPEA SGELTDLLTD VAFAAKLVRR EVVRAGLVDI LGFAGTTNVQ 

        70         80         90        100        110        120 
GEEVKKLDLF ANEKIINAIG QHGRFAVMGS EENDGIIIPP KNETGNYALL FDPLDGSSNI 

       130        140        150        160        170        180 
DVNVSVGTIF SIYRLKGDDP GKASISDCLQ QGSEQVAAGY VIYGSSVVMV YTTGNGVHGF 

       190        200        210        220        230        240 
TYDPTIGEFL LSHENIVTPK TGKYYSINEG SYAQFNEGTK KYLDYIKEED PATGRPYSTR 

       250        260        270        280        290        300 
YIGSLVADFH RNLLTGGVFV YPPTTTHTNG KLRLMYEANP LAFICEQAGG RATDGRNRIL 

       310        320        330 
DIQPTALHQR TPLYIGSEDD VIVAEEFEQG VR

« Hide

References

[1]"Complete sequence of Chlorobium limicola DSM 245."
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., Ovchinnikova G., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 245 / NBRC 103803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001097 Genomic DNA. Translation: ACD89649.1.
RefSeqYP_001942628.1. NC_010803.1.

3D structure databases

ProteinModelPortalB3EGL2.
SMRB3EGL2. Positions 3-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3EGL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6354908.
GenomeReviewsGene locus Clim_0557 in contig CP001097_GR.
KEGGcli:Clim_0557.
PATRIC21373117. VBIChlLim118737_0601.

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_CHLL2
AccessionPrimary (citable) accession number: B3EGL2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: July 22, 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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