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Q3B5N2 (F16PA_PELLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:Plut_0461
OrganismPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]
Taxonomic identifier319225 [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_0000364624

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
Q3B5N2 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 676143986EAC6D6E

FASTA33336,481
        10         20         30         40         50         60 
MSQLITIERH ILEQQKNFPE ATGELTDLLS DVAFAAKLVR REVVRAGLVD ILGFAGSTNV 

        70         80         90        100        110        120 
QGEEVKKLDL FANDKIINAI GQHGRFAIMG SEENEGIIIP PKNETGSYAL LFDPLDGSSN 

       130        140        150        160        170        180 
IDVNVSVGTI FSIYRIKSSD PGNASISDCL QKGSEQVAAG YVIYGSSVVM VYTTGHGVHG 

       190        200        210        220        230        240 
FTYDPTIGEF LLSHENITTP GSGKYYSINE GSYAQFNDGT KRYLDYIKEE DPATGRPYST 

       250        260        270        280        290        300 
RYIGSLVADF HRNLLTGGVF VYPPTTKHPS GKLRLMYEAN PLAFICEQAG GRATDGHRRI 

       310        320        330 
LDIDPSELHQ RTPLYIGSMA DVKVAEEFEQ GIR

« Hide

References

[1]"Complete sequence of Pelodictyon luteolum DSM 273."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000096 Genomic DNA. Translation: ABB23349.1.
RefSeqYP_374392.1. NC_007512.1.

3D structure databases

HSSPHSSP built from PDB template 2GQ1 based on UniProtKB P0A993.
ProteinModelPortalQ3B5N2.
SMRQ3B5N2. Positions 4-330.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3B5N2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3745774.
GenomeReviewsGene locus Plut_0461 in contig CP000096_GR.
KEGGplt:Plut_0461.
NMPDRfig|319225.3.peg.449.
PATRIC21378392. VBIChlLut1287_0481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAVMVYTTG.
PhylomeDBQ3B5N2.
ProtClustDBPRK09293.

Enzyme and pathway databases

BioCycPLUT319225:PLUT_0461-MONOMER.

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_PELLD
AccessionPrimary (citable) accession number: Q3B5N2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 51 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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