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A0M764 (F16A2_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-1,6-bisphosphatase class 1 2

Short name=FBPase class 1 2
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 2
Gene names
Name:fbp2
Ordered Locus Names:GFO_3521
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length348 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; 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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

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 – 348348Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855
PRO_0000364564

Regions

Region120 – 1234Substrate binding By similarity

Sites

Metal binding931Magnesium 1 By similarity
Metal binding1171Magnesium 1 By similarity
Metal binding1171Magnesium 2 By similarity
Metal binding1191Magnesium 1; via carbonyl oxygen By similarity
Metal binding1201Magnesium 2 By similarity
Metal binding2801Magnesium 2 By similarity
Binding site2131Substrate By similarity
Binding site2441Substrate By similarity
Binding site2741Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M764 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: F02AE711AEF6AA0D

FASTA34838,767
        10         20         30         40         50         60 
MSKPNQTLGE FIIENQSDFP GSSGELSRLI NSLRLAAKVV NHEVNKAGLV DIIGAYGETN 

        70         80         90        100        110        120 
VQGEDQQKLD VYANNKFIQT LTNREIVCGI ASEENDDFIQ IEGHKGDHQN KYVVLMDPLD 

       130        140        150        160        170        180 
GSSNIDVNVS VGTIFSIYQR VTPVGTPVQK EDFLQPGNKQ VAAGYIIYGT STMLVYTTGH 

       190        200        210        220        230        240 
GVNGFTLNPA LGSWYLSHPD MKFPEEGQIY SINEGNYIHF PQGVKDYIKY CQQEEGNRPY 

       250        260        270        280        290        300 
TSRYIGSMVS DIHRNMIKGG IFMYPKSSKA SEGKLRLLYE CNPFAFITEQ AGGKASDGFQ 

       310        320        330        340 
RIMDIDPTEL HQRVPFFCGS KKMVEKAEEF MANAKANPQS QEFSFSSK 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL68459.1.
RefSeqYP_863526.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M764.
SMRA0M764. Positions 6-331.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4651540.
GenomeReviewsGene locus GFO_3521 in contig CU207366_GR.
KEGGgfo:GFO_3521.
NMPDRfig|411154.5.peg.3323.
PATRIC22075766. VBIGraFor5527_3393.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAHWEAPVQ.
PhylomeDBA0M764.
ProtClustDBPRK09293.

Enzyme and pathway databases

BioCycGFOR411154:GFO_3521-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 nameF16A2_GRAFK
AccessionPrimary (citable) accession number: A0M764
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 41 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