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B3R3R6 (F16A1_CUPTR) 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 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
Ordered Locus Names:RALTA_A0983
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length338 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 – 338338Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855
PRO_0000364530

Regions

Region116 – 1194Substrate binding By similarity

Sites

Metal binding911Magnesium 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 binding2801Magnesium 2 By similarity
Binding site2081Substrate By similarity
Binding site2741Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R3R6 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: D34DEE04D1836A16

FASTA33837,408
        10         20         30         40         50         60 
MTRISLTRYL VEEQRKHNTI QPELRLLIEV VARACKAISN AVSKGALAGV LGSAGTGNVQ 

        70         80         90        100        110        120 
GETQQKLDVI ANEVLLDANE WGGHLAAMAS EEMESFYEIP NRYPKGEYLL MFDPLDGSSN 

       130        140        150        160        170        180 
IDVNVSIGTI FSVLHMPKPG QTVTEADFLQ PGTHQVAAGY AVYGPQTTLV LTVGNGVHMF 

       190        200        210        220        230        240 
TLDREAGSFV LTQSNVTIPE DTKEFAINMS NMRHWAPPVR KYIDECLAGD EGPRGKNFNM 

       250        260        270        280        290        300 
RWVASMVADV HRILTRGGIF MYPWDKREPE KPGKLRLMYE ANPMAMLVEQ AGGAATNGEQ 

       310        320        330 
RILDVQPEKL HQRVSVILGS KNEVERVTRY HQEAQAKA

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633749 Genomic DNA. Translation: CAQ68948.1.
RefSeqYP_002005015.1. NC_010528.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3R3R6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6454235.
GenomeReviewsGene locus RALTA_A0983 in contig CU633749_GR.
KEGGcti:RALTA_A0983.
PATRIC21528536. VBICupTai42494_0946.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731261.
OMAHWEAPVQ.
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 nameF16A1_CUPTR
AccessionPrimary (citable) accession number: B3R3R6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 2, 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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