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B0T0R1 (F16PA_CAUSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Caul_3013
OrganismCaulobacter sp. (strain K31) [Complete proteome] [HAMAP]
Taxonomic identifier366602 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length322 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 – 322322Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364518

Regions

Region109 – 1124Substrate binding By similarity

Sites

Metal binding871Magnesium 1 By similarity
Metal binding1061Magnesium 1 By similarity
Metal binding1061Magnesium 2 By similarity
Metal binding1081Magnesium 1; via carbonyl oxygen By similarity
Metal binding1091Magnesium 2 By similarity
Metal binding2711Magnesium 2 By similarity
Binding site1991Substrate By similarity
Binding site2651Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0T0R1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: DC3F30B6ECB6EFD5

FASTA32233,951
        10         20         30         40         50         60 
MTTLTDLAGW LAMEPAGDDV KAVVTVIAGA CAQISKVVAS GAISGSLGAA GQVNVQDEEQ 

        70         80         90        100        110        120 
KKLDIITNDI LRGALKACGP VAGLASEELE EIETTGREGG FLVTFDPLDG SSNIDVNVSV 

       130        140        150        160        170        180 
GTIFSILPAP ATGIPTEADF LQPGRQQVAA GYAVYGPQTM LVLTLSKGVA GFTLDADGAW 

       190        200        210        220        230        240 
RLTHGDVAIP ADTAEFAINM SNQRHWAQPV RRYIDGCLQG KSGPRGKNFN MRWVASMVAD 

       250        260        270        280        290        300 
VHRIAMRGGI FMYPWDAREP DKPGKLRLLY EANPMSLIVE RAGGKSTLDG VTAILDVQPT 

       310        320 
KLHQRVPVVL GSANEVDQVA AG

« Hide

References

[1]"Complete sequence of chromosome of Caulobacter sp. K31."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Stephens C., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000927 Genomic DNA. Translation: ABZ72140.1.
RefSeqYP_001684638.1. NC_010338.1.

3D structure databases

ProteinModelPortalB0T0R1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0T0R1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5900468.
GenomeReviewsGene locus Caul_3013 in contig CP000927_GR.
KEGGcak:Caul_3013.
PATRIC21319132. VBICauSp18104_3414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731261.
OMANEWAGHL.
ProtClustDBPRK09293.

Enzyme and pathway databases

BioCycCSP78:CAUL_3013-MONOMER.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
[Tree]
InterProIPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
KOK03841.
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16PA_CAUSK
AccessionPrimary (citable) accession number: B0T0R1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 34 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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