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Q088C3 (F16PA_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Sfri_0531
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length330 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 – 330330Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364704

Regions

Region106 – 1094Substrate binding By similarity

Sites

Metal binding841Magnesium 1 By similarity
Metal binding1031Magnesium 1 By similarity
Metal binding1031Magnesium 2 By similarity
Metal binding1051Magnesium 1; via carbonyl oxygen By similarity
Metal binding1061Magnesium 2 By similarity
Metal binding2681Magnesium 2 By similarity
Binding site1961Substrate By similarity
Binding site2621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q088C3 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: B6A892D3947824B2

FASTA33035,736
        10         20         30         40         50         60 
MQTLAQTLSV QAVNASLTQL LLTLADTSKA ISGAVRHGAL AGVLGATEQE NIQGETQKKL 

        70         80         90        100        110        120 
DVITNDMLKD ALKADGNVRG LASEEEDYVV EVNAKGEYLV CFDPLDGSSN IDINSLVGTI 

       130        140        150        160        170        180 
FSVLPAPAGE LNEQSFLQAG RKQVAAGYVL YGPSTMMALT TGQGTQFYTL APDSQEFLLT 

       190        200        210        220        230        240 
DDSVQITPDT AEFAINMSNQ RFWEAPMQTY IADLLLGEIG PREQSFNMRW IAAMVGDVHR 

       250        260        270        280        290        300 
VLCRGGIFSY PTDNKNPAKP FKLRLMYEAN PMALLVEQAG GKASTGYETI LDIQPTEIHQ 

       310        320        330 
RVAVILGSAN EVDTCLSYHG IDYSEEPSID 

« Hide

References

[1]"Complete sequence of Shewanella frigidimarina NCIMB 400."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. expand/collapse author list , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIMB 400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000447 Genomic DNA. Translation: ABI70392.1.
RefSeqYP_749230.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ088C3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ088C3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4276951.
GenomeReviewsGene locus Sfri_0531 in contig CP000447_GR.
KEGGsfr:Sfri_0531.
NMPDRfig|318167.10.peg.506.
PATRIC23494849. VBISheFri14343_0549.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAANEVDTC.
PhylomeDBQ088C3.
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_SHEFN
AccessionPrimary (citable) accession number: Q088C3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 31, 2006
Last modified: January 25, 2012
This is version 43 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