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Reviewed, UniProtKB/Swiss-Prot Q3IH61 (F16A2_PSEHT)

Last modified January 19, 2010. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: PSHAa1742
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length326 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 biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionfructose 1,6-bisphosphate 1-phosphatase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855
PRO_0000364638

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 site1981Substrate By similarity
Binding site2621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IH61-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 46291B44700EBDBF

FASTA32635,770
        10         20         30         40         50         60 
MKRLNTVLKE DGVQTDLILL IRTILATSKE IAFRVSQGEL AGVLGSTLNE NIQGEVQKKL 

        70         80         90        100        110        120 
DVIANQLLKD ILLDDNSVRT VASEEEDHAV GANPEGKFIV AFDPLDGSSN IDVNGQIGTI 

       130        140        150        160        170        180 
FTIYLARDDV PYDSDEQFNQ LGANQVCAGY VLYGPSSLLV MSTGGPTRCY TLDSTHGGYL 

       190        200        210        220        230        240 
LTNNQLSVPE QSSEFAVNMA NYRYWDEPTQ VYFDKLLYTC KSFDKSSVRW NAAMVGDVHR 

       250        260        270        280        290        300 
ILCRGGLFLY PQDNRAGNEN GKIRLLYEAN PLALLVENAG GKATSKGARI LDIAPTNLHQ 

       310        320 
RVPVVLGSIA PAEYFNSTVY NSNAKY 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954246 Genomic DNA. Translation: CAI86814.1.
RefSeqYP_340257.1.

3D structure databases

HSSPHSSP built from PDB template 2GQ1 based on UniProtKB P0A993.
SMRQ3IH61. Positions 18-317.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IH61.

Genome annotation databases

GeneID3709464.
GenomeReviewsGene locus PSHAa1742 in contig CR954246_GR.
KEGGpha:PSHAa1742.
NMPDRfig|326442.4.peg.1134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAWIASEES.
PhylomeDBQ3IH61.

Enzyme and pathway databases

BioCycPHAL326442:PSHAA1742-MONOMER.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
[Tree]
InterProIPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16A2_PSEHT
AccessionPrimary (citable) accession number: Q3IH61
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: November 8, 2005
Last modified: January 19, 2010
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents