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Reviewed, UniProtKB/Swiss-Prot Q3IFQ5 (F16A1_PSEHT)

Last modified January 19, 2010. Version 38. 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 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: PSHAa0463
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

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 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 – 322322Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855
PRO_0000364637

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 binding2701Magnesium 2 By similarity
Binding site1981Substrate By similarity
Binding site2641Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IFQ5-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 9E4689C2E3350C29

FASTA32235,147
        10         20         30         40         50         60 
MRRLPPVLLE DGCPRELISL IRTILAACKE ISFRVGQGEL SGVLGSTLDE NIQGETQKKL 

        70         80         90        100        110        120 
DVLTNQLLKD ILLESGYVKA IASEEEDYTV AGNPDAEYIV AFDPLDGSSN TDINSLVGTI 

       130        140        150        160        170        180 
FSVMKAPEGA DPADQSIFMQ PGINQVAAGY VLYGPSTILA LTTGKGTRFF TLDKTHGTFL 

       190        200        210        220        230        240 
LTQDFAKIPA DTNEYAINAS NQRHWQPAMQ NYINDLVAGD TGPRARNFNM RWIAAMVGDV 

       250        260        270        280        290        300 
HRVLSRGGLF TYPTDTKNPS QPNKLRLLYE ANPMAMLVEQ AGGIASTGTE RIMDIQPNAI 

       310        320 
HQRVAVILGS KNEVETCLGY HK 

« 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: CAI85560.1.
RefSeqYP_339003.1.

3D structure databases

HSSPHSSP built from PDB template 2GQ1 based on UniProtKB P0A993.
SMRQ3IFQ5. Positions 13-321.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IFQ5.

Genome annotation databases

GeneID3709325.
GenomeReviewsGene locus PSHAa0463 in contig CR954246_GR.
KEGGpha:PSHAa0463.
NMPDRfig|326442.4.peg.446.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMACEETSAL.
PhylomeDBQ3IFQ5.

Enzyme and pathway databases

BioCycPHAL326442:PSHAA0463-MONOMER.

Family and domain databases

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

Entry information

Entry nameF16A1_PSEHT
AccessionPrimary (citable) accession number: Q3IFQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: November 8, 2005
Last modified: January 19, 2010
This is version 38 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