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Q0T9F7 (F16PA_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. 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:ECP_4481
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. HAMAP-Rule MF_01855

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_01855

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm Potential HAMAP-Rule 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_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

reductive pentose-phosphate cycle

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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Fructose-1,6-bisphosphatase class 1 HAMAP-Rule MF_01855
PRO_0000364553

Regions

Region113 – 1164Substrate binding By similarity
Region257 – 2593Substrate binding By similarity

Sites

Metal binding891Magnesium 1 By similarity
Metal binding1101Magnesium 1 By similarity
Metal binding1101Magnesium 2 By similarity
Metal binding1121Magnesium 1; via carbonyl oxygen By similarity
Metal binding1131Magnesium 2 By similarity
Metal binding2751Magnesium 2 By similarity
Binding site2061Substrate By similarity
Binding site2391Substrate By similarity
Binding site2691Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0T9F7 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 4F0FC8109491D78F

FASTA33236,834
        10         20         30         40         50         60 
MKTLGEFIVE KQHEFSHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG ASGAENVQGE 

        70         80         90        100        110        120 
VQQKLDLFAN EKLKAALKAR DIVAGIASEE EDEIVVFEGC EHAKYVVLMD PLDGSSNIDV 

       130        140        150        160        170        180 
NVSVGTIFSI YRRVTPVGTP VTEEDFLQPG NKQVAAGYVV YGSSTMLVYT TGCGVHAFTY 

       190        200        210        220        230        240 
DPSLGVFCLC QERMRFPEKG KTYSINEGNY IKFPNGVKKY IKFCQEEDKS TNRPYTSRYI 

       250        260        270        280        290        300 
GSLVADFHRN LLKGGIYLYP STASHPDGKL RLLYECNPMA FLAEQAGGKA SDGKERILDI 

       310        320        330 
IPETLHQRRS FFVGNDHMVE DVERFIREFP DA

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000247 Genomic DNA. Translation: ABG72422.1.
RefSeqYP_672323.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0T9F7.
SMRQ0T9F7. Positions 1-332.
ModBaseSearch...

Protein-protein interaction databases

STRING362663.ECP_4481.

Proteomic databases

PRIDEQ0T9F7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG72422; ABG72422; ECP_4481.
GeneID4187900.
KEGGecp:ECP_4481.
PATRIC18199906. VBIEscCol77757_4528.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHOG000191265.
KOK03841.
OMACQEEDKA.
PhylomeDBQ0T9F7.
ProtClustDBPRK09293.

Enzyme and pathway databases

BioCycECOL362663:GIY5-4523-MONOMER.
UniPathwayUPA00138.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
InterProIPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. PTHR11556. 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_ECOL5
AccessionPrimary (citable) accession number: Q0T9F7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 5, 2006
Last modified: May 1, 2013
This is version 57 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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