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Q0PAS0 (ALF_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase

Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:fba
Synonyms:fda, fdaC
Ordered Locus Names:Cj0597
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity.

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Fructose-bisphosphate aldolase
PRO_0000178711

Regions

Region261 – 2633Dihydroxyacetone phosphate binding By similarity
Region282 – 2854Dihydroxyacetone phosphate binding By similarity

Sites

Active site1041Proton donor By similarity
Metal binding1051Zinc 1; catalytic By similarity
Metal binding1391Zinc 2 By similarity
Metal binding1691Zinc 2 By similarity
Metal binding2211Zinc 1; catalytic By similarity
Metal binding2601Zinc 1; catalytic By similarity
Binding site611Glyceraldehyde 3-phosphate By similarity
Binding site2221Dihydroxyacetone phosphate; via amide nitrogen By similarity

Secondary structure

...................................................... 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q0PAS0 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: E4ACB44EA1860135

FASTA35438,730
        10         20         30         40         50         60 
MGVLDIVKAG VISGDELNKI YDYAKAEGFA IPAVNVVGTD SINAVLEAAK KVNSPVIIQF 

        70         80         90        100        110        120 
SNGGAKFYAG KNCPNGEVLG AISGAKHVHL LAKAYGVPVI LHTDHAARKL LPWIDGLIEA 

       130        140        150        160        170        180 
NAQYKKTHGQ ALFSSHMLDL SEESLEENLS TCEVYLQKLD ALGVALEIEL GCTGGEEDGV 

       190        200        210        220        230        240 
DNTGIDNSKL YTQPEDVALA YERLGKISDK FSIAASFGNV HGVYKPGNVS LQPEILKNSQ 

       250        260        270        280        290        300 
KFVKDKFALN SDKPINFVFH GGSGSELKDI KNAVSYGVIK MNIDTDTQWA FWDGVREYEL 

       310        320        330        340        350 
KNRAYLQGQI GNPEGDDKPN KKYYDPRVWL RSGEESMIKR LEIAFEDLNC INKN 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34743.1.
PIRS52413.
RefSeqYP_002344027.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QM3X-ray1.85A/B/C/D/E/F/G/H1-354[»]
ProteinModelPortalQ0PAS0.
SMRQ0PAS0. Positions 3-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ0PAS0. 9 interactions.
STRING192222.Cj0597.

Proteomic databases

PRIDEQ0PAS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL34743; CAL34743; Cj0597.
GeneID904922.
KEGGcje:Cj0597.
PATRIC20058138. VBICamJej33762_0589.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAKKAYDPR.
OrthoDBEOG69GZPB.
ProtClustDBPRK09197.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-584-MONOMER.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_CAMJE
AccessionPrimary (citable) accession number: Q0PAS0
Secondary accession number(s): P53818
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: September 19, 2006
Last modified: November 13, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways