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Q703I2 (ALF_THECA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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
OrganismThermus caldophilus
Taxonomic identifier272 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length305 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

Homotetramer. Ref.1

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processfructose 1,6-bisphosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolysis

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 – 305305Fructose-bisphosphate aldolase
PRO_0000178752

Regions

Region209 – 2113Dihydroxyacetone phosphate binding By similarity
Region251 – 2544Dihydroxyacetone phosphate binding By similarity

Sites

Active site801Proton donor By similarity
Metal binding811Zinc 1; catalytic By similarity UniProtKB P11604
Metal binding1021Zinc 2 By similarity
Metal binding1321Zinc 2 By similarity
Metal binding1781Zinc 1; catalytic By similarity
Metal binding2081Zinc 1; catalytic By similarity
Binding site491Glyceraldehyde 3-phosphate By similarity
Binding site1791Dihydroxyacetone phosphate; via amide nitrogen By similarity

Secondary structure

............................................ 305
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q703I2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9FE260186F29B98A

FASTA30532,987
        10         20         30         40         50         60 
MLVTGLEILR KARAEGYGVG AFNTNNMEFT QAILEAAEEM KSPVILALSE GAMKYGGRAL 

        70         80         90        100        110        120 
TRMVVALAQE ARVPVAVHLD HGSSYESVLK ALREGFTSVM IDKSHEDFET NVRETKRVVE 

       130        140        150        160        170        180 
AAHAVGVTVE AELGRLAGIE EHVAVDEKDA LLTNPEEARI FMERTGADYL AVAIGTSHGA 

       190        200        210        220        230        240 
YKGKGRPFID HPRLARIAKL VPAPLVLHGA SAVPQELVER FRAAGGEIGE ASGIHPEDIK 

       250        260        270        280        290        300 
KAISLGIAKI NTDTDLRLAF TALVRETLGK NPKEFDPRKY LGPAREAVKE VVKSRMELFG 


SVGRA 

« Hide

References

[1]"Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus."
Lee J.H., Im Y.J., Rho S.-H., Park S.H., Kim M.-K., Cho S.J., Kim T.-Y., Oh J.H., Shin H.-J., Lee D.-S., Eom S.H.
Protein Pept. Lett. 10:511-515(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ621816 Genomic DNA. Translation: CAF32659.1.
AY526903 Genomic DNA. Translation: AAS19362.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FJKX-ray2.20A/B/C/D1-305[»]
ProteinModelPortalQ703I2.
SMRQ703I2. Positions 1-305.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
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.
TIGR01859. fruc_bis_ald_. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ703I2.

Entry information

Entry nameALF_THECA
AccessionPrimary (citable) accession number: Q703I2
Secondary accession number(s): P83739
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 47 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