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P83155 (ALF_ANASL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismAnabaena sp. (strain L31)
Taxonomic identifier29412 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length16 AA.
Sequence statusFragment.
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. UniProtKB P29271

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. UniProtKB P29271

Subunit structure

Homodimer By similarity. UniProtKB P29271

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›16›16Fructose-bisphosphate aldolase
PRO_0000262929

Experimental info

Non-terminal residue161

Sequences

Sequence LengthMass (Da)Tools
P83155 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 5D2670D9E4833A8B

FASTA161,702
        10 
ALVPLRLLLD HAAENG 

« Hide

References

[1]Apte S.K., Uhlemann E., Schmid R., Altendorf K.
Submitted (OCT-2001) to UniProtKB
Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameALF_ANASL
AccessionPrimary (citable) accession number: P83155
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 26 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

PATHWAY comments

Index of metabolic and biosynthesis pathways