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Protein

Fructose-bisphosphate aldolase

Gene
N/A
Organism
Anabaena sp. (strain L31)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Pathwayi

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
OrganismiAnabaena sp. (strain L31)
Taxonomic identifieri29412 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›16›16Fructose-bisphosphate aldolasePRO_0000262929Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the class II fructose-bisphosphate aldolase family.Sequence Analysis

Sequencei

Sequence statusi: Fragment.

P83155-1 [UniParc]FASTAAdd to basket

« Hide

        10 
ALVPLRLLLD HAAENG
Length:16
Mass (Da):1,702
Last modified:March 1, 2002 - v1
Checksum:i5D2670D9E4833A8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei16 – 161

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiALF_ANASL
AccessioniPrimary (citable) accession number: P83155
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2002
Last modified: November 26, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.