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P91759 (ALF_LYMST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. 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

EC=4.1.2.13
OrganismLymnaea stagnalis (Great pond snail) (Helix stagnalis)
Taxonomic identifier6523 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataHygrophilaLymnaeoideaLymnaeidaeLymnaea

Protein attributes

Sequence length101 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Pathway

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

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›101›101Fructose-bisphosphate aldolase
PRO_0000216932

Sites

Active site111Schiff-base intermediate with dihydroxyacetone-P By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1011

Sequences

Sequence LengthMass (Da)Tools
P91759 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: A151A6471A6AAFBD

FASTA10110,831
        10         20         30         40         50         60 
HNMFLEGTLL KPNMVTAGQG CPKKYTPEDI ARATVTALNR TVPAAVAGIT FLSGGQSEED 

        70         80         90        100 
ATINLNAINQ FPGRKPWPLT FSYGRALQAS VLKAWGGKDE L 

« Hide

References

[1]Fainzilber M., Kesteren R.E., Smit A.B.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73114 mRNA. Translation: AAC47398.1.

3D structure databases

ProteinModelPortalP91759.
SMRP91759. Positions 1-100.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_LYMST
AccessionPrimary (citable) accession number: P91759
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways