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P86830 (AAE_RAUVE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 6. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length46 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deacetylates 17-O-acetylajmaline and 17-O-acetylnorajmaline, but is inactive toward other acetylated alkaloids By similarity. UniProtKB Q3MKY2

Catalytic activity

17-O-acetylajmaline + H2O = ajmaline + acetate. Ref.1 UniProtKB Q3MKY2

17-O-acetylnorajmaline + H2O = norajmaline + acetate. Ref.1 UniProtKB Q3MKY2

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processalkaloid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionacetylajmaline esterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›46›46Acetylajmalan esterase
PRO_0000402568

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential

Experimental info

Non-terminal residue11
Non-terminal residue461

Sequences

Sequence LengthMass (Da)Tools
P86830 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: 7F9778EE939B4CBD

FASTA465,242
        10         20         30         40 
NALFILGNIG NNDVNYAFPD RAIEEIRFYV PFITEAVANA TREIIR 

« Hide

References

[1]"Functional expression of an ajmaline pathway-specific esterase from Rauvolfia in a novel plant-virus expression system."
Ruppert M., Woll J., Giritch A., Genady E., Ma X., Stockigt J.
Planta 222:888-898(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameAAE_RAUVE
AccessionPrimary (citable) accession number: P86830
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 6 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families