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Reviewed, UniProtKB/Swiss-Prot P83451 (ASPG_ASOTA)

Last modified June 16, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
    EC=3.5.1.26
Alternative name(s):
    Glycosylasparaginase
    Aspartylglucosaminidase
      Short name=AGA
    N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Cleaved into the following 2 chains:
    1- Recommended name:
            Glycosylasparaginase alpha chain
                Short name=AGA subunit alpha
        Alternative name(s):
            p18
    2- Recommended name:
            Glycosylasparaginase beta chain
                Short name=AGA subunit beta
        Alternative name(s):
            p30
OrganismAsobara tabida (Parasitic wasp)
Taxonomic identifier58720 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaIchneumonoideaBraconidaeAlysiinaeAsobara

Protein attributes

Sequence length40 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins By similarity. UniProtKB P20933

Catalytic activity

N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate. UniProtKB P20933

Subunit structure

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. Ref.1

Subcellular location

Secreted. Ref.1

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

May be N-glycosylated. Ref.1

Sequence similarities

Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Glycosylasparaginase alpha chain Ref.1
PRO_0000002341
Chain21 – ›40›20Glycosylasparaginase beta chain Ref.1
PRO_0000002342

Sites

Active site211Nucleophile By similarity UniProtKB P20933

Experimental info

Non-adjacent residues20 – 212
Non-terminal residue401

Sequences

Sequence LengthMass (Da)Tools
P83451-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 24CDC49700732BAD

FASTA404,138
        10         20         30         40 
RIIEPIAGGP FIVMTWNYPG TIGIIAVDAN GHIAVGTSTN 

« Hide

References

[1]"Identification of an aspartylglucosaminidase-like protein in the venom of the parasitic wasp Asobara tabida (Hymenoptera: Braconidae)."
Moreau S.J.M., Cherqui A., Doury G., Dubois F., Fourdrain Y., Sabatier L., Bulet P., Saarela J., Prevost G., Giordanengo P.
Insect Biochem. Mol. Biol. 34:485-492(2004) [PubMed: 15110870] [Abstract]
Cited for: PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.5.1.26. 294119.

Family and domain databases

InterProIPR000246. Peptidase_T2.
[Graphical view]
PfamPF01112. Asparaginase_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASPG_ASOTA
AccessionPrimary (citable) accession number: P83451
Secondary accession number(s): P83452
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: October 25, 2004
Last modified: June 16, 2009
This is version 26 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents