ASPG_ASOTA
ID ASPG_ASOTA Reviewed; 40 AA.
AC P83451; P83452;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase;
DE EC=3.5.1.26;
DE AltName: Full=Aspartylglucosaminidase;
DE Short=AGA;
DE AltName: Full=Glycosylasparaginase;
DE AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase;
DE Contains:
DE RecName: Full=Glycosylasparaginase alpha chain;
DE Short=AGA subunit alpha;
DE AltName: Full=p18;
DE Contains:
DE RecName: Full=Glycosylasparaginase beta chain;
DE Short=AGA subunit beta;
DE AltName: Full=p30;
DE Flags: Fragments;
OS Asobara tabida (Parasitic wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida;
OC Ichneumonoidea; Braconidae; Alysiinae; Asobara.
OX NCBI_TaxID=58720;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Venom {ECO:0000269|PubMed:15110870};
RX PubMed=15110870; DOI=10.1016/j.ibmb.2004.03.001;
RA Moreau S.J.M., Cherqui A., Doury G., Dubois F., Fourdrain Y., Sabatier L.,
RA Bulet P., Saarela J., Prevost G., Giordanengo P.;
RT "Identification of an aspartylglucosaminidase-like protein in the venom of
RT the parasitic wasp Asobara tabida (Hymenoptera: Braconidae).";
RL Insect Biochem. Mol. Biol. 34:485-492(2004).
CC -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC the peptide of asparagine-linked glycoproteins.
CC {ECO:0000250|UniProtKB:P20933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+)
CC + L-aspartate + N-acetyl-beta-D-glucosaminylamine;
CC Xref=Rhea:RHEA:11544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15947, ChEBI:CHEBI:29991, ChEBI:CHEBI:58080; EC=3.5.1.26;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000269|PubMed:15110870}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15110870}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15110870}.
CC -!- PTM: May be N-glycosylated. {ECO:0000269|PubMed:15110870}.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR AlphaFoldDB; P83451; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IEA:UniProtKB-EC.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Protease; Secreted.
FT CHAIN 1..>20
FT /note="Glycosylasparaginase alpha chain"
FT /evidence="ECO:0000303|PubMed:15110870"
FT /id="PRO_0000002341"
FT CHAIN 21..>40
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000303|PubMed:15110870"
FT /id="PRO_0000002342"
FT ACT_SITE 21
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT NON_CONS 20..21
FT /evidence="ECO:0000303|PubMed:15110870"
FT NON_TER 40
FT /evidence="ECO:0000303|PubMed:15110870"
SQ SEQUENCE 40 AA; 4138 MW; 24CDC49700732BAD CRC64;
RIIEPIAGGP FIVMTWNYPG TIGIIAVDAN GHIAVGTSTN
