ID   ASPG_PIG                Reviewed;          34 AA.
AC   P30918;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase;
DE            EC=3.5.1.26 {ECO:0000269|PubMed:1554372};
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   Contains:
DE     RecName: Full=Glycosylasparaginase beta chain;
DE   Flags: Fragments;
GN   Name=AGA;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RC   TISSUE=Liver;
RX   PubMed=1554372; DOI=10.1042/bj2820891;
RA   Tollersrud O.-K., Aronson N.N. Jr.;
RT   "Comparison of liver glycosylasparaginases from six vertebrates.";
RL   Biochem. J. 282:891-897(1992).
CC   -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC       the peptide of asparagine-linked glycoproteins.
CC       {ECO:0000269|PubMed:1554372}.
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         Evidence={ECO:0000269|PubMed:1554372};
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers. {ECO:0000250|UniProtKB:P20933}.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
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.
CC       {ECO:0000250|UniProtKB:P20933}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20933}.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR   MEROPS; T02.001; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005764; C:lysosome; 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.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Direct protein sequencing; Hydrolase; Lysosome;
KW   Protease; Reference proteome.
FT   CHAIN           1..>17
FT                   /note="Glycosylasparaginase alpha chain"
FT                   /id="PRO_0000002337"
FT   CHAIN           18..>34
FT                   /note="Glycosylasparaginase beta chain"
FT                   /id="PRO_0000002338"
FT   ACT_SITE        18
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P20933"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000305"
FT   NON_TER         34
SQ   SEQUENCE   34 AA;  3621 MW;  A527053E8DBA8B56 CRC64;
     SXPLPLIVNT WPFKXATTIG MVVIHLKGYT AAGT