ID   ASPG1_DROSE             Reviewed;         393 AA.
AC   B4HT15;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase GM21137 {ECO:0000250|UniProtKB:P20933};
DE            EC=3.5.1.26;
DE   AltName: Full=Aspartylglucosaminidase {ECO:0000250|UniProtKB:P20933};
DE            Short=AGA {ECO:0000250|UniProtKB:P20933};
DE   AltName: Full=Glycosylasparaginase {ECO:0000250|UniProtKB:P20933};
DE   AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase {ECO:0000250|UniProtKB:P20933};
DE   Contains:
DE     RecName: Full=Glycosylasparaginase alpha chain {ECO:0000250|UniProtKB:P20933};
DE   Contains:
DE     RecName: Full=Glycosylasparaginase beta chain {ECO:0000250|UniProtKB:P20933};
DE   Flags: Precursor;
GN   ORFNames=GM21137;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1] {ECO:0000312|EMBL:EDW47125.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW47125.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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         Evidence={ECO:0000250|UniProtKB:P20933};
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers. {ECO:0000250|UniProtKB:P20933}.
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:0000255}.
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DR   EMBL; CH480816; EDW47125.1; -; Genomic_DNA.
DR   RefSeq; XP_002033112.1; XM_002033076.1.
DR   AlphaFoldDB; B4HT15; -.
DR   SMR; B4HT15; -.
DR   STRING; 7238.B4HT15; -.
DR   EnsemblMetazoa; FBtr0204122; FBpp0202614; FBgn0176018.
DR   GeneID; 6608376; -.
DR   KEGG; dse:6608376; -.
DR   HOGENOM; CLU_021603_0_0_1; -.
DR   OMA; PDENCET; -.
DR   PhylomeDB; B4HT15; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000246; Peptidase_T2.
DR   PANTHER; PTHR10188; PTHR10188; 1.
DR   Pfam; PF01112; Asparaginase_2; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..242
FT                   /note="Glycosylasparaginase alpha chain"
FT                   /evidence="ECO:0000250|UniProtKB:P20933"
FT                   /id="PRO_0000384135"
FT   CHAIN           243..393
FT                   /note="Glycosylasparaginase beta chain"
FT                   /evidence="ECO:0000250|UniProtKB:P20933"
FT                   /id="PRO_0000384136"
FT   ACT_SITE        243
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P20933"
FT   BINDING         271..274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         294..297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        97..102
FT                   /evidence="ECO:0000250|UniProtKB:P20933"
FT   DISULFID        196..212
FT                   /evidence="ECO:0000250|UniProtKB:P20933"
FT   DISULFID        354..381
FT                   /evidence="ECO:0000250|UniProtKB:P20933"
SQ   SEQUENCE   393 AA;  42213 MW;  B26DC932159E159C CRC64;
     MRTHLRASLW VLCLASTAFS ILAAVNTSPK PTLASAFSGK AGTTAVKANK TTDELLPMVI
     NTWNFTAANV LAWRILKQSK GGLRQTRNAV VEGCSKCEKL QCDRTVGYGG SPDELGETTL
     DAMVMDGATM DVGAVAGLRR IKDAIKVARH VLEHTQHTML VGDAASAFAN AMGFESESLV
     TPESKDMWLQ WTAENCQPNF WKNVHPDPKV SCGPYKPRPT PLTRWKEDRA RNEYEIGRKN
     HDTIGMIAID VENNIHAGTS TNGANHKIPG RVGDSPIPGA GAYADNEVGA AVATGDGDVM
     MRFLPSLLAV EAMRAGKPPA EAAQKGLRRI LKHQKDFMGA LIAVDRLGNY GAACYGLAEF
     PFMVSSPAGA DRPTRLETVK CIAGQDKVNI VAL