ASPG1_DROPE
ID ASPG1_DROPE Reviewed; 388 AA.
AC B4GGF2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase GL17147 {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=GL17147;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW35572.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479183; EDW35572.1; -; Genomic_DNA.
DR RefSeq; XP_002017733.1; XM_002017697.1.
DR AlphaFoldDB; B4GGF2; -.
DR SMR; B4GGF2; -.
DR STRING; 7234.FBpp0181254; -.
DR EnsemblMetazoa; FBtr0182762; FBpp0181254; FBgn0154751.
DR GeneID; 6592696; -.
DR KEGG; dpe:6592696; -.
DR eggNOG; KOG1593; Eukaryota.
DR HOGENOM; CLU_021603_0_0_1; -.
DR OMA; PDENCET; -.
DR PhylomeDB; B4GGF2; -.
DR Proteomes; UP000008744; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..239
FT /note="Glycosylasparaginase alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384131"
FT CHAIN 240..388
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384132"
FT ACT_SITE 240
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT BINDING 268..271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 291..294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 94..99
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 193..209
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 351..378
FT /evidence="ECO:0000250|UniProtKB:P20933"
SQ SEQUENCE 388 AA; 41869 MW; 52473D13A27F4A58 CRC64;
MYKAQYLWLF GLVLISRSAT ERTTPKINFT TVVGLKTTPA MRSSSASSLG GSLPMVINTW
NFTDANFLAW RILNVTQGGL RQTRNAVVEG CTRCEQQQCD RTVGYGGSPD ELGETTLDAM
IMDGSSMDVG AVAGLRGIKD AIRVARHVLE HTKHSILVGD LASQFAQAMG FRSESLATPE
SKAMWMEWTA ANCQPNFWRN VHPDPSISCG PYKPKATPLT RWKEDRARTE YSIGHLNHDT
IGMIAIDAAN NIHAGTSSNG ARHKIPGRVG DSPIPGAGAY ADNEVGAAVA TGDGDIMMRF
LPTLLAVEAM RAGKKPAEAA EVGIRRISKH YKDFSGAVIA VDRLGQYGAA CYGMTEFPFV
VSNPSKTDIP SRQESVKCIT GKEAVNVV
