ASPG1_DROSI
ID ASPG1_DROSI Reviewed; 393 AA.
AC B4QHB1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase GD10667 {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=GD10667;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX06365.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CM000362; EDX06365.1; -; Genomic_DNA.
DR RefSeq; XP_002080780.1; XM_002080744.2.
DR AlphaFoldDB; B4QHB1; -.
DR SMR; B4QHB1; -.
DR STRING; 7240.B4QHB1; -.
DR EnsemblMetazoa; FBtr0210577; FBpp0209069; FBgn0182434.
DR GeneID; 6733734; -.
DR HOGENOM; CLU_021603_0_0_1; -.
DR OMA; PDENCET; -.
DR PhylomeDB; B4QHB1; -.
DR Proteomes; UP000000304; Chromosome 2r.
DR Bgee; FBgn0182434; Expressed in male reproductive system and 3 other tissues.
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_0000384137"
FT CHAIN 243..393
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384138"
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; 42219 MW; 76F0AF4EE97CE4C3 CRC64;
MRTHLRASLW VLCLASMAFS ILAAVNTSPK PTLASAFSGK AGTPAVKANK TTGELLPMVI
NTWNFTAANV LAWRILKQSK GGLRQTRNAV VEGCSKCEKL QCDRTVGYGG SPDELGETTL
DAMVMDGATM DVGAVAGLRR IKDAIKVARH VLEHTQHTML VGDAASAFAN AMGFESESLV
TPESKDMWLQ WTAENCQPNF WKNVHPDPKV SCGPYKPRPT PLTRWKEDRA RNEYEIGRKN
HDTIGMIAID VENNIHAGTS TNGARHKIPG RVGDSPIPGA GAYADNEVGA AVATGDGDVM
MRFLPSLLAV EAMRAGKPPA EAAQGGLRRI LKHHKDFMGA LIAVDRLGNY GAACYGLEEF
PFMVSSPAGA DRPTRLETVK CIAGQDKVNI VAL
