ASPG1_DROYA
ID ASPG1_DROYA Reviewed; 396 AA.
AC B4NWI1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase GE19290 {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=GE19290;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW89526.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW89526.1};
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; CM000157; EDW89526.1; -; Genomic_DNA.
DR RefSeq; XP_002089814.2; XM_002089778.2.
DR AlphaFoldDB; B4NWI1; -.
DR SMR; B4NWI1; -.
DR STRING; 7245.FBpp0264300; -.
DR EnsemblMetazoa; FBtr0265808; FBpp0264300; FBgn0236640.
DR GeneID; 6528780; -.
DR KEGG; dya:Dyak_GE19290; -.
DR eggNOG; KOG1593; Eukaryota.
DR HOGENOM; CLU_021603_0_0_1; -.
DR OMA; PDENCET; -.
DR OrthoDB; 1487354at2759; -.
DR PhylomeDB; B4NWI1; -.
DR Proteomes; UP000002282; Chromosome 2L.
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; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..245
FT /note="Glycosylasparaginase alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384139"
FT CHAIN 246..396
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384140"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT BINDING 274..277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 100..105
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 199..215
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 357..384
FT /evidence="ECO:0000250|UniProtKB:P20933"
SQ SEQUENCE 396 AA; 42742 MW; B9D5457CDB8A998F CRC64;
MKRHLKACLW VLCFASTALS SLADTTSPKP TLASAFSGKS KTTAVSTALK ANKTASELLP
MVINTWNFTA ANVLAWRILK QSKGGLRQTR NAVVEGCSKC EKLQCDRTVG YGGSPDELGE
TTLDAMVMDG ATMEVGAVAG LRRIKDAIKV ARHVLEHTQH TMLVGDAASA FANAMGFESE
SLVTPESKDM WLQWTAENCQ PNFWKNVHPD PKVSCGPYKP RPTPLTRWKE DRARNEYEIG
RKNHDTIGMI AIDVESNIHA GTSTNGARHK IPGRVGDSPI PGAGAYADNE VGAAVATGDG
DVMMRFLPSL LAVEAMRAGK PPADAAEESL RRIIRHHKDF MGALIAVDRL GRYGAACYGL
DEFPFMVSSP AGRDGPTRLE TVKCIAGQDK VNIVSF
