ASPG1_DROGR
ID ASPG1_DROGR Reviewed; 393 AA.
AC B4JVW6;
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 GH22932 {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=GH22932;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV98104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV98104.1};
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; CH916375; EDV98104.1; -; Genomic_DNA.
DR RefSeq; XP_001995032.1; XM_001994996.1.
DR AlphaFoldDB; B4JVW6; -.
DR SMR; B4JVW6; -.
DR STRING; 7222.FBpp0156838; -.
DR PRIDE; B4JVW6; -.
DR EnsemblMetazoa; FBtr0471536; FBpp0421571; FBgn0130389.
DR GeneID; 6568928; -.
DR KEGG; dgr:6568928; -.
DR eggNOG; KOG1593; Eukaryota.
DR HOGENOM; CLU_021603_0_0_1; -.
DR InParanoid; B4JVW6; -.
DR OMA; PDENCET; -.
DR OrthoDB; 1487354at2759; -.
DR PhylomeDB; B4JVW6; -.
DR Proteomes; UP000001070; 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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..245
FT /note="Glycosylasparaginase alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384127"
FT CHAIN 246..393
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384128"
FT REGION 15..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..381
FT /evidence="ECO:0000250|UniProtKB:P20933"
SQ SEQUENCE 393 AA; 42874 MW; 108F4424B182E50C CRC64;
MPMVIHSTSA SWGTALKPIT NSSSDTITPN PNLITTSRGS STRPSYITTL TAKKMEQLLP
MVINTWNMSE ANEMAWRILQ QSEGGVRQTR NAVVEGVTRC EELQCFHSVG YGGSPDERGE
TTLDAMVMDG GLMDVGAVGG LRNIKEAIRV ARFVLEHTSH TLLVGQSATD FAVSMGFRTS
SLVTPWSHDE WEKWKAKNCQ PNCWLNVNPD PKLSCGPYVP KATPLTRWKE DRARNEYEIG
ENNHDTIGMI AIDVENQIHT GTSTNGMTHK IPGRVGDSPI VGAGSYADNE VGAAVATGDG
DVMMRFLPSL LAVEAMRNGK SPQEAAELGI KRIAKYYKDF IGAVIAVNRL GQYAAACYGI
PEFPYMISNP THTVSVQTVK CLPYVHVEPL PKS
