ASPG1_DROPS
ID ASPG1_DROPS Reviewed; 388 AA.
AC Q28Y14;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase GA14866 {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=GA14866;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL26152.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CM000071; EAL26152.2; -; Genomic_DNA.
DR RefSeq; XP_001361573.2; XM_001361536.3.
DR AlphaFoldDB; Q28Y14; -.
DR SMR; Q28Y14; -.
DR STRING; 7237.FBpp0278411; -.
DR MEROPS; T02.001; -.
DR EnsemblMetazoa; FBtr0279973; FBpp0278411; FBgn0074893.
DR GeneID; 4805115; -.
DR KEGG; dpo:Dpse_GA14866; -.
DR eggNOG; KOG1593; Eukaryota.
DR InParanoid; Q28Y14; -.
DR OMA; PDENCET; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0074893; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..239
FT /note="Glycosylasparaginase alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384133"
FT CHAIN 240..388
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384134"
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; 41875 MW; 24F6676D0F7EDC3A CRC64;
MYEAQYLWLF GLVLISGSVT ERTTPKINFT TVVGLKTTPA MRSSSASSLG GSLPMVINTW
NFTDANFLAW RILNVTQGGL RQTRNAVVEG CTRCEQQQCD RTVGYGGSPD ELGETTLDAM
IMDGSSMDVG AVAGLRGIKD AIRVARHVLE HTKHSMLVGD LASQFAQAMG FRSESLATPE
SKAMWMEWTA ANCQPNFWRN VHPDPSISCG PYKPKATPLT RWKEDRARTE YSIGHLNHDT
IGMIAIDAEN NIHAGTSSNG ARHKIPGRVG DSPIPGAGAY ADNEVGAAVA TGDGDIMMRF
LPTLLAVEAM RAGKKPAEAA EVGIRRISKH YKDFSGAVIA VDRLGQYGAA CYGMTEFPFV
VSNPSKTDIP SRQESVKCIT GKEAVNVV
