ASPG_SPOFR
ID ASPG_SPOFR Reviewed; 320 AA.
AC O02467;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase;
DE EC=3.5.1.26;
DE AltName: Full=Aspartylglucosaminidase;
DE Short=AGA;
DE AltName: Full=Glycosylasparaginase;
DE AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase;
DE Contains:
DE RecName: Full=Glycosylasparaginase alpha chain;
DE Contains:
DE RecName: Full=Glycosylasparaginase beta chain;
DE Flags: Fragment;
OS Spodoptera frugiperda (Fall armyworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7108;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=8877373; DOI=10.1093/glycob/6.5.527;
RA Liu Y., Dunn G.S., Aronson N.N. Jr.;
RT "Purification, biochemistry and molecular cloning of an insect
RT glycosylasparaginase from Spodoptera frugiperda.";
RL Glycobiology 6:527-536(1996).
CC -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC the peptide of asparagine-linked glycoproteins.
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 -!- SUBUNIT: Heterotetramer of two alpha and two beta chains or heterodimer
CC of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Lysosome.
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 (Probable).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; S83425; AAB50885.2; -; mRNA.
DR AlphaFoldDB; O02467; -.
DR SMR; O02467; -.
DR MEROPS; T02.001; -.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IEA:UniProtKB-EC.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Autocatalytic cleavage; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW Protease.
FT CHAIN 1..183
FT /note="Glycosylasparaginase alpha chain"
FT /id="PRO_0000002345"
FT CHAIN 184..320
FT /note="Glycosylasparaginase beta chain"
FT /id="PRO_0000002346"
FT ACT_SITE 184
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 212..215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235..238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..46
FT /evidence="ECO:0000250"
FT DISULFID 141..157
FT /evidence="ECO:0000250"
FT DISULFID 295..320
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 320 AA; 34841 MW; D0C57ACA6F2A6183 CRC64;
EKNMPIVITT WSFTNASQKA WEVLKDEGKA LDAVEQGGIV CENEQCDRTV GYGGSPDEDG
ETTLDAFIMD GSTMNVGAVA ALRRIKSAIS VARHVMEYTT HSFLAGELAT KFAVEMGFKE
ESLSTDESRE LWSKWRFEKQ CQPNFRKNVK PDPRKHCGPY HKKRNFVDYI HPEVFVVDQY
NHDTIGMVAV DSKGDVAAGT STNGAKFKIP GRVGDSPIPG AGAYADNTVG GAAATGNGDT
MMRFLPSFLA VEEMRRGASP ANAAKTAIKR ISAHHPDFMG AVIALSKNGQ YGAACNGIET
FPFVVQDKTR KTFEVVTIKC
