ID   ASPG_LUPAN              Reviewed;         325 AA.
AC   P30364;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE            EC=3.4.19.5;
DE   AltName: Full=L-asparagine amidohydrolase;
DE   Contains:
DE     RecName: Full=Isoaspartyl peptidase/L-asparaginase subunit alpha;
DE   Contains:
DE     RecName: Full=Isoaspartyl peptidase/L-asparaginase subunit beta;
DE   Flags: Precursor;
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Uniharvest; TISSUE=Seed;
RX   PubMed=1391778; DOI=10.1007/bf00014503;
RA   Dickson J.M.J.J., Vincze E., Grant M.R., Smith L.A., Rodber K.A.,
RA   Farnden K.J.F., Reynolds P.H.S.;
RT   "Molecular cloning of the gene encoding developing seed L-asparaginase from
RT   Lupinus angustifolius.";
RL   Plant Mol. Biol. 20:333-336(1992).
CC   -!- FUNCTION: Acts in asparagine catabolism but also in the final steps of
CC       protein degradation via hydrolysis of a range of isoaspartyl
CC       dipeptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC         polypeptide.; EC=3.4.19.5;
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Developing seeds.
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:0000305}.
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DR   EMBL; X60691; CAA43099.1; -; Genomic_DNA.
DR   PIR; S24757; S24757.
DR   RefSeq; XP_019439000.1; XM_019583455.1.
DR   AlphaFoldDB; P30364; -.
DR   SMR; P30364; -.
DR   MEROPS; T02.A01; -.
DR   EnsemblPlants; OIW19678; OIW19678; TanjilG_18488.
DR   GeneID; 109344701; -.
DR   Gramene; OIW19678; OIW19678; TanjilG_18488.
DR   KEGG; lang:109344701; -.
DR   OrthoDB; 797598at2759; -.
DR   GO; GO:0008798; F:beta-aspartyl-peptidase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Hydrolase; Protease.
FT   CHAIN           1..192
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit alpha"
FT                   /id="PRO_0000045452"
FT   CHAIN           193..325
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit beta"
FT                   /id="PRO_0000045453"
FT   ACT_SITE        193
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         221..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            192..193
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  34312 MW;  4F9368FFDFF084A6 CRC64;
     MGGWSIALHG GAGDIPFSLP PERRQPREEG LRHCLQIGVE ALKSQKPPLD VVELVVRELE
     NIQHFNAGIG SVLTNSGTVE MEASIMDGKT MKCGAVSGLS TVLNPISLAR LVMDKTPHIY
     LAFQGAQDFA KQQGVETVDS SHFITAENVE RLKLAIEANR VQVDYSQYNY PQPAQDDAEK
     ELPLANGDSQ IGTVGCVAVD SHGNLASATS TGGLVNKMVG RIGDTPLIGA GTYANELCAV
     SATGKGEAII SATVARDVAA LMEFKGLSLK EAADYVVHER TPKGTVGLIA VSAAGEIAMP
     FNTTGMFRAS ATEDGYSEIA IWPTT