ID   ASPG_LUPAL              Reviewed;         325 AA.
AC   P50288;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 69.
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 albus (White lupine) (Lupinus termis).
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=3870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Nyirsegi;
RA   Lamping E., Reddington B.D., Reynolds P.H.S., Farnden K.J.F.;
RT   "Cloning and expression of an asparaginase gene from Lupinus albus.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; L19141; AAA33409.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50288; -.
DR   SMR; P50288; -.
DR   MEROPS; T02.A01; -.
DR   PRIDE; P50288; -.
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   3: Inferred from homology;
KW   Autocatalytic cleavage; Hydrolase; Protease.
FT   CHAIN           1..192
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit alpha"
FT                   /id="PRO_0000045450"
FT   CHAIN           193..325
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit beta"
FT                   /id="PRO_0000045451"
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;  34363 MW;  CCFA1B2E6CF05B90 CRC64;
     MGGWSIALHG GAGDIPFSLP PERRKPREEG LRHCLQIGIE ALKAQNPPLD VVELVVRELE
     NIQHFNAGIG SVLTNSGTVE MEASIMDGNT MKCGAVSGLN TVMNPISLAR QVMDKTPHIF
     LAFQGAQDLG KQQGVETVDS SHFITEENVE RLKLAIEANR VQVDYSQYNY TQPVQDDAEK
     ELPLANGDSQ IGTVGCVAVD SHGNLASATS TGGLVNKMVG RIGDTPLIGA GTYANELCAV
     SATGKGEAII RATVARDVAA LMEFKGLSLK EAADCVVHER TPKGTVGLIA VSAAGEIAMP
     FNTTGMFRAC ATEDGYSEIA IWPTA