ID   ASGX_NOSS1              Reviewed;         318 AA.
AC   Q8YQB1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE            EC=3.4.19.5;
DE   AltName: Full=Beta-aspartyl-peptidase;
DE   AltName: Full=Isoaspartyl dipeptidase;
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;
GN   OrderedLocusNames=all3922;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 180-185, FUNCTION, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE.
RX   PubMed=11988085; DOI=10.1042/bj3640129;
RA   Hejazi M., Piotukh K., Mattow J., Deutzmann R., Volkmer-Engert R.,
RA   Lockau W.;
RT   "Isoaspartyl dipeptidase activity of plant-type asparaginases.";
RL   Biochem. J. 364:129-136(2002).
CC   -!- FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation
CC       (also known as beta-Asp residues). Probably performs the final step in
CC       the degradation of the reserve polymer cyanophycin (depolymerizes the
CC       building block L-beta-Asp-Arg). Also has L-asparaginase activity.
CC       {ECO:0000269|PubMed:11988085}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.0 mM for L-Asn;
CC         KM=1.54 mM for L-beta-Asp-Ala;
CC         KM=0.27 mM for L-beta-Asp-Arg;
CC         KM=0.52 mM for L-beta-Asp-Gly;
CC         KM=0.26 mM for L-beta-Asp-Leu;
CC         KM=0.53 mM for L-beta-Asp-Lys;
CC         KM=0.68 mM for L-beta-Asp-Phe;
CC         Vmax=2.2 umol/min/mg enzyme with L-Asn as substrate;
CC         Vmax=12.3 umol/min/mg enzyme with L-beta-Asp-Ala as substrate;
CC         Vmax=5.7 umol/min/mg enzyme with L-beta-Asp-Arg as substrate;
CC         Vmax=2.7 umol/min/mg enzyme with L-beta-Asp-Gly as substrate;
CC         Vmax=4.5 umol/min/mg enzyme with L-beta-Asp-Leu as substrate;
CC         Vmax=22.2 umol/min/mg enzyme with L-beta-Asp-Lys as substrate;
CC         Vmax=20.1 umol/min/mg enzyme with L-beta-Asp-Phe as substrate;
CC         Note=Enzyme is inactive on alpha-aspartyl dipeptides.;
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers. {ECO:0000305|PubMed:11988085}.
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.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000019; BAB75621.1; -; Genomic_DNA.
DR   PIR; AC2296; AC2296.
DR   RefSeq; WP_010998063.1; NZ_RSCN01000043.1.
DR   AlphaFoldDB; Q8YQB1; -.
DR   SMR; Q8YQB1; -.
DR   STRING; 103690.17133056; -.
DR   MEROPS; T02.002; -.
DR   EnsemblBacteria; BAB75621; BAB75621; BAB75621.
DR   KEGG; ana:all3922; -.
DR   eggNOG; COG1446; Bacteria.
DR   OMA; YSRMRWK; -.
DR   OrthoDB; 890789at2; -.
DR   BioCyc; MetaCyc:MON-21306; -.
DR   SABIO-RK; Q8YQB1; -.
DR   Proteomes; UP000002483; Chromosome.
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   1: Evidence at protein level;
KW   Autocatalytic cleavage; Direct protein sequencing; Hydrolase; Protease;
KW   Reference proteome.
FT   CHAIN           1..179
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit alpha"
FT                   /id="PRO_0000344063"
FT   CHAIN           180..318
FT                   /note="Isoaspartyl peptidase/L-asparaginase subunit beta"
FT                   /id="PRO_0000344064"
FT   ACT_SITE        180
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            179..180
FT                   /note="Cleavage; by autolysis"
SQ   SEQUENCE   318 AA;  33638 MW;  BB922A9D87C7B557 CRC64;
     MKSQVQPKLI IHGGAGSSLH GKGGLEAVRQ TLHAVVEEVY ALLLSGVNAS VAVVRGCQLL
     EDEPRFNAGT GSVLQSDGQI RMSASIMDGA LGRFSGVINV SRVKNPIELA QFLQNSPDRV
     LSDYGSAELA REMQIPSYNA LTELRLQEWI QERQDNFKRT MAGVIAEPEL LETSNAGRGT
     IGVVALDTYG KLAVGTSTGG KGFERIGRVS DSAMPAGNYA TSYAAVSCTG IGEDIIDECL
     APKIVIRVTD GLSLQDSMQR SFAEAHDNKR DFGAIALDAN GAIAWGKTCD IILAAFHDGE
     KIGDTLELAV GTQVGSIS