ID   B3R2F3_CUPTR            Unreviewed;       323 AA.
AC   B3R2F3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=Isoaspartyl peptidase {ECO:0000256|ARBA:ARBA00069124};
GN   Name=iaaA {ECO:0000313|EMBL:CAQ69671.1};
GN   OrderedLocusNames=RALTA_A1728 {ECO:0000313|EMBL:CAQ69671.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ69671.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAQ69671.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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DR   EMBL; CU633749; CAQ69671.1; -; Genomic_DNA.
DR   RefSeq; WP_012352991.1; NC_010528.1.
DR   AlphaFoldDB; B3R2F3; -.
DR   GeneID; 29762706; -.
DR   KEGG; cti:RALTA_A1728; -.
DR   eggNOG; COG1446; Bacteria.
DR   HOGENOM; CLU_021603_1_2_4; -.
DR   BioCyc; CTAI977880:RALTA_RS08320-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 1.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-ARBA.
DR   CDD; cd04701; Asparaginase_2; 1.
DR   FunFam; 3.60.20.30:FF:000001; Isoaspartyl peptidase/L-asparaginase; 1.
DR   Gene3D; 3.60.20.30; (Glycosyl)asparaginase; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000246; Peptidase_T2.
DR   PANTHER; PTHR10188; L-ASPARAGINASE; 1.
DR   PANTHER; PTHR10188:SF6; N(4)-(BETA-N-ACETYLGLUCOSAMINYL)-L-ASPARAGINASE; 1.
DR   Pfam; PF01112; Asparaginase_2; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE   4: Predicted;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAQ69671.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001692}.
FT   ACT_SITE        191
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-1"
FT   BINDING         219..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-2"
FT   BINDING         241..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-2"
FT   SITE            190..191
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-3"
SQ   SEQUENCE   323 AA;  33409 MW;  30270EAF1BD38959 CRC64;
     MQAAVIAIHG GAGTITRAAM DAAREREYIE ALQHVLQAGQ RILADGGSAL DAVTEAVRLL
     EECPLFNAGK GAVLTHAGTY ELDAAVMDGA TRNAGAVACV TRLRNPVLAA RAVLDHSEHV
     LFAGAGAEAF AQAQGLELVA PEYYFTQARH DQWQRARGNA GMALLDHDAA TLAAQQARGT
     APIDPDSKFG TVGAVACDCR GNLAAATSTG GVTNKQVGRV GDTPLIGAGC YADDVAAVSA
     TGTGEMFIRT VAAHDVAAQM RYAGLPLDEA ARRVVMEKLP AIQGRGGLIA VDRDGNVTLP
     FNTEGMYRGV ARVGEAVDVS IYG
//