ID   A0KPS0_AERHH            Unreviewed;       352 AA.
AC   A0KPS0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   04-NOV-2026, entry version 107.
DE   RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE            EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
GN   OrderedLocusNames=AHA_3828 {ECO:0000313|EMBL:ABK37200.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Aeromonadales; Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37200.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37200.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC   KCTC 2358 / NCIMB 9240 / NCTC 8049
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-asparagine + H2O = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00049366};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010518, ECO:0000256|RuleBase:RU004456}.
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DR   EMBL; CP000462; ABK37200.1; -; Genomic_DNA.
DR   RefSeq; WP_011707533.1; NC_008570.1.
DR   AlphaFoldDB; A0KPS0; -.
DR   SMR; A0KPS0; -.
DR   STRING; 380703.AHA_3828; -.
DR   PaxDb; 380703-AHA_3828; -.
DR   EnsemblBacteria; ABK37200; ABK37200; AHA_3828.
DR   GeneID; 4489928; -.
DR   KEGG; aha:AHA_3828; -.
DR   PATRIC; fig|380703.7.peg.3801; -.
DR   eggNOG; COG0252; Bacteria.
DR   HOGENOM; CLU_019134_1_2_6; -.
DR   OrthoDB; 9788068at2; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00411; L-asparaginase_like; 1.
DR   FunFam; 3.40.50.1170:FF:000001; L-asparaginase 2; 1.
DR   FunFam; 3.40.50.40:FF:000002; L-asparaginase 2; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 1.
DR   InterPro; IPR004550; AsnASE_II.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   NCBIfam; NF008304; ansB; 1.
DR   NCBIfam; TIGR00520; asnASE_II; 1.
DR   PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR   PANTHER; PTHR11707; L-ASPARAGINASE; 1.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PIRSF; PIRSF500176; L_ASNase; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR   PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABK37200.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..352
FT                   /note="asparaginase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002625397"
FT   DOMAIN          27..220
FT                   /note="L-asparaginase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00710"
FT   DOMAIN          239..349
FT                   /note="Asparaginase/glutaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17763"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10099"
FT   ACT_SITE        36
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001220-1"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
FT   BINDING         115..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
SQ   SEQUENCE   352 AA;  37583 MW;  14BD4E3F7FB10542 CRC64;
     MTLPIRKTLL AAVLGLTLSP MAMALPNVHI LATGGTIAGA GQSATQSNYE AGKVAIETLI
     AAVPEMKNVA DVQGEQVVKI GSQDMNDEVW LKLAKRVNEL LAKDDVDGIV ITHGTDTMEE
     TAYFLNLTVK SDKPVVLVGA MRPSTAMSAD GPMNLYNAVV TASDPASKGR GVMVAMNDTV
     LDARDVTKTN TTGVQTFASP NFGPLGYIHN GKIDYQRSPA RLHTSKTPFD VSKLDKLPQV
     GIVYSYANAT DLPAKAMVDA KFDGIVSAGV GNGNLYHTLF DTLAKASKDG IRVVRSARVP
     TGSTTLDAEI DDAKYGFVAA ETLNPQKARI LLMLSLTQSK DPAQIQRWFQ QF
//