ID   ASPG_BACLI              Reviewed;         322 AA.
AC   P30363;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-SEP-2026, entry version 86.
DE   RecName: Full=L-asparaginase;
DE            Short=L-ASNase;
DE            EC=3.5.1.1;
DE   AltName: Full=L-asparagine amidohydrolase;
GN   Name=ansA;
OS   Bacillus licheniformis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1916233; DOI=10.1016/0378-1097(91)90239-7;
RA   van Dijl J.M., de Jong A., Smith H., Bron S., Venema G.;
RT   "Lack of specific hybridization between the lep genes of Salmonella
RT   typhimurium and Bacillus licheniformis.";
RL   FEMS Microbiol. Lett. 65:345-351(1991).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR   EMBL; Z11497; CAA77574.1; -; Genomic_DNA.
DR   PIR; S18999; S18999.
DR   AlphaFoldDB; P30363; -.
DR   SMR; P30363; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0006528; P:asparagine metabolic process; IEA:InterPro.
DR   CDD; cd08964; L-asparaginase_II; 1.
DR   FunFam; 3.40.50.1170:FF:000001; 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   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   SFLD; SFLDS00057; Glutaminase/Asparaginase; 1.
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   Cytoplasm; Hydrolase.
FT   CHAIN           1..322
FT                   /note="L-asparaginase"
FT                   /id="PRO_0000171076"
FT   DOMAIN          3..322
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        13
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT                   ECO:0000255|PROSITE-ProRule:PRU10100"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         89..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  35442 MW;  7048BEC52D0B1DFB CRC64;
     MNKKVALITT GGTIASRKTE SGRLAAGAIS GPELAEMCSL PEDVQIDVYP AFQLPSMHIT
     FQHLLELKQT IERVFQDGGY DGAVVTHGTD TLEETAYFLD LTIEDERPVV VTGSQRAPEQ
     QGTDAYTNIR HAVYTACSPD IKGAGTVVVF NERIFNARYV KKVHASNLQG FDVFGFGYLG
     IIDNDKVYVY QKLLKRDVHQ LQRPLPAVDI VKCYLDGDGK FIRAAVREGV EGIVLEGVGR
     GQVPPNMMAD IEQALNQGVY IVITTSAEEG EVYTTYDYAG SSYDLAKKGV ILGKDYDSKK
     ARMKLAVLLA SYKEGIKDKF CY
//