ID   A0A0S2S306_9BACL        Unreviewed;       380 AA.
AC   A0A0S2S306;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   10-APR-2019, entry version 10.
DE   SubName: Full=L-asparaginase {ECO:0000313|EMBL:ALP36110.1};
GN   ORFNames=ASL14_07925 {ECO:0000313|EMBL:ALP36110.1};
OS   Paenibacillus sp. IHB B 3084.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=867076 {ECO:0000313|EMBL:ALP36110.1};
RN   [1] {ECO:0000313|EMBL:ALP36110.1, ECO:0000313|Proteomes:UP000056285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHB B 3084 {ECO:0000313|EMBL:ALP36110.1,
RC   ECO:0000313|Proteomes:UP000056285};
RA   Dhar H., Swarnkar M.K., Rana A., Kaushal K., Singh A.K., Gulati A.;
RT   "Complete Genome Sequencing of Paenibacillus sp. IHB B 3084.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family.
CC       {ECO:0000256|RuleBase:RU004456}.
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DR   EMBL; CP013203; ALP36110.1; -; Genomic_DNA.
DR   EnsemblBacteria; ALP36110; ALP36110; ASL14_07925.
DR   KEGG; paih:ASL14_07925; -.
DR   KO; K01424; -.
DR   Proteomes; UP000056285; Chromosome.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006528; P:asparagine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1170; -; 1.
DR   Gene3D; 3.40.50.40; -; 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   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF53774; SSF53774; 1.
DR   TIGRFAMs; TIGR00520; asnASE_II; 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   Complete proteome {ECO:0000313|Proteomes:UP000056285};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    380       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006604018.
FT   DOMAIN       56    248       Asparaginase. {ECO:0000259|Pfam:PF00710}.
FT   DOMAIN      269    377       Asparaginase_C. {ECO:0000259|Pfam:
FT                                PF17763}.
FT   REGION      145    146       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001220-2}.
FT   ACT_SITE     65     65       {ECO:0000256|PROSITE-ProRule:PRU10099}.
FT   ACT_SITE     65     65       Acyl-ester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR604550-50}.
FT   ACT_SITE     65     65       O-isoaspartyl threonine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR001220-1}.
FT   ACT_SITE    145    145       {ECO:0000256|PROSITE-ProRule:PRU10100}.
FT   BINDING     112    112       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001220-2}.
SQ   SEQUENCE   380 AA;  39781 MW;  4D3ABFCAEFEB8529 CRC64;
     MTMIPLLASF ILGSTLWSGG FTANAAAAAT TSTTVPPSAT TITDKSEKPQ TNNLPNIKIL
     ATGGTIAGSS AVNTDTTDYK AGALGIETLI NAVPEMKSIA NVSGEQVVNV GSPDINNDIL
     LKLAKRTNEL LARDDVDGIV ITHGTDTLEE TAYFLNLVVN SDKPVVVVGS MRPATAISAD
     GPFNLYNAVK VAGASASKGQ GVLVLLNDRI GAARYITKTN TTTVDTFKSV EQGYLGAVVG
     DQVYYYNKST HKHTTASMFD ISILTQLPQV DILYEYQNNG RYLYDAAVAA GAKGIVVAGS
     GNGSLSKTST EGAEAAGKKG VIIARSSRVG SGIVSPSTKD AASNFVSTDS LNPQKARILL
     MLALTQTHDV KEIQSFFNEY
//