ID   A0A0W7TX51_9GAMM        Unreviewed;       352 AA.
AC   A0A0W7TX51;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   25-APR-2018, entry version 16.
DE   SubName: Full=L-asparaginase {ECO:0000313|EMBL:KUE78401.1};
GN   Name=ansB {ECO:0000313|EMBL:KUE78401.1};
GN   ORFNames=ATO46_10430 {ECO:0000313|EMBL:KUE78401.1};
OS   Aeromonas schubertii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=652 {ECO:0000313|EMBL:KUE78401.1, ECO:0000313|Proteomes:UP000054876};
RN   [1] {ECO:0000313|EMBL:KUE78401.1, ECO:0000313|Proteomes:UP000054876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE78401.1,
RC   ECO:0000313|Proteomes:UP000054876};
RA   Liu L., Li Q., Zhang F., Shi B.;
RT   "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family.
CC       {ECO:0000256|RuleBase:RU004456}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUE78401.1}.
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DR   EMBL; LPUO01000055; KUE78401.1; -; Genomic_DNA.
DR   RefSeq; WP_050666808.1; NZ_LPUO01000055.1.
DR   EnsemblBacteria; KUE78401; KUE78401; ATO46_10430.
DR   Proteomes; UP000054876; Unassembled WGS sequence.
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; IPR027473; L-asparaginase_C.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   Pfam; PF00710; Asparaginase; 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:UP000054876};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054876};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    352       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006934602.
FT   DOMAIN       28    220       Asparaginase. {ECO:0000259|Pfam:PF00710}.
FT   REGION      115    116       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001220-2}.
FT   ACT_SITE     36     36       Acyl-ester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR604550-50}.
FT   ACT_SITE     36     36       O-isoaspartyl threonine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR001220-1}.
FT   BINDING      82     82       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001220-2}.
SQ   SEQUENCE   352 AA;  37599 MW;  351C0CEF64735AD2 CRC64;
     MSLPLRKSLI AAVLGMTLSP LAFALPSVHI LATGGTIAGA GQSATQSNYE AGKVAIETLI
     AAVPEMKKVA DVQGEQVVKI GSQDMNDEVW LKLAKRVNEL LAKDDVDGIV ITHGTDTMEE
     TAYFLNLTVK SDKPVVLVGA MRPSTAMSAD GPMNLYNAVV TASDPASKGR GVMVAMNDTV
     LDARDVTKTN TTGVQTFASP NFGPLGYIHN GKIDYQRTPA RLHTSQTPFD VSKLDKLPRV
     GIVYSYANAS DLPAKALVDA KFDGIVSAGV GNGNLYHTLF DTLAKASEKG IRVVRSARVP
     TGSTTLDAEI DDAKYGFVAA ESLNPQKARV LLMLSLTQTQ DPKQIQHYFQ QY
//