ID   ASPQ_PSEFA              Reviewed;         362 AA.
AC   O68897;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Glutaminase-asparaginase {ECO:0000305};
DE            EC=3.5.1.38 {ECO:0000269|PubMed:10499283};
DE   AltName: Full=L-ASNase/L-GLNase {ECO:0000305};
DE   AltName: Full=L-asparagine/L-glutamine amidohydrolase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ansB {ECO:0000303|PubMed:10499283};
OS   Pseudomonas fluorescens biotype A.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=32035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-31, CATALYTIC
RP   ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 13525 / DSM 50090 / JCM 5963 / NBRC 14160 / NCIMB 9046 / NCTC
RC   10038 / VKM B-894;
RX   PubMed=10499283; DOI=10.1111/j.1574-6968.1999.tb08695.x;
RA   Hueser A., Kloeppner U., Roehm K.H.;
RT   "Cloning, sequence analysis, and expression of ansB from Pseudomonas
RT   fluorescens, encoding periplasmic glutaminase/asparaginase.";
RL   FEMS Microbiol. Lett. 178:327-335(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.38;
CC         Evidence={ECO:0000269|PubMed:10499283};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.38;
CC         Evidence={ECO:0000269|PubMed:10499283};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P10182}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10499283}.
CC   -!- INDUCTION: Induced by glutamate, via the alternate sigma factor 54.
CC       {ECO:0000269|PubMed:10499283}.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR   EMBL; AF056495; AAC33155.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68897; -.
DR   SMR; O68897; -.
DR   World-2DPAGE; 0008:O68897; -.
DR   PRIDE; O68897; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004067; F:asparaginase activity; IEA:InterPro.
DR   GO; GO:0050417; F:glutamin-(asparagin-)ase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Periplasm; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:10499283"
FT   CHAIN           26..362
FT                   /note="Glutaminase-asparaginase"
FT                   /id="PRO_0000002360"
FT   DOMAIN          35..362
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        45
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P10182"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  38735 MW;  E8C640D24C5FF31B CRC64;
     MKSALKTFVP GALALLLLFP VAAQAKEVET KTKLANVVIL ATGGTIAGAG ASAANSATYQ
     AAKVGIEQLI AGVPELSQIA NVRGEQVMQI ASESINNENL LQLGRRVAEL ADSKDVDGIV
     ITHGTDTLEE TAYFLNLVEK TDKPIIVVGS MRPGTAMSAD GMLNLYNAVA VAGSKDARGK
     GVLVTMNDEI QSGRDVSKMI NIKTEAFKSP WGPLGMVVEG KSYWFRLPAK RHTMDSEFDI
     KTIKSLPDVE IAYGYGNVSD TAVKALAQAG AKAIIHAGTG NGSVSSKVVP ALQELRKQGV
     QIIRSSHVNA GGFVLRNAEQ PDDKYDWVVA HDLNPQKARI LAMVALTKTQ DSKELQRMFW
     EY