ID   ASPQ_DELAC              Reviewed;          33 AA.
AC   P83712;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   07-APR-2021, entry version 40.
DE   RecName: Full=Glutaminase-asparaginase;
DE            EC=3.5.1.38;
DE   AltName: Full=L-ASNase/L-GLNase;
DE   AltName: Full=L-asparagine/L-glutamine amidohydrolase;
DE   Flags: Fragments;
GN   Name=ansB;
OS   Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=80866 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=MC1 {ECO:0000305};
RA   Benndorf D., Davidson I., Babel W.;
RT   "Responses of Delftia acidovorans MC1 to chlorophenoxy herbicides and
RT   mechanisms of long-term adaptation.";
RL   Submitted (NOV-2003) to UniProtKB.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-15, AND REPRESSION BY 2,4-DCPP.
RC   STRAIN=MC1 {ECO:0000269|PubMed:15073309};
RX   PubMed=15073309; DOI=10.1099/mic.0.26774-0;
RA   Benndorf D., Davidson I., Babel W.;
RT   "Regulation of catabolic enzymes during long-term exposure of Delftia
RT   acidovorans MC1 to chlorophenoxy herbicides.";
RL   Microbiology 150:1005-1014(2004).
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   -!- 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:0000250|UniProtKB:O68897};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- INDUCTION: Repressed during growth on high concentrations of 2,4-
CC       dichlorophenoxypropionic acid (2,4-DCPP).
CC       {ECO:0000269|PubMed:15073309}.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004067; F:asparaginase activity; IEA:RHEA.
DR   GO; GO:0050417; F:glutamin-(asparagin-)ase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR   PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Periplasm.
FT   CHAIN           <1..>33
FT                   /note="Glutaminase-asparaginase"
FT                   /id="PRO_0000171088"
FT   DOMAIN          <1..>33
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        10
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10099"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         33
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   33 AA;  3099 MW;  F900EE02AD545F39 CRC64;
     NVVVLATGGT IAGAGTNAFA SQXGPLGMVV EGK