ID   AQDA2_RHOER             Reviewed;         454 AA.
AC   A0A0E4AET8;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Probable N-octanoylanthranilate hydrolase AqdA2 {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000305|PubMed:26319870};
GN   Name=aqdA2 {ECO:0000303|PubMed:26319870};
GN   ORFNames=XU06_29730 {ECO:0000312|EMBL:AKE01140.1};
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OG   Plasmid pRLCBG43.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46869 / BG43;
RX   PubMed=26210289; DOI=10.1016/j.jbiotec.2015.07.014;
RA   Rueckert C., Birmes F.S., Mueller C., Niewerth H., Winkler A., Fetzner S.,
RA   Kalinowski J.;
RT   "Complete genome sequence of Rhodococcus erythropolis BG43 (DSM 46869), a
RT   degrader of Pseudomonas aeruginosa quorum sensing signal molecules.";
RL   J. Biotechnol. 211:99-100(2015).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=DSM 46869 / BG43;
RX   PubMed=26319870; DOI=10.1128/aem.02145-15;
RA   Mueller C., Birmes F.S., Rueckert C., Kalinowski J., Fetzner S.;
RT   "Rhodococcus erythropolis BG43 genes mediating Pseudomonas aeruginosa
RT   quinolone signal degradation and virulence factor attenuation.";
RL   Appl. Environ. Microbiol. 81:7720-7729(2015).
CC   -!- FUNCTION: Involved in the degradation of the Pseudomonas aeruginosa
CC       quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-
CC       heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes
CC       the hydrolysis of N-octanoylanthranilic acid to anthranilic acid.
CC       {ECO:0000269|PubMed:26319870}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-octanoylanthranilate = anthranilate + H(+) +
CC         octanoate; Xref=Rhea:RHEA:60356, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:25646,
CC         ChEBI:CHEBI:143722; Evidence={ECO:0000305|PubMed:26319870};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60357;
CC         Evidence={ECO:0000305|PubMed:26319870};
CC   -!- INDUCTION: Up-regulated by PQS. {ECO:0000269|PubMed:26319870}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; CP011296; AKE01140.1; -; Genomic_DNA.
DR   RefSeq; WP_046380183.1; NZ_CP011296.1.
DR   AlphaFoldDB; A0A0E4AET8; -.
DR   SMR; A0A0E4AET8; -.
DR   ESTHER; rhoer-a0a0e4aet8; Carb_B_Bacteria.
DR   EnsemblBacteria; AKE01140; AKE01140; XU06_29730.
DR   KEGG; reb:XU06_29730; -.
DR   PATRIC; fig|1833.80.peg.6123; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Plasmid.
FT   CHAIN           1..454
FT                   /note="Probable N-octanoylanthranilate hydrolase AqdA2"
FT                   /id="PRO_0000447586"
FT   ACT_SITE        185
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        306
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23141"
FT   ACT_SITE        379
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23141"
SQ   SEQUENCE   454 AA;  48937 MW;  6EAE36024893F340 CRC64;
     MFQTVTAPTG VWRGRVTGDV TVFHGIQYAR ADRFAPPQRC EPQLQHLVEV PEPGPIAPQS
     PSRLEGVMGA PSSLKQSEAC LTVTVTTPHL AQPGSLPVLV WLHGGAFLSG SGAWEQYGAE
     QLVRETGIVV VSVNYRLGVL GYLCAPGISS GNLGLLDQIT ALEWVRDNIE AFGGDNGRVT
     LDGQSAGAHS IVAMLGIDRA RSLFSRAIIQ SAPLGLGFHS VEQARRAAEI FEEELGSDPR
     RAVVTDILAA QARTAHRLAG RGAMNSAPPF LPVHGMAPLP FVGEWNGKVA ANAARRKILI
     GNTRDEMAAF FGPHPVFSAM RRVPLAGPQL AGAIQRRVQK VVFDNPVQEF ADRFASAGAS
     VWRYGIGPLH PDNPFGACHC IDIPLLFGDG DTWRDAPMLR PLSPKEIGES GTRTRRYWGE
     FVHTGRISDP AWPMHRPKSR YAHLLTDETI GGSA