ID   AQDA1_RHOER             Reviewed;         302 AA.
AC   A0A0G3FWY4;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Probable N-octanoylanthranilate hydrolase AqdA1 {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000305|PubMed:26319870};
GN   Name=aqdA1 {ECO:0000303|PubMed:26319870};
GN   ORFNames=XU06_29630 {ECO:0000312|EMBL:AKJ93518.1};
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 AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; CP011296; AKJ93518.1; -; Genomic_DNA.
DR   RefSeq; WP_052741019.1; NZ_CP011296.1.
DR   AlphaFoldDB; A0A0G3FWY4; -.
DR   SMR; A0A0G3FWY4; -.
DR   EnsemblBacteria; AKJ93518; AKJ93518; XU06_29630.
DR   KEGG; reb:XU06_29630; -.
DR   PATRIC; fig|1833.80.peg.6101; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Plasmid.
FT   CHAIN           1..302
FT                   /note="Probable N-octanoylanthranilate hydrolase AqdA1"
FT                   /id="PRO_0000447585"
FT   REGION          280..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   302 AA;  33270 MW;  6F757D12877C177C CRC64;
     MTANGDVRQP DARTYFTHQH PADYHADWKG YYERALVSRA RSMERFAHEL DIRYGTDPHQ
     ILNVFRAADT RSAPVIIYFH GGRWREGHPA FYDHLADTWA ADGAVFVSAG YRLTPEHSIA
     DSVADAWAVT DWVVRNIAAY GGDPSRITVA GHSSGGHLAS MVALTDNCAV SIVGLVCMSA
     PVDLRTLGFW DDDTLSPHLQ ISRVPRRVVV SFGDPEPNRK GDDALRLTRE GQMLADSLVA
     YGASLRTVVL PNADHVRTAT AFADRQSPLF GAAHSVIFGD STEDRSAPRS PHFQEEKQSC
     PE