ID   AQDC1_RHOER             Reviewed;         278 AA.
AC   A0A0E4AE72;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=2-heptyl-3-hydroxy-4-quinolone dioxygenase AqdC1 {ECO:0000305};
DE            Short=PQS dioxygenase {ECO:0000303|PubMed:26319870};
DE            EC=1.13.11.- {ECO:0000269|PubMed:26319870};
GN   Name=aqdC1 {ECO:0000303|PubMed:26319870};
GN   ORFNames=XU06_29640 {ECO:0000312|EMBL:AKE01130.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, 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. Catalyzes the
CC       cleavage of PQS to form N-octanoylanthranilic acid and carbon monoxide.
CC       {ECO:0000269|PubMed:26319870}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-heptyl-3-hydroxy-4(1H)-quinolone + O2 = CO + H(+) + N-
CC         octanoylanthranilate; Xref=Rhea:RHEA:60352, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29472,
CC         ChEBI:CHEBI:143722; Evidence={ECO:0000269|PubMed:26319870};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60353;
CC         Evidence={ECO:0000269|PubMed:26319870};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27 uM for PQS {ECO:0000269|PubMed:26319870};
CC         Note=kcat is 20.5 sec(-1). {ECO:0000269|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; AKE01130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E4AE72; -.
DR   SMR; A0A0E4AE72; -.
DR   ESTHER; rhoer-aqdC1; HOD-cofactorfree-dioxygenase.
DR   ESTHER; rhoer-aqdC2; HOD-cofactorfree-dioxygenase.
DR   EnsemblBacteria; AKE01130; AKE01130; XU06_29640.
DR   KEGG; reb:XU06_29640; -.
DR   PATRIC; fig|1833.80.peg.6103; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Oxidoreductase; Plasmid.
FT   CHAIN           1..278
FT                   /note="2-heptyl-3-hydroxy-4-quinolone dioxygenase AqdC1"
FT                   /id="PRO_0000447583"
FT   DOMAIN          29..158
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        250
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:B1MFK2"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B1MFK2"
FT   SITE            127
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000250|UniProtKB:B1MFK2"
SQ   SEQUENCE   278 AA;  30938 MW;  C1043B9CB3A9BB95 CRC64;
     MNMPQLSTIQ IGDHELAYLD NKLTSAVTPT IVMLPGWCGD HHSFSELIPQ LNDTHRVVAV
     NWRGHAPVPH DVSDFGYAEQ AQDALAILDA IGVDEFLPVS ASHGGWALVQ LLVDAGPARA
     RAGVVLDWLM RRPTPEFTAA LLSLQDPEGW VDSCRALFHT WRPNDSDWVE SRVERAKEFG
     FDMWARSGRV ISGAYGEHGT PLEFMKTITP ERHIRHLFST PSDSDYVAPQ EAFASENEWF
     SYALLGGTSH FPHLEMPDRV AAHIVELAKN TYQAGAMR