ID   AQDB1_RHOER             Reviewed;         381 AA.
AC   A0A0E4AFG7;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Putative 2-heptyl-3-hydroxy-4(1H)-quinolone synthase AqdB1 {ECO:0000305};
DE            EC=1.14.13.182 {ECO:0000305|PubMed:26319870};
DE   AltName: Full=2-heptyl-4-quinolone monooxygenase {ECO:0000305};
DE            Short=HHQ monooxygenase {ECO:0000305};
GN   Name=aqdB1 {ECO:0000303|PubMed:26319870};
GN   ORFNames=XU06_29635 {ECO:0000312|EMBL:AKE01129.1};
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: Could be involved in the degradation of the Pseudomonas
CC       aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4-quinolone) to
CC       anthranilic acid. May catalyze the hydroxylation of HHQ to PQS (2-
CC       heptyl-3-hydroxy-4-quinolone). {ECO:0000269|PubMed:26319870}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-
CC         hydroxy-4(1H)-quinolone + H2O + NAD(+); Xref=Rhea:RHEA:37871,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29472, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:62219; EC=1.14.13.182;
CC         Evidence={ECO:0000305|PubMed:26319870};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37872;
CC         Evidence={ECO:0000305|PubMed:26319870};
CC   -!- INDUCTION: Up-regulated by PQS. {ECO:0000269|PubMed:26319870}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; CP011296; AKE01129.1; -; Genomic_DNA.
DR   RefSeq; WP_046380172.1; NZ_CP011296.1.
DR   AlphaFoldDB; A0A0E4AFG7; -.
DR   SMR; A0A0E4AFG7; -.
DR   EnsemblBacteria; AKE01129; AKE01129; XU06_29635.
DR   KEGG; reb:XU06_29635; -.
DR   PATRIC; fig|1833.80.peg.6102; -.
DR   GO; GO:0102164; F:2-heptyl-3-hydroxy-4(1H)-quinolone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Monooxygenase; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..381
FT                   /note="Putative 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
FT                   AqdB1"
FT                   /id="PRO_0000447581"
SQ   SEQUENCE   381 AA;  40799 MW;  228A231DF8F2ADF7 CRC64;
     MSGVAGHAEV VGGGIGGLSA AIALGKRGWT VRLHERNDEI RASGSGIYLW DNGLAALDYL
     GALDSTLVGA HFGARMQTRD AHNALVASSE VNRAGGPRVV TVARERLINA LLASADAVGV
     EVVTGSTVTR VDAAGRIEFD NGHADADLIV VADGIGSRSR DQLGVKTRRR QLNQKCARVL
     LPREPGMVPS EWVDEYVTFY SGQRFLLYTP CSADLLYLAL VCPSDDAPAT GDPLPREAWI
     ASFPQLAPLI DRIGPTPRWD EFEMLTLDSW SSGRVAILGD AAHAQPPSLG QGGGCAMLSA
     LGLAHSLSKN YDLTTALGEW ESSERSVIQR TQWFSYWLAR ANKLPDRPRS LLLSAAGHSS
     LYRNNRMRAA LTTPTGITSS K