ID   AQDB_MYCA9              Reviewed;         375 AA.
AC   B1MFK1;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=2-heptyl-3-hydroxy-4(1H)-quinolone synthase {ECO:0000305|PubMed:28303132};
DE            Short=PQS synthase {ECO:0000305|PubMed:28303132};
DE            EC=1.14.13.182 {ECO:0000269|PubMed:28303132};
DE   AltName: Full=2-heptyl-4(1H)-quinolone monooxygenase {ECO:0000305|PubMed:28303132};
DE            Short=HHQ monooxygenase {ECO:0000305|PubMed:28303132};
GN   Name=aqdB {ECO:0000303|PubMed:28303132};
GN   OrderedLocusNames=MAB_0302 {ECO:0000312|EMBL:CAM60401.1};
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS   13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC   1543;
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC   1543;
RX   PubMed=28303132; DOI=10.3389/fmicb.2017.00339;
RA   Birmes F.S., Wolf T., Kohl T.A., Rueger K., Bange F., Kalinowski J.,
RA   Fetzner S.;
RT   "Mycobacterium abscessus subsp. abscessus Is Capable of Degrading
RT   Pseudomonas aeruginosa Quinolone Signals.";
RL   Front. Microbiol. 8:339-339(2017).
CC   -!- FUNCTION: Involved in the degradation pathway of the Pseudomonas
CC       aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4(1H)-
CC       quinolone) to anthranilate. Catalyzes the hydroxylation of HHQ to PQS
CC       (2-heptyl-3-hydroxy-4(1H)-quinolone). {ECO:0000269|PubMed:28303132}.
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:0000269|PubMed:28303132};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37872;
CC         Evidence={ECO:0000269|PubMed:28303132};
CC   -!- INDUCTION: Up-regulated by PQS. {ECO:0000269|PubMed:28303132}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; CU458896; CAM60401.1; -; Genomic_DNA.
DR   RefSeq; WP_005090569.1; NZ_MLCG01000005.1.
DR   AlphaFoldDB; B1MFK1; -.
DR   SMR; B1MFK1; -.
DR   EnsemblBacteria; CAM60401; CAM60401; MAB_0302.
DR   GeneID; 66970685; -.
DR   KEGG; mab:MAB_0302; -.
DR   OMA; KEDGWNI; -.
DR   Proteomes; UP000007137; Chromosome.
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.
FT   CHAIN           1..375
FT                   /note="2-heptyl-3-hydroxy-4(1H)-quinolone synthase"
FT                   /id="PRO_0000448003"
SQ   SEQUENCE   375 AA;  39751 MW;  302332A337EE1A5A CRC64;
     MSSGHAEVVG GGIGGLTAAT ALALRGWTVR LHERDTRIRT VGAGIYVWDN GLEALDTIGA
     AAEGLDDAYE APAITVRASD GRPLYRIDVN QPGGARCVTL LRDRLIGALH VAAEHAGVEV
     CTGSAAVSAT ADGTVEFSTG TSTRADLVVA ADGVHSLLRD RLGISYRRIR MRQGAARVMV
     SGERPFIPGM DVDQHHEFLG GRRRLLYTPC TATQTYLAFV ADNDDTATVG PELDLAAWAR
     AFPLLVPVFD AARGRALIRW DNFELIRLST WSHGRVAVLG DAAHAQPPYV GQGGGTAMNS
     AVGLAAAVSE SADVEDGLNR WEQALRPPIE KAQTTSYRMR LIGSVPEVLR GPLLGALGRS
     RSSATSQLIK KRSAA