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PQSH_PSEAE
ID   PQSH_PSEAE              Reviewed;         382 AA.
AC   Q9I0Q0;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=2-heptyl-3-hydroxy-4(1H)-quinolone synthase;
DE            EC=1.14.13.182;
DE   AltName: Full=2-heptyl-3,4-dihydroxyquinoline synthase;
GN   Name=pqsH; OrderedLocusNames=PA2587;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   FUNCTION, AND NOMENCLATURE.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=12426334; DOI=10.1128/jb.184.23.6472-6480.2002;
RA   Gallagher L.A., McKnight S.L., Kuznetsova M.S., Pesci E.C., Manoil C.;
RT   "Functions required for extracellular quinolone signaling by Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 184:6472-6480(2002).
CC   -!- FUNCTION: Involved in the terminal step of the biosynthesis of
CC       quinolone which in addition to serve as a potent signal for quorum
CC       sensing, chelates iron and promotes the formation of membrane vesicles
CC       (MVs). Catalyzes the hydroxylation of 2-heptyl-4-quinolone (C7-HHQ) to
CC       yield 2-heptyl-3-hydroxy-4-quinolone (PQS).
CC       {ECO:0000269|PubMed:12426334}.
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   -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG05975.1; -; Genomic_DNA.
DR   PIR; E83322; E83322.
DR   RefSeq; NP_251277.1; NC_002516.2.
DR   RefSeq; WP_003090354.1; NZ_QZGE01000008.1.
DR   AlphaFoldDB; Q9I0Q0; -.
DR   SMR; Q9I0Q0; -.
DR   STRING; 287.DR97_5458; -.
DR   PaxDb; Q9I0Q0; -.
DR   PRIDE; Q9I0Q0; -.
DR   DNASU; 879540; -.
DR   EnsemblBacteria; AAG05975; AAG05975; PA2587.
DR   GeneID; 879540; -.
DR   KEGG; pae:PA2587; -.
DR   PATRIC; fig|208964.12.peg.2708; -.
DR   PseudoCAP; PA2587; -.
DR   HOGENOM; CLU_009665_19_5_6; -.
DR   InParanoid; Q9I0Q0; -.
DR   OMA; RWMLGYD; -.
DR   PhylomeDB; Q9I0Q0; -.
DR   BioCyc; MetaCyc:MON-16010; -.
DR   BioCyc; PAER208964:G1FZ6-2626-MON; -.
DR   BRENDA; 1.14.13.182; 5087.
DR   Proteomes; UP000002438; 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   GO; GO:0004497; F:monooxygenase activity; IDA:PseudoCAP.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IDA:PseudoCAP.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR044560; MO/PqsH.
DR   PANTHER; PTHR45934; PTHR45934; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Monooxygenase; NAD; Oxidoreductase; Quorum sensing; Reference proteome.
FT   CHAIN           1..382
FT                   /note="2-heptyl-3-hydroxy-4(1H)-quinolone synthase"
FT                   /id="PRO_0000429450"
SQ   SEQUENCE   382 AA;  42081 MW;  201AF7A4F00470A1 CRC64;
     MTVLIQGAGI AGLALAREFT KAGIDWLLVE RASEIRPIGT GITLASNALT ALSSTLDLDR
     LFRRGMPLAG INVYAHDGSM LMSMPSSLGG NSRGGLALQR HELHAALLEG LDESRIRVGV
     SIVQILDGLD HERVTLSDGT VHDCSLVVGA DGIRSSVRRY VWPEATLRHS GETCWRLVVP
     HRLEDAELAG EVWGHGKRLG FIQISPREMY VYATLKVRRE EPEDEEGFVT PQRLAAHYAD
     FDGIGASIAR LIPSATTLVH NDLEELAGAS WCRGRVVLIG DAAHAMTPNL GQGAAMALED
     AFLLARLWCL APRAETLILF QQQREARIEF IRKQSWIVGR LGQWESPWSV WLRNTLVRLV
     PNASRRRLHQ RLFTGVGEMA AQ
 
 
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