PQSH_PSEAB
ID PQSH_PSEAB Reviewed; 382 AA.
AC Q02N79;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=PA14_30630;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=UCBPP-PA14;
RX PubMed=14739337; DOI=10.1073/pnas.0307694100;
RA Deziel E., Lepine F., Milot S., He J., Mindrinos M.N., Tompkins R.G.,
RA Rahme L.G.;
RT "Analysis of Pseudomonas aeruginosa 4-hydroxy-2-alkylquinolines (HAQs)
RT reveals a role for 4-hydroxy-2-heptylquinoline in cell-to-cell
RT communication.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1339-1344(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=UCBPP-PA14;
RX PubMed=20662781; DOI=10.1111/j.1365-2958.2010.07303.x;
RA Schertzer J.W., Brown S.A., Whiteley M.;
RT "Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours
RT via substrate limitation of PqsH.";
RL Mol. Microbiol. 77:1527-1538(2010).
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). PqsH is also able to
CC hydroxylate HHQ analogs having alkyl side-chain lengths of 3 (C3-HHQ),
CC 5 (C5-HHQ) and 9 (C9-HHQ) carbons, however catalytic efficiencies are
CC significantly reduced for substrates with alkyl side-chain lengths
CC below 7 carbons. {ECO:0000269|PubMed:14739337,
CC ECO:0000269|PubMed:20662781}.
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:20662781};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 nM for 2-heptyl-4-quinolone (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20662781};
CC KM=520 nM for oxygen (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20662781};
CC KM=32 uM for NADH (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20662781};
CC KM=740 uM for NADPH (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20662781};
CC Note=kcat is 1.2 min(-1) for hydroxylation with oxygen (at 37 degrees
CC Celsius). kcat is 2.7 min(-1) for hydroxylation with 2-heptyl-4-
CC quinolone (at 37 degrees Celsius). kcat is 3.2 min(-1) for
CC hydroxylation with NADH (at 37 degrees Celsius). kcat is 3.8 min(-1)
CC for hydroxylation with NADPH (at 37 degrees Celsius).;
CC -!- INDUCTION: By LasR. {ECO:0000269|PubMed:14739337}.
CC -!- MISCELLANEOUS: Oxygen is essential for PQS production and anaerobic
CC P.aeruginosa produces undetectable levels of MVs and display reduced
CC killing of prokaryotic and eukaryotic cells.
CC {ECO:0000305|PubMed:20662781}.
CC -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ11810.1; -; Genomic_DNA.
DR RefSeq; WP_003119987.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02N79; -.
DR SMR; Q02N79; -.
DR PRIDE; Q02N79; -.
DR EnsemblBacteria; ABJ11810; ABJ11810; PA14_30630.
DR KEGG; pau:PA14_30630; -.
DR HOGENOM; CLU_009665_19_5_6; -.
DR OMA; RWMLGYD; -.
DR BioCyc; PAER208963:G1G74-2565-MON; -.
DR PHI-base; PHI:3290; -.
DR Proteomes; UP000000653; 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:0009372; P:quorum sensing; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Monooxygenase; NAD; Oxidoreductase; Quorum sensing.
FT CHAIN 1..382
FT /note="2-heptyl-3-hydroxy-4(1H)-quinolone synthase"
FT /id="PRO_0000429449"
SQ SEQUENCE 382 AA; 42054 MW; 7CE9379098D1F99A CRC64;
MTVLIQGAGI AGLALAREFT KAGIDWLLVE RASEIRPIGT GITLASNALT ALSSTLDLDR
LFRRGMPLAG INVYAHDGSM LMSMPSSLGG SSRGGLALQR 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
