AQDB2_RHOER
ID AQDB2_RHOER Reviewed; 384 AA.
AC A0A0E4AFH6;
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=Probable 2-heptyl-3-hydroxy-4(1H)-quinolone synthase AqdB2 {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=aqdB2 {ECO:0000303|PubMed:26319870};
GN ORFNames=XU06_29735 {ECO:0000312|EMBL:AKE01141.1};
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: Involved in the degradation of the Pseudomonas aeruginosa
CC quorum sensing signal molecule HHQ (2-heptyl-4-quinolone) to
CC anthranilic acid. Probably catalyzes the hydroxylation of HHQ to PQS
CC (2-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; AKE01141.1; -; Genomic_DNA.
DR RefSeq; WP_046380184.1; NZ_CP011296.1.
DR AlphaFoldDB; A0A0E4AFH6; -.
DR SMR; A0A0E4AFH6; -.
DR EnsemblBacteria; AKE01141; AKE01141; XU06_29735.
DR KEGG; reb:XU06_29735; -.
DR PATRIC; fig|1833.80.peg.6124; -.
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..384
FT /note="Probable 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
FT AqdB2"
FT /id="PRO_0000447582"
SQ SEQUENCE 384 AA; 41671 MW; A05F79BFD97A5A59 CRC64;
MTQRNAIVVG GGIGGLTAAS ALARQGWRVQ LHERQPEIRA VGAGIYIWDN GLFALDAVHA
YSEAIEGAHE PPSIDMRGQS GKTLMRIKIN GESQPRCLTL LRDQLIKALV NAAKDAGVEL
VTNSSVVAVR PEGEVHFEHG DHSTTDLVVV ADGVHSRLRD SVDLSYSRIR MSQGAARIMI
PQSSHELPAE DRGRILESFH GSRRLLYTPC TPELVYLAFT CDSDDPAISG AYINTSEWSR
SFPTLSDALR ATEGVPATRW DTFEYVRLAS WSRGKVAFLG DAAHAQPPYL GQGGGTAMTN
AIALANAVSS DMELSEALAT WERITRPGIE STQRTSYQQR LLNYVPDRVR NPLVRIAGLT
SNVAKSQLKA TEIRPTLGST GGSR
