AZOR2_PSEAE
ID AZOR2_PSEAE Reviewed; 202 AA.
AC Q9I2E2;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:24915188};
DE AltName: Full=Azo-dye reductase 2 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase 2 {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:20417637};
GN Name=azoR2 {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000303|PubMed:20417637};
GN OrderedLocusNames=PA1962;
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 CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=20417637; DOI=10.1016/j.jmb.2010.04.023;
RA Ryan A., Laurieri N., Westwood I., Wang C.J., Lowe E., Sim E.;
RT "A novel mechanism for azoreduction.";
RL J. Mol. Biol. 400:24-37(2010).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24915188; DOI=10.1371/journal.pone.0098551;
RA Ryan A., Kaplan E., Nebel J.C., Polycarpou E., Crescente V., Lowe E.,
RA Preston G.M., Sim E.;
RT "Identification of NAD(P)H quinone oxidoreductase activity in azoreductases
RT from P. aeruginosa: azoreductases and NAD(P)H quinone oxidoreductases
RT belong to the same FMN-dependent superfamily of enzymes.";
RL PLoS ONE 9:e98551-e98551(2014).
CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC stress caused by electrophilic quinones (PubMed:24915188). Reduces both
CC benzoquinones and naphthoquinones efficiently (PubMed:24915188).
CC {ECO:0000269|PubMed:24915188}.
CC -!- FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive
CC cleavage of the azo bond in aromatic azo compounds to the corresponding
CC amines (PubMed:20417637). Preferred substrates are the large bis-azo
CC dye Ponceau BS, amaranth and tropaeolin O (PubMed:20417637).
CC {ECO:0000269|PubMed:20417637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+);
CC Xref=Rhea:RHEA:65952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:24915188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65953;
CC Evidence={ECO:0000269|PubMed:24915188};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) =
CC 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH;
CC Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378, ChEBI:CHEBI:15783,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:71579; EC=1.7.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01216, ECO:0000269|PubMed:20417637};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874;
CC Evidence={ECO:0000269|PubMed:20417637};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216}.
CC -!- MISCELLANEOUS: Rate of quinone reduction is higher than reduction of
CC azo substrates, suggesting the enzyme is better suited for carrying out
CC quinone rather than azo reduction. {ECO:0000269|PubMed:24915188}.
CC -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01216}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG05350.1; -; Genomic_DNA.
DR PIR; A83402; A83402.
DR RefSeq; NP_250652.1; NC_002516.2.
DR RefSeq; WP_003113473.1; NZ_QZGE01000030.1.
DR AlphaFoldDB; Q9I2E2; -.
DR SMR; Q9I2E2; -.
DR STRING; 287.DR97_5886; -.
DR PaxDb; Q9I2E2; -.
DR EnsemblBacteria; AAG05350; AAG05350; PA1962.
DR GeneID; 877936; -.
DR KEGG; pae:PA1962; -.
DR PATRIC; fig|208964.12.peg.2045; -.
DR PseudoCAP; PA1962; -.
DR HOGENOM; CLU_088964_0_0_6; -.
DR InParanoid; Q9I2E2; -.
DR OMA; REGWDHS; -.
DR PhylomeDB; Q9I2E2; -.
DR BioCyc; PAER208964:G1FZ6-2000-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:PseudoCAP.
DR Gene3D; 3.40.50.360; -; 1.
DR HAMAP; MF_01216; Azoreductase_type1; 1.
DR InterPro; IPR003680; Flavodoxin_fold.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR023048; NADH:quinone_OxRdtase_FMN_depd.
DR Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..202
FT /note="FMN-dependent NADH:quinone oxidoreductase 2"
FT /id="PRO_0000166348"
FT BINDING 9
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT BINDING 15..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT BINDING 95..98
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT BINDING 139..142
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
SQ SEQUENCE 202 AA; 21290 MW; B6F21D0AEDCD4705 CRC64;
MKLLHIDSSI LGDASASRQL SAELVQAWRQ NEDGLDVTYR DLAADAVAHF SALTLAAGST
PAELRDAALK HEVAVGEEVL EEFLAADVVV IGAPMYNFTI SSQLKAWIDR IAVAGKTFRY
TENGPVGLAG DKKVVIVSTA GGVHAGQPTG AAHEGYLRTV LGFFGITDIE VVRAEGLAYG
EEPRTQAIAA ARRQIAGQFA AA
