UniProt functional annotation for P41407



	UniProt functional annotation for P41407

UniProt code: P41407.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Can reduce several benzo-, naphtho-, and anthraquinone compounds. {ECO:0000269|PubMed:19666717}.

Function: Also exhibits azoreductase activity (PubMed:11583992, PubMed:18337254). Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines (PubMed:11583992, PubMed:18337254). Can reduce ethyl red, methyl red and p-methyl red, but is not able to convert sulfonated azo dyes (PubMed:11583992, PubMed:18337254, PubMed:23795903). The stoichiometry implies that 2 cycles of the ping-pong mechanism are required for the cleavage of the azo bond (PubMed:11583992). Can also act as a nitroreductase and is able to reduce nitro compounds such as 7-nitrocoumarin-3-carboxylic acid (7NCCA) (PubMed:23795903). {ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254, ECO:0000269|PubMed:23795903}.

Catalytic activity: Reaction=2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+); Xref=Rhea:RHEA:65952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225; Evidence={ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:19666717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65953; Evidence={ECO:0000269|PubMed:19666717};

Catalytic activity: Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378, ChEBI:CHEBI:15783, ChEBI:CHEBI:16567, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:71579; EC=1.7.1.17; Evidence={ECO:0000255|HAMAP- Rule:MF_01216, ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874; Evidence={ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254};

Cofactor: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254, ECO:0000269|PubMed:19666717}; Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254};

Activity regulation: The azo reduction activity is inhibited by dicoumarol. {ECO:0000269|PubMed:11583992}.

Biophysicochemical properties: Kinetic parameters: KM=8.1 uM for anthaquinone-2-sulfonate {ECO:0000269|PubMed:19666717}; KM=14.6 uM for antraquinone-2,6-disulfonate {ECO:0000269|PubMed:19666717}; KM=87.3 uM for 2-hydroxy-1,4-naphthoquinone {ECO:0000269|PubMed:19666717}; KM=1704 uM for 2-methyl-1,4-benzoquinone {ECO:0000269|PubMed:19666717}; KM=17.9 uM for methyl red {ECO:0000269|PubMed:11583992}; KM=41.9 uM for methyl red {ECO:0000269|PubMed:18337254}; KM=266 uM for p-methyl red {ECO:0000269|PubMed:18337254}; KM=31.6 uM for NADH {ECO:0000269|PubMed:11583992}; KM=70.6 uM for NADH {ECO:0000269|PubMed:18337254}; Note=kcat is 1.1 sec(-1) with anthaquinone-2-sulfonate as substrate. kcat is 2.6 sec(-1) with antraquinone-2,6-disulfonate as substrate. kcat is 5.8 sec(-1) with 2-hydroxy-1,4-naphthoquinone as substrate. kcat is 72.0 sec(-1) with 2-methyl-1,4-benzoquinone as substrate. {ECO:0000269|PubMed:19666717};

Subunit: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:16684776, ECO:0000269|PubMed:18337254}.

Induction: Expression is induced by electrophiles, including 2- methylhydroquinone, catechol, menadione, and diamide. {ECO:0000269|PubMed:19666717}.

Disruption phenotype: Deletion mutant displays reduced viability when exposed to electrophilic quinones. {ECO:0000269|PubMed:19666717}.

Miscellaneous: NADH cannot be replaced with NADPH for both reductase activities (PubMed:11583992, PubMed:19666717). Quinone compounds are better substrates than the model azo substrate methyl red (PubMed:19666717). AzoR probably does not contribute to dye reduction in vivo (PubMed:19666717). {ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:19666717}.

Similarity: Belongs to the azoreductase type 1 family. {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Can reduce several benzo-, naphtho-, and anthraquinone compounds. {ECO:0000269\|PubMed:19666717}.



Function:		Also exhibits azoreductase activity (PubMed:11583992, PubMed:18337254). Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines (PubMed:11583992, PubMed:18337254). Can reduce ethyl red, methyl red and p-methyl red, but is not able to convert sulfonated azo dyes (PubMed:11583992, PubMed:18337254, PubMed:23795903). The stoichiometry implies that 2 cycles of the ping-pong mechanism are required for the cleavage of the azo bond (PubMed:11583992). Can also act as a nitroreductase and is able to reduce nitro compounds such as 7-nitrocoumarin-3-carboxylic acid (7NCCA) (PubMed:23795903). {ECO:0000269\|PubMed:11583992, ECO:0000269\|PubMed:18337254, ECO:0000269\|PubMed:23795903}.


Catalytic activity:		Reaction=2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+); Xref=Rhea:RHEA:65952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225; Evidence={ECO:0000255\|HAMAP-Rule:MF_01216, ECO:0000269\|PubMed:19666717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65953; Evidence={ECO:0000269\|PubMed:19666717};
Catalytic activity:		Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378, ChEBI:CHEBI:15783, ChEBI:CHEBI:16567, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:71579; EC=1.7.1.17; Evidence={ECO:0000255\|HAMAP- Rule:MF_01216, ECO:0000269\|PubMed:11583992, ECO:0000269\|PubMed:18337254}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874; Evidence={ECO:0000269\|PubMed:11583992, ECO:0000269\|PubMed:18337254};
Cofactor:		Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255\|HAMAP-Rule:MF_01216, ECO:0000269\|PubMed:11583992, ECO:0000269\|PubMed:18337254, ECO:0000269\|PubMed:19666717}; Note=Binds 1 FMN per subunit. {ECO:0000255\|HAMAP-Rule:MF_01216, ECO:0000269\|PubMed:11583992, ECO:0000269\|PubMed:18337254};
Activity regulation:		The azo reduction activity is inhibited by dicoumarol. {ECO:0000269\|PubMed:11583992}.
Biophysicochemical properties:		Kinetic parameters: KM=8.1 uM for anthaquinone-2-sulfonate {ECO:0000269\|PubMed:19666717}; KM=14.6 uM for antraquinone-2,6-disulfonate {ECO:0000269\|PubMed:19666717}; KM=87.3 uM for 2-hydroxy-1,4-naphthoquinone {ECO:0000269\|PubMed:19666717}; KM=1704 uM for 2-methyl-1,4-benzoquinone {ECO:0000269\|PubMed:19666717}; KM=17.9 uM for methyl red {ECO:0000269\|PubMed:11583992}; KM=41.9 uM for methyl red {ECO:0000269\|PubMed:18337254}; KM=266 uM for p-methyl red {ECO:0000269\|PubMed:18337254}; KM=31.6 uM for NADH {ECO:0000269\|PubMed:11583992}; KM=70.6 uM for NADH {ECO:0000269\|PubMed:18337254}; Note=kcat is 1.1 sec(-1) with anthaquinone-2-sulfonate as substrate. kcat is 2.6 sec(-1) with antraquinone-2,6-disulfonate as substrate. kcat is 5.8 sec(-1) with 2-hydroxy-1,4-naphthoquinone as substrate. kcat is 72.0 sec(-1) with 2-methyl-1,4-benzoquinone as substrate. {ECO:0000269\|PubMed:19666717};
Subunit:		Homodimer. {ECO:0000255\|HAMAP-Rule:MF_01216, ECO:0000269\|PubMed:11583992, ECO:0000269\|PubMed:16684776, ECO:0000269\|PubMed:18337254}.
Induction:		Expression is induced by electrophiles, including 2- methylhydroquinone, catechol, menadione, and diamide. {ECO:0000269\|PubMed:19666717}.
Disruption phenotype:		Deletion mutant displays reduced viability when exposed to electrophilic quinones. {ECO:0000269\|PubMed:19666717}.
Miscellaneous:		NADH cannot be replaced with NADPH for both reductase activities (PubMed:11583992, PubMed:19666717). Quinone compounds are better substrates than the model azo substrate methyl red (PubMed:19666717). AzoR probably does not contribute to dye reduction in vivo (PubMed:19666717). {ECO:0000269\|PubMed:11583992, ECO:0000269\|PubMed:19666717}.
Similarity:		Belongs to the azoreductase type 1 family. {ECO:0000255\|HAMAP-Rule:MF_01216, ECO:0000305}.