AC   MF_01216;
DC   Protein; auto
TR   HAMAP; MF_01216; -; 1; level=0
XX
Names: Azoreductase_type1
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ID   AZOR
DE   RecName: Full=FMN dependent NADH:quinone oxidoreductase;
DE            EC=1.6.5.-;
DE   AltName: Full=Azo-dye reductase;
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase;
DE   AltName: Full=FMN-dependent NADH-azoreductase;
DE            EC=1.7.1.17;
GN   Name=azoR;
XX
CC   -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC       stress caused by electrophilic quinones.
CC   -!- FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive
CC       cleavage of the azo bond in aromatic azo compounds to the corresponding
CC       amines.
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   -!- 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;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the azoreductase type 1 family.
XX
DR   Pfam; PF02525; Flavodoxin_2; 1; trigger=no
DR   PRINTS; PR00453; VWFADOMAIN; 1; trigger=no
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KW   FMN
KW   Flavoprotein
KW   NAD
KW   Oxidoreductase
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GO   GO:0009055; F:electron transfer activity
GO   GO:0010181; F:FMN binding
GO   GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor
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FT   From: AZOR1_PSEAE (Q9I5F3)
FT   BINDING         16..18
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: S-x-S
FT   BINDING         97..100
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: M-[YW]-N-[FL]
FT   BINDING         145..148
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [ST]-x-G-G
FT   BINDING         10
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: S
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Size: 186-240;
Related: None;
Template: P41407; Q9I5F3; Q9I2E2; Q9HZ17; Q831B2;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in TRIV2, BACAN, BACC1, BACCR, BACCZ, HALH5, BACHK, BACLD, BACSU,
 BURL3, CLOAB, CLOPE, COLP3, HAHCH, IDILO, JANSC, LACLA, LISIN, LISMF, LISMO,
 MESFL, PHOPR, PSEAE, PSEF5, PSEPF, PSEPK, PSEPM, CUPPJ, RHIEC, XANAC, XANC5
Plasmid: in TRIV2, RALN1, RHIEC
Comments: Divergent STRCO and first copy in CLOAB and CLOPE; sequences not included
 in alignment and not taken into account in size range.
 In some species there are many duplicates.
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# Revision 1.42 2023/11/28
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