ID   AZOR1_TRIV2             Reviewed;         207 AA.
AC   Q3M1N6;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=FMN-dependent NADH:quinone oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=Azo-dye reductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azoreductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
GN   Name=azoR1 {ECO:0000255|HAMAP-Rule:MF_01216}; OrderedLocusNames=Ava_C0025;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OG   Plasmid pAnaC.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
CC   -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC       stress caused by electrophilic quinones. {ECO:0000255|HAMAP-
CC       Rule:MF_01216}.
CC   -!- FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive
CC       cleavage of the azo bond in aromatic azo compounds to the corresponding
CC       amines. {ECO:0000255|HAMAP-Rule:MF_01216}.
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   -!- 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};
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   -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01216}.
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DR   EMBL; CP000121; ABA25114.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M1N6; -.
DR   SMR; Q3M1N6; -.
DR   STRING; 240292.Ava_C0025; -.
DR   EnsemblBacteria; ABA25114; ABA25114; Ava_C0025.
DR   KEGG; ava:Ava_C0025; -.
DR   eggNOG; COG1182; Bacteria.
DR   HOGENOM; CLU_088964_0_0_3; -.
DR   OMA; HASGWLR; -.
DR   Proteomes; UP000002533; Plasmid pAnaC.
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; IEA:InterPro.
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   3: Inferred from homology;
KW   Flavoprotein; FMN; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..207
FT                   /note="FMN-dependent NADH:quinone oxidoreductase 1"
FT                   /id="PRO_0000245870"
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         139..142
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
SQ   SEQUENCE   207 AA;  23123 MW;  D1F0B4A9AF7A6432 CRC64;
     MKLLHLDSSP RGERSISRSL TQQFVSLWKQ MHLDVPVIYR DLGRYPVPAI DEAWIAAAFC
     PPAQLTPELQ SALMISDELI AELLAANLYI FGIPMYNYSV PASFKAYIDQ IVRVRRTFVV
     SADGYEGLLK DKKVLVITTR GGSYAGEPLD FQEPYLRAVF GFIGITDVTF IHAENLAIGS
     EERQLAIATA HEAIQQVVKT WQSSTCI