ID J3U2M4_BACTU Unreviewed; 211 AA. AC J3U2M4; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 03-MAY-2023, entry version 44. DE RecName: Full=FMN dependent NADH:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216}; DE EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_01216}; DE AltName: Full=Azo-dye reductase {ECO:0000256|HAMAP-Rule:MF_01216}; DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216}; DE AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000256|HAMAP-Rule:MF_01216}; DE EC=1.7.1.17 {ECO:0000256|HAMAP-Rule:MF_01216}; GN Name=azoR {ECO:0000256|HAMAP-Rule:MF_01216}; GN ORFNames=BTG_08915 {ECO:0000313|EMBL:AFQ15253.1}; OS Bacillus thuringiensis HD-771. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1218175 {ECO:0000313|EMBL:AFQ15253.1, ECO:0000313|Proteomes:UP000005259}; RN [1] {ECO:0000313|EMBL:AFQ15253.1, ECO:0000313|Proteomes:UP000005259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HD-771 {ECO:0000313|EMBL:AFQ15253.1, RC ECO:0000313|Proteomes:UP000005259}; RA Doggett N., Teshima H., Bruce D., Detter J.C., Johnson S.L., Han C.; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01216}. CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific CC stress caused by electrophilic quinones. {ECO:0000256|HAMAP- CC 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00023925}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874; CC Evidence={ECO:0000256|ARBA:ARBA00023925}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01216}; CC Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01216}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01216}. CC -!- SIMILARITY: Belongs to the azoreductase type 1 family. CC {ECO:0000256|HAMAP-Rule:MF_01216}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CP003752; AFQ15253.1; -; Genomic_DNA. DR RefSeq; WP_000170033.1; NC_018500.1. DR AlphaFoldDB; J3U2M4; -. DR EnsemblBacteria; AFQ15253; AFQ15253; BTG_08915. DR KEGG; bti:BTG_08915; -. DR PATRIC; fig|1218175.3.peg.1775; -. DR HOGENOM; CLU_088964_3_1_9; -. DR Proteomes; UP000005259; 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; 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 PANTHER; PTHR43741; FMN-DEPENDENT NADH-AZOREDUCTASE 1; 1. DR PANTHER; PTHR43741:SF7; FMN-DEPENDENT NADH:QUINONE OXIDOREDUCTASE; 1. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. PE 3: Inferred from homology; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_01216}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01216}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01216}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01216}. FT DOMAIN 2..206 FT /note="Flavodoxin-like fold" FT /evidence="ECO:0000259|Pfam:PF02525" FT BINDING 102..105 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216" SQ SEQUENCE 211 AA; 22984 MW; 2367909A8B0E0ACD CRC64; MTKVLFITAN PNSAEGSFGM AVGEAFIEAY KNEHPQDEVV TIDLFNTTVP AIDADVFGAW GKFAAGEGFE TLTEVQQQKV AAMNTNLETF MHADRYVFVT PMWNFSYPPV VKAYLDNVAI AGKTFKYTEN GPVGLLEGKK ALHIQATGGV YSEGAYAAVD FGRNHLKTVL GFVGVNETEY IAVEGMNANP EKAQEIKEAA IANARELAKR F //