ID A0A7U9BGT1_ECOLX Unreviewed; 201 AA. AC A0A7U9BGT1; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. 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=ECLG_02576 {ECO:0000313|EMBL:EGI37262.1}; OS Escherichia coli TA271. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656443 {ECO:0000313|EMBL:EGI37262.1, ECO:0000313|Proteomes:UP000004645}; RN [1] {ECO:0000313|EMBL:EGI37262.1, ECO:0000313|Proteomes:UP000004645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TA271 {ECO:0000313|EMBL:EGI37262.1, RC ECO:0000313|Proteomes:UP000004645}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA271."; RL Submitted (JAN-2010) 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 --------------------------------------------------------------------------- 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; GL884266; EGI37262.1; -; Genomic_DNA. DR SMR; A0A7U9BGT1; -. DR Proteomes; UP000004645; Unassembled WGS sequence. 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 {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 3..195 FT /note="Flavodoxin_2" FT /evidence="ECO:0000259|Pfam:PF02525" FT NP_BIND 16..18 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216" FT NP_BIND 96..99 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216" FT NP_BIND 140..143 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216" FT BINDING 10 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216" SQ SEQUENCE 201 AA; 21642 MW; E29550DC4DA42297 CRC64; MSKVLVLKSS ILAGYSQSNQ LSDYFVEQWR EKHSADEITV RDLAANPIPV LDGELVGALR PSDAPLTPRQ QEALALSDEL IAELKAHDVI VIAAPMYNFN ISTQLKNYFD LVARAGVTFR YTENGPEGLV TGKKAIVITS RGGIHKDGPT DLVTPYLSTF LGFIGITDVK FVFAEGIAYG PEMAAKAQSD AKAAIDSIVA A //