ID   AZOR_SODGM              Reviewed;         201 AA.
AC   Q2NSV8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=FMN-dependent NADH:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=Azo-dye reductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
GN   Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216}; OrderedLocusNames=SG1492;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE74767.1; -; Genomic_DNA.
DR   RefSeq; WP_011411312.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NSV8; -.
DR   SMR; Q2NSV8; -.
DR   STRING; 343509.SG1492; -.
DR   EnsemblBacteria; BAE74767; BAE74767; SG1492.
DR   KEGG; sgl:SG1492; -.
DR   eggNOG; COG1182; Bacteria.
DR   HOGENOM; CLU_088964_0_0_6; -.
DR   OMA; AGITFKY; -.
DR   OrthoDB; 1402654at2; -.
DR   Proteomes; UP000001932; 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   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; NAD; Oxidoreductase.
FT   CHAIN           1..201
FT                   /note="FMN-dependent NADH:quinone oxidoreductase"
FT                   /id="PRO_0000245974"
FT   BINDING         10
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT   BINDING         16..18
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT   BINDING         96..99
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
SQ   SEQUENCE   201 AA;  22228 MW;  446C45335865D35B CRC64;
     MSKVLVVKSS ILATFSQSNP LADHFIDQWR EQHLNDDITV RDLGAQPVPE LDGELVGALR
     PSDATLTQRQ QQALELSDAL IGELQANDVL VFTAPMYNFA IPSKLKNYFD LIARASVTFR
     YSEQGPERLV KNKRALILTT RDGIHKDTSS DLVTHYLRLF LGFIGITDVS FIYAEGVAYG
     PEAAVKAQEE AKASIQSFVS A