AZOR_ERYLH
ID AZOR_ERYLH Reviewed; 197 AA.
AC Q2N970;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=ELI_08395;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC63771.1; -; Genomic_DNA.
DR RefSeq; WP_011414601.1; NC_007722.1.
DR AlphaFoldDB; Q2N970; -.
DR SMR; Q2N970; -.
DR STRING; 314225.ELI_08395; -.
DR EnsemblBacteria; ABC63771; ABC63771; ELI_08395.
DR KEGG; eli:ELI_08395; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_0_0_5; -.
DR OMA; AGITFKY; -.
DR OrthoDB; 1402654at2; -.
DR Proteomes; UP000008808; 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; Reference proteome.
FT CHAIN 1..197
FT /note="FMN-dependent NADH:quinone oxidoreductase"
FT /id="PRO_1000066508"
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"
SQ SEQUENCE 197 AA; 20997 MW; E66A1A9419947762 CRC64;
MSTILHITAS IRGDESISRA LSSKLVERLS GTDTKVITRD LSQNDIPYVD ADRFAANLSP
YTERSPEQQE LAAIADTLIE ELQAADTIVL GVPIYNFSVP ATVKAWADTV ARAGTTFEYT
PTGPKGKLDG KKAYITVASG GTPVGSEVDF MSPWLKFFLG FLGISEVEVV ATADGIMGEG
GEEKIASAHK QVEQVAA
