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AZOR8_BURL3
ID   AZOR8_BURL3             Reviewed;         210 AA.
AC   Q39M29;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=FMN-dependent NADH:quinone oxidoreductase 8 {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=Azo-dye reductase 8 {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase 8 {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azoreductase 8 {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
GN   Name=azoR8 {ECO:0000255|HAMAP-Rule:MF_01216};
GN   OrderedLocusNames=Bcep18194_C7443;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000150; ABB06487.1; -; Genomic_DNA.
DR   RefSeq; WP_011350130.1; NC_007509.1.
DR   AlphaFoldDB; Q39M29; -.
DR   SMR; Q39M29; -.
DR   EnsemblBacteria; ABB06487; ABB06487; Bcep18194_C7443.
DR   GeneID; 45092811; -.
DR   KEGG; bur:Bcep18194_C7443; -.
DR   PATRIC; fig|482957.22.peg.8040; -.
DR   HOGENOM; CLU_088964_0_0_4; -.
DR   OMA; AGITFKY; -.
DR   OrthoDB; 1402654at2; -.
DR   Proteomes; UP000002705; Chromosome 3.
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..210
FT                   /note="FMN-dependent NADH:quinone oxidoreductase 8"
FT                   /id="PRO_0000245908"
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   210 AA;  22942 MW;  380E844A258EBF49 CRC64;
     MPTLLVVEAS PRGEQSISRG LTKMFVNQWK REQHDGRVIQ RDLMATDLPF VTMPWLGAYF
     TPPEHQTQDM KNLLRLSDEL VAEILSADHI VIGTPVYNYN VPAVLKAYID HIVRKGKTLG
     FSGEGLVKGK ACTIVMASGG AYTPDSPIRD RDIATGYLRL ILKVIGIEDV TVIAGGNAKA
     VDMGEISRSD FLEAFASDMA DAAARPVVQV
 
 
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