ID   AZOR_MYCMO              Reviewed;         202 AA.
AC   Q6KHU1;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=MMOB3510;
OS   Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS   mobile).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=267748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX   PubMed=15289470; DOI=10.1101/gr.2674004;
RA   Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA   Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA   Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA   Church G.M.;
RT   "The complete genome and proteome of Mycoplasma mobile.";
RL   Genome Res. 14:1447-1461(2004).
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; AE017308; AAT27837.1; -; Genomic_DNA.
DR   RefSeq; WP_011264871.1; NC_006908.1.
DR   AlphaFoldDB; Q6KHU1; -.
DR   SMR; Q6KHU1; -.
DR   STRING; 267748.MMOB3510; -.
DR   EnsemblBacteria; AAT27837; AAT27837; MMOB3510.
DR   KEGG; mmo:MMOB3510; -.
DR   eggNOG; COG1182; Bacteria.
DR   HOGENOM; CLU_088964_2_0_14; -.
DR   OMA; PLGWYPF; -.
DR   OrthoDB; 1402654at2; -.
DR   Proteomes; UP000009072; 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..202
FT                   /note="FMN-dependent NADH:quinone oxidoreductase"
FT                   /id="PRO_0000245936"
FT   BINDING         12
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT   BINDING         21..23
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
SQ   SEQUENCE   202 AA;  22744 MW;  8666D6FF73650BAC CRC64;
     MKIQKVLVIK SSMTENLPSG SFSSALSDKF MEYYRKENPI DKIIELNLND QKDLISLSSQ
     NFNTFFTDGV SDKYIDQLKS VDKVVISSPM TNFNYTALLK NYLDRILVAN KTFSYKYSKK
     GEAIGLLPHL KVQILTTQGA PLGWYTWGDH TKNLEGTFEF IGAKVAKSVV MDGLKTPQYS
     SLKAPEALDL FDKVIKTAAE NF