AZOR_XANP2
ID AZOR_XANP2 Reviewed; 208 AA.
AC A7IDY1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Xaut_0973;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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}.
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; CP000781; ABS66224.1; -; Genomic_DNA.
DR RefSeq; WP_012112993.1; NC_009720.1.
DR AlphaFoldDB; A7IDY1; -.
DR SMR; A7IDY1; -.
DR STRING; 78245.Xaut_0973; -.
DR PRIDE; A7IDY1; -.
DR EnsemblBacteria; ABS66224; ABS66224; Xaut_0973.
DR KEGG; xau:Xaut_0973; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_0_3_5; -.
DR OMA; AGITFKY; -.
DR PhylomeDB; A7IDY1; -.
DR Proteomes; UP000002417; 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..208
FT /note="FMN-dependent NADH:quinone oxidoreductase"
FT /id="PRO_1000138989"
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 208 AA; 21930 MW; 9F7EF13FCC79F067 CRC64;
MKTLLRIDSS ARIEGSRSRR LGDALEARWR AGSPDGAVVR RDLAADPVPH IEATTIAGFF
TPADQVTDAM RAATVLSDRL IGEVEAADAL LITAPMYNFG LPSTLKAWID HVVRIHRTVA
YDGTTFRGLV TGKAAYVALA YGAGSYEPGG TLAPFDYAKP YLTHVLGFIG FRDIEVVGVE
GTSGEEGAAA AALDAALKAI ENLPSLAA
