ID   AZO1_STAAU              Reviewed;         188 AA.
AC   Q50H63;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=FMN-dependent NADPH-azoreductase;
DE            EC=1.7.1.17;
DE   AltName: Full=NADPH-dependent flavo-azoreductase;
DE   AltName: Full=NADPH-flavin azoreductase;
GN   Name=azo1;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND CHARACTERIZATION.
RC   STRAIN=ATCC 25923 / DSM 1104 / JCM 2413 / NBRC 14462 / NCIMB 12702 / NCTC
RC   12981 / Seattle 1945;
RX   PubMed=15870453; DOI=10.1099/mic.0.27805-0;
RA   Chen H., Hopper S.L., Cerniglia C.E., Wang R.-F.;
RT   "Biochemical and molecular characterization of an azoreductase from
RT   Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein.";
RL   Microbiology 151:1433-1441(2005).
CC   -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic azo
CC       compounds to the corresponding amines. Requires NADPH, but not NADH, as
CC       an electron donor for its activity. The enzyme can also reduce a wide
CC       range of sulfonated azo dyes. The substrate preference order is methyl
CC       red > Ponceau BS, Ponceau S > Orange II > Amaranth.
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;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:15870453};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=57.0 uM for methyl red {ECO:0000269|PubMed:15870453};
CC         KM=74.0 uM for NADPH {ECO:0000269|PubMed:15870453};
CC         Vmax=0.41 umol/min/mg enzyme toward methyl red
CC         {ECO:0000269|PubMed:15870453};
CC         Vmax=0.39 umol/min/mg enzyme toward NADPH
CC         {ECO:0000269|PubMed:15870453};
CC       pH dependence:
CC         Optimum pH is 6.0-6.6. {ECO:0000269|PubMed:15870453};
CC       Temperature dependence:
CC         Optimum temperature is 35-40 degrees Celsius. Inactive above 60
CC         degrees Celsius. Thermostable up to 55 degrees Celsius.
CC         {ECO:0000269|PubMed:15870453};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15870453}.
CC   -!- INDUCTION: Constitutively expressed.
CC   -!- SIMILARITY: Belongs to the azoreductase type 2 family. {ECO:0000305}.
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DR   EMBL; AY545994; AAT29034.1; -; Genomic_DNA.
DR   RefSeq; WP_000677261.1; NZ_WYDB01000005.1.
DR   AlphaFoldDB; Q50H63; -.
DR   SMR; Q50H63; -.
DR   OMA; PEYHSGM; -.
DR   BRENDA; 1.7.1.6; 3352.
DR   SABIO-RK; Q50H63; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; NADP; Oxidoreductase.
FT   CHAIN           1..188
FT                   /note="FMN-dependent NADPH-azoreductase"
FT                   /id="PRO_0000234086"
SQ   SEQUENCE   188 AA;  20912 MW;  D7CA1764A344D641 CRC64;
     MKGLIIIGSA QVNSHTSALA RYLTEHFKTH DIEAEIFDLA EKPLNQLDFS GTTPSIDEIK
     QNMKDLKEKA MAADFLILGT PNYHGSYSGI LKNALDHLNM DYFKMKPVGL IGNSGGIVSS
     EPLSHLRVIV RSLLGIAVPT QIATHDSDFA KNEDGSYYLN DSEFQLRARL FVDQIVSFVN
     NSPYEHLK