ID   AZRB_BACOY              Reviewed;         178 AA.
AC   Q9FAW5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=NADPH azoreductase;
DE            EC=1.7.1.6;
GN   Name=azr;
OS   Bacillus sp. (strain OY1-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=104667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-31, AND
RP   CHARACTERIZATION.
RX   PubMed=11134015; DOI=10.1074/jbc.m008083200;
RA   Suzuki Y., Yoda T., Ruhul A., Sugiura W.;
RT   "Molecular cloning and characterization of the gene coding for azoreductase
RT   from Bacillus sp. OY1-2 isolated from soil.";
RL   J. Biol. Chem. 276:9059-9065(2001).
CC   -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic azo
CC       compounds to the corresponding amines. Requires NADPH as an electron
CC       donor for its activity. Compounds with paired naphthalene groups
CC       coupled with the azo group are good substrates, with the following
CC       preference order: Rocceline > Sumifix Black B > Solar Orange.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aniline + N,N-dimethyl-1,4-phenylenediamine + 2 NADP(+) = 4-
CC         (dimethylamino)azobenzene + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:16269,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15783, ChEBI:CHEBI:17296,
CC         ChEBI:CHEBI:17903, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.7.1.6;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
CC   -!- INDUCTION: Constitutively expressed.
CC   -!- SIMILARITY: Belongs to the azoreductase type 2 family. {ECO:0000305}.
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; AB032601; BAB13746.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9FAW5; -.
DR   SMR; Q9FAW5; -.
DR   DrugBank; DB01014; Balsalazide.
DR   KEGG; ag:BAB13746; -.
DR   BRENDA; 1.7.1.6; 691.
DR   SABIO-RK; Q9FAW5; -.
DR   GO; GO:0050446; F:azobenzene reductase activity; IEA:UniProtKB-EC.
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; NADP; Oxidoreductase.
FT   CHAIN           1..178
FT                   /note="NADPH azoreductase"
FT                   /id="PRO_0000234085"
FT   BINDING         106..111
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   178 AA;  19293 MW;  ADAF53CF849ABC59 CRC64;
     MKLVVINGTP RKFGRTRVVA KYIADQFEGE LYDLAIEELP LYNGEESQRD LEAVKKLKTL
     VKAADGVVLC TPEYHNAMSG ALKNSLDYLS SSEFIHKPVA LLAVAGGGKG GINALNSMHA
     SLAGVYANAI PKQVVLDGLH VQDGELGEDA KPLIHDVVKE LKAYMSVYKE VKKQLGVE