ID   AZOB_XENAZ              Reviewed;         286 AA.
AC   Q8KU07;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-MAY-2023, entry version 57.
DE   RecName: Full=NAD(P)H azoreductase;
DE            EC=1.7.-.-;
GN   Name=azoB;
OS   Xenophilus azovorans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Xenophilus.
OX   NCBI_TaxID=151755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11; 54-78; 123-136
RP   AND 240-264, SUBUNIT, AND CHARACTERIZATION.
RC   STRAIN=KF46F / DSM 13620;
RX   PubMed=12147495; DOI=10.1128/aem.68.8.3948-3955.2002;
RA   Bluemel S., Knackmuss H.-J., Stolz A.;
RT   "Molecular cloning and characterization of the gene coding for the aerobic
RT   azoreductase from Xenophilus azovorans KF46F.";
RL   Appl. Environ. Microbiol. 68:3948-3955(2002).
CC   -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic azo
CC       compounds to the corresponding amines. Uses preferentially NADPH rather
CC       than NADH as an electron donor for its activity. The enzyme reductively
CC       cleaved Orange II and carboxy-Orange II, and can also reduce several
CC       sulfonated structural analogs, which carry a hydroxy group in the 2
CC       position of the naphthol ring.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 uM for NADPH;
CC         KM=180 uM for NADH;
CC       pH dependence:
CC         Optimum pH is 6.2-6.8.;
CC       Temperature dependence:
CC         Optimum temperature is 41 degrees Celsius.;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12147495}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC       Azoreductase type 3 subfamily. {ECO:0000305}.
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DR   EMBL; AF466104; AAM92125.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KU07; -.
DR   SMR; Q8KU07; -.
DR   BRENDA; 1.7.1.6; 7792.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05269; TMR_SDR_a; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   PANTHER; PTHR43162; -; 1.
DR   PANTHER; PTHR43162:SF1; PRESTALK A DIFFERENTIATION PROTEIN A; 1.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..286
FT                   /note="NAD(P)H azoreductase"
FT                   /id="PRO_0000234087"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P39315"
FT   BINDING         31
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P39315"
FT   BINDING         136..141
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P39315"
SQ   SEQUENCE   286 AA;  30082 MW;  8B231C5E3739F818 CRC64;
     MILVVGGTGT IGSEVVRLLQ EAKLPFKALV RDAAKARELN ARGVQTAAGD LREPRTLPAA
     LGGVDKVFVV TPLVPDQVQM RAALITAAKT AGVKHFVMST GIGAAPDSPV QIGRWLGENQ
     QQVQESGMAW TFVQPGFFMQ NLLMYAQAIR EKGEFYMPLG EGKVSWIDAR DIAAVAVQAL
     TKPGHENQAY PVTGPQALSG AEVAAALSAA AGRPVRYVAI TLEQAKQAMT GMGMPESLAD
     AMNELYALAP PDYLAGVLDT VPKVTGRPAR TFAEFAKAHA AAFGAA
//