FMN-dependent NADH-azoreductase

Details

Name
FMN-dependent NADH-azoreductase
Synonyms
  • 1.7.-.-
  • acpD
  • Azo-dye reductase
  • FMN-dependent NADH-azo compound oxidoreductase
Gene Name
azoR
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016834|FMN-dependent NADH-azoreductase
MSKVLVLKSSILAGYSQSNQLSDYFVEQWREKHSADEITVRDLAANPIPVLDGELVGALR
PSDAPLTPRQQEALALSDELIAELKAHDVIVIAAPMYNFNISTQLKNYFDLVARAGVTFR
YTENGPEGLVTGKKAIVITSRGGIHKDGPTDLVTPYLSTFLGFIGITDVKFVFAEGIAYG
PEMAAKAQSDAKAAIDSIVSA
Number of residues
201
Molecular Weight
21657.47
Theoretical pI
4.84
GO Classification
Functions
azobenzene reductase activity / electron carrier activity / FMN binding / FMN reductase activity / oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
Processes
response to oxidative stress
Components
cytosol
General Function
Oxidoreductase activity, acting on nad(p)h, quinone or similar compound as acceptor
Specific Function
Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016835|FMN-dependent NADH-azoreductase (azoR)
ATGAGCAAGGTATTAGTTCTTAAATCCAGCATCCTGGCAGGGTACTCTCAGTCTAATCAG
TTGTCCGATTATTTTGTTGAACAATGGCGCGAAAAGCACTCCGCTGATGAAATCACCGTT
CGCGACCTGGCTGCAAATCCGATTCCGGTACTGGATGGCGAACTGGTTGGCGCTCTGCGT
CCGAGCGATGCGCCGCTGACTCCGCGTCAGCAGGAAGCTCTGGCACTTTCCGATGAGTTG
ATTGCCGAGCTGAAAGCCCACGACGTTATCGTTATTGCGGCACCGATGTATAACTTCAAC
ATCTCGACTCAGTTGAAAAACTATTTTGACCTGGTTGCCCGCGCAGGCGTTACTTTCCGC
TATACCGAGAACGGTCCGGAAGGTCTGGTAACGGGTAAAAAAGCCATCGTTATTACCAGC
CGCGGCGGGATCCACAAAGATGGACCAACGGACCTGGTGACGCCGTATCTGTCCACGTTC
CTCGGCTTTATCGGCATTACCGATGTGAAATTTGTCTTCGCCGAAGGGATCGCATACGGT
CCGGAAATGGCAGCGAAAGCACAGTCTGACGCAAAAGCAGCCATCGACAGCATTGTTTCT
GCATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP41407
UniProtKB Entry NameAZOR_ECOLI
GenBank Gene IDD85081
General References
  1. Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Moriya H, Kasai H, Isono K: Cloning and characterization of the hrpA gene in the terC region of Escherichia coli that is highly similar to the DEAH family RNA helicase genes of Saccharomyces cerevisiae. Nucleic Acids Res. 1995 Feb 25;23(4):595-8. [Article]
  5. Fischl AS, Kennedy EP: Isolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli. J Bacteriol. 1990 Sep;172(9):5445-9. [Article]
  6. Nakanishi M, Yatome C, Ishida N, Kitade Y: Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J Biol Chem. 2001 Dec 7;276(49):46394-9. Epub 2001 Oct 2. [Article]
  7. Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M: Crystallization and preliminary X-ray analysis of AzoR (azoreductase) from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt 4):399-402. Epub 2005 Mar 24. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03247Flavin mononucleotideapproved, investigationalunknownDetails
DB04392Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone]experimentalunknownDetails