Oxygen-insensitive NADPH nitroreductase

NameOxygen-insensitive NADPH nitroreductase
Synonyms
  • 1.-.-.-
  • mda18
  • mdaA
  • Modulator of drug activity A
  • ybjB
Gene NamenfsA
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0001238|Oxygen-insensitive NADPH nitroreductase
MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREEL
VTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAE
SLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENS
YQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR
Number of residuesNone
Molecular Weight26800.375
Theoretical pI6.94
GO Classification
Functions
  • FMN binding
  • chromate reductase activity
  • oxidoreductase activity, acting on NAD(P)H, nitrogenous group as acceptor
Processes
Components
  • cytosol
General FunctionOxidoreductase activity, acting on nad(p)h, nitrogenous group as acceptor
Specific FunctionReduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major component of the oxygen-insensitive nitroreductase activity in E.coli.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP17117
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0016154|Oxygen-insensitive NADPH nitroreductase (nfsA)
ATGACGCCAACCATTGAACTTATTTGTGGCCATCGCTCCATTCGCCATTTCACTGATGAA
CCCATTTCCGAAGCGCAGCGTGAGGCGATTATTAACAGCGCCCGTGCGACGTCCAGTTCC
AGTTTTTTGCAGTGCAGTAGCATTATTCGCATTACCGACAAAGCGTTACGTGAAGAACTG
GTGACGCTGACCGGCGGGCAAAAACACGTAGCGCAAGCGGCGGAGTTCTGGGTGTTCTGT
GCCGACTTTAACCGCCATTTACAGATCTGTCCGGATGCTCAGCTCGGCCTGGCGGAACAA
CTGTTGCTCGGTGTCGTTGATACGGCAATGATGGCGCAGAATGCATTAATCGCAGCGGAA
TCGCTGGGATTGGGCGGGGTATATATCGGCGGCCTGCGCAATAATATTGAAGCGGTGACG
AAACTGCTTAAATTACCGCAGCATGTTCTGCCGCTGTTTGGGCTGTGCCTTGGCTGGCCT
GCGGATAATCCGGATCTTAAGCCGCGTTTACCGGCCTCCATTTTGGTGCATGAAAACAGC
TATCAACCGCTGGATAAAGGCGCACTGGCGCAGTATGACGAGCAACTGGCGGAATATTAC
CTCACCCGTGGCAGCAATAATCGCCGGGATACCTGGAGCGATCATATCCGCCGAACAATC
ATTAAAGAAAGCCGCCCATTTATTCTGGATTATTTGCACAAACAGGGTTGGGCGACGCGC
TAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Chatterjee PK, Sternberg NL: A general genetic approach in Escherichia coli for determining the mechanism(s) of action of tumoricidal agents: application to DMP 840, a tumoricidal agent. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8950-4. [7568050 ]
  2. Zenno S, Koike H, Kumar AN, Jayaraman R, Tanokura M, Saigo K: Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. J Bacteriol. 1996 Aug;178(15):4508-14. [8755878 ]
  3. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [8905232 ]
  4. 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. [9278503 ]
  5. 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. [16738553 ]
  6. Kang WK, Icho T, Isono S, Kitakawa M, Isono K: Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12. Mol Gen Genet. 1989 Jun;217(2-3):281-8. [2570347 ]
  7. Zenno S, Kobori T, Tanokura M, Saigo K: Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution. J Bacteriol. 1998 Jan;180(2):422-5. [9440535 ]
  8. Kobori T, Sasaki H, Lee WC, Zenno S, Saigo K, Murphy ME, Tanokura M: Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution. J Biol Chem. 2001 Jan 26;276(4):2816-23. Epub 2000 Oct 16. [11034992 ]

From www.t3db.ca