Anaerobic nitric oxide reductase flavorubredoxin (Q46877)

Identification
Name:Anaerobic nitric oxide reductase flavorubredoxin
Synonyms:
  • FlRd
  • FlavoRb
Gene Name:norV
Enzyme Class:Not Available
Biological Properties
General Function:Involved in iron ion binding
Specific Function:Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0Thumb+1.0Thumb+2.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0NADH + 2.0Nitric oxide → 1.0Water + 1.0Nitrous oxide + 1.0NAD
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB03378Nitric oxideMetaboCard
ECMDB21255Nitrous oxideMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
electron carrier activity
FMN binding
hydrolase activity
ion binding
metal ion binding
nucleotide binding
oxidoreductase activity
Gene Properties
Blattner:b2710
Gene OrientationClockwise
Centisome Percentage:61.01
Left Sequence End2830498
Right Sequence End2831937
Gene Sequence:
>1440 bp
ATGTCAGTACCCGTTCAACATCCTATGTATATCGATGGACAGTTTGTTACCTGGCGTGGA
GACGCATGGATTGATGTGGTAAACCCTGCTACAGAGGCTGTCATTTCCCGCATACCCGAT
GGTCAGGCCGAGGATGCCCGTAAGGCAATCGATGCAGCAGAACGTGCACAACCAGAATGG
GAAGCGTTGCCTGCTATTGAACGCGCCAGTTGGTTGCGCAAAATCTCCGCCGGGATCCGC
GAACGCGCCAGTGAAATCAGTGCGCTGATTGTTGAAGAAGGGGGCAAGATCCAGCAGCTG
GCTGAAGTCGAAGTGGCTTTTACTGCCGACTATATCGATTACATGGCGGAGTGGGCACGG
CGTTACGAGGGCGAGATTATTCAAAGCGATCGTCCAGGAGAAAATATTCTTTTGTTTAAA
CGTGCGCTTGGTGTGACTACCGGCATTCTGCCGTGGAACTTCCCGTTCTTCCTCATTGCC
CGCAAAATGGCTCCCGCTCTTTTGACCGGTAATACCATCGTCATTAAACCTAGTGAATTT
ACGCCAAACAATGCGATTGCATTCGCCAAAATCGTCGATGAAATAGGCCTTCCGCGCGGC
GTGTTTAACCTTGTACTGGGGCGTGGTGAAACCGTTGGGCAAGAACTGGCGGGTAACCCA
AAGGTCGCAATGGTCAGTATGACAGGCAGCGTCTCTGCAGGTGAGAAGATCATGGCGACT
GCGGCGAAAAACATCACCAAAGTGTGTCTGGAATTGGGGGGTAAAGCACCAGCTATCGTA
ATGGACGATGCCGATCTTGAACTGGCAGTCAAAGCCATCGTTGATTCACGCGTCATTAAT
AGTGGGCAAGTGTGTAACTGTGCAGAACGTGTTTATGTACAGAAAGGCATTTATGATCAG
TTCGTCAATCGGCTGGGTGAAGCGATGCAGGCGGTTCAATTTGGTAACCCCGCTGAACGC
AACGACATTGCGATGGGGCCGTTGATTAACGCCGCGGCGCTGGAAAGGGTCGAGCAAAAA
GTGGCGCGCGCAGTAGAAGAAGGGGCGAGAGTGGCGTTCGGTGGCAAAGCGGTAGAGGGG
AAAGGATATTATTATCCGCCGACATTGCTGCTGGATGTTCGCCAGGAAATGTCGATTATG
CATGAGGAAACCTTTGGCCCGGTGCTGCCAGTTGTCGCATTTGACACGCTGGAAGATGCT
ATCTCAATGGCTAATGACAGTGATTACGGCCTGACCTCATCAATCTATACCCAAAATCTG
AACGTCGCGATGAAAGCCATTAAAGGGCTGAAGTTTGGTGAAACTTACATCAACCGTGAA
AACTTCGAAGCTATGCAAGGCTTCCACGCCGGATGGCGTAAATCCGGTATTGGCGGCGCA
GATGGTAAACATGGCTTGCATGAATATCTGCAGACCCAGGTGGTTTATTTACAGTCTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:479
Protein Molecular Weight:54234
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Anaerobic nitric oxide reductase flavorubredoxin
MSIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFV
QNLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWN
FNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLFND
EVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVE
LYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILT
NVFRSKGVLVGTSTMNNVMMPKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRL
QDAGFEMSLSLKAKWRPDQDALKLCREHGREIARQWALAPLPQSTVNTVVKEETSATTTA
DLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFEELASEAK
References
External Links:
ResourceLink
Uniprot ID:Q46877
Uniprot Name:NORV_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742307
Ecogene ID:EG12963
Ecocyc:EG12963
ColiBase:b2710
Kegg Gene:b2710
EchoBASE ID:EB2793
CCDB:NORV_ECOLI
BacMap:16130617
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • da Costa, P. N., Teixeira, M., Saraiva, L. M. (2003). "Regulation of the flavorubredoxin nitric oxide reductase gene in Escherichia coli: nitrate repression, nitrite induction, and possible post-transcription control." FEMS Microbiol Lett 218:385-393. Pubmed: 12586421
  • Gardner, A. M., Gessner, C. R., Gardner, P. R. (2003). "Regulation of the nitric oxide reduction operon (norRVW) in Escherichia coli. Role of NorR and sigma54 in the nitric oxide stress response." J Biol Chem 278:10081-10086. Pubmed: 12529359
  • Gardner, A. M., Helmick, R. A., Gardner, P. R. (2002). "Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli." J Biol Chem 277:8172-8177. Pubmed: 11751865
  • Gomes, C. M., Giuffre, A., Forte, E., Vicente, J. B., Saraiva, L. M., Brunori, M., Teixeira, M. (2002). "A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin." J Biol Chem 277:25273-25276. Pubmed: 12101220
  • Gomes, C. M., Vicente, J. B., Wasserfallen, A., Teixeira, M. (2000). "Spectroscopic studies and characterization of a novel electron-transfer chain from Escherichia coli involving a flavorubredoxin and its flavoprotein reductase partner." Biochemistry 39:16230-16237. Pubmed: 11123953
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Wasserfallen, A., Ragettli, S., Jouanneau, Y., Leisinger, T. (1998). "A family of flavoproteins in the domains Archaea and Bacteria." Eur J Biochem 254:325-332. Pubmed: 9660187