Major NAD(P)H-flavin oxidoreductase

Details

Name
Major NAD(P)H-flavin oxidoreductase
Synonyms
  • 1.6.99.-
  • FRASE I
Gene Name
Not Available
Organism
Aliivibrio fischeri
Amino acid sequence
>lcl|BSEQ0010853|Major NAD(P)H-flavin oxidoreductase
MTHPIIHDLENRYTSKKYDPSKKVSQEDLAVLLEALRLSASSINSQPWKFIVIESDAAKQ
RMHDSFANMHQFNQPHIKACSHVILFANKLSYTRDDYDVVLSKAVADKRITEEQKEAAFA
SFKFVELNCDENGEHKAWTKPQAYLALGNALHTLARLNIDSTTMEGIDPELLSEIFADEL
KGYECHVALAIGYHHPSEDYNASLPKSRKAFEDVITIL
Number of residues
218
Molecular Weight
24720.685
Theoretical pI
6.12
GO Classification
Functions
oxidoreductase activity
Processes
bioluminescence
General Function
Oxidoreductase activity
Specific Function
Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Major FMN reductase. It is capable of using both NADH and NADPH as electron donors. As electron acceptor, FMN is the most effective, FAD is considerably effective, and riboflavin is the least effective.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0002440|657 bp
ATGACGCATCCAATTATTCATGATCTTGAAAATCGTTATACATCAAAAAAATATGACCCA
TCAAAGAAAGTATCTCAAGAAGATTTAGCGGTTTTGCTTGAGGCTCTGCGTTTATCTGCT
TCTTCAATTAATTCACAGCCTTGGAAATTCATTGTTATTGAATCCGATGCAGCGAAGCAA
CGTATGCATGATTCGTTTGCAAATATGCATCAGTTTAATCAACCTCACATCAAAGCGTGT
TCTCATGTGATTTTATTTGCAAATAAGCTTTCGTATACACGAGATGATTATGATGTGGTT
TTATCTAAAGCGGTTGCTGACAAGCGTATTACTGAAGAGCAAAAAGAAGCTGCTTTTGCT
TCGTTTAAGTTTGTAGAATTGAACTGTGATGAAAATGGTGAGCATAAAGCATGGACTAAG
CCTCAAGCTTATTTAGCTCTTGGTAATGCTCTGCATACATTAGCTAGACTGAACATTGAC
TCAACAACAATGGAAGGCATTGATCCTGAATTATTGAGTGAAATTTTTGCTGATGAATTA
AAAGGGTATGAATGTCATGTTGCTTTAGCCATTGGTTATCATCATCCAAGCGAAGATTAT
AATGCCTCTTTGCCTAAGTCTCGTAAGGCATTTGAAGACGTAATTACCATCCTTTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP46072
UniProtKB Entry NameFRA1_ALIFS
GenBank Protein ID6539550
GenBank Gene IDD17743
General References
  1. Zenno S, Saigo K, Kanoh H, Inouye S: Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744. J Bacteriol. 1994 Jun;176(12):3536-43. [Article]
  2. Inouye S: NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein. FEBS Lett. 1994 Jun 27;347(2-3):163-8. [Article]
  3. Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M: 1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins. J Mol Biol. 1998 Jul 10;280(2):259-73. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01650trans-2-hydroxycinnamic acidexperimentalunknownDetails
DB03247Flavin mononucleotideapproved, investigationalunknownDetails
DB034104-hydroxycoumarinexperimentalunknownDetails