EC number:1.5.1.38

Enzyme

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     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.1 With NAD+ or NADP+ as acceptor
ID:1.5.1.38
Description:FMN reductase (NADPH).
Alternative Name: Flavin reductase P.
Cath: 3.20.20.30; 3.40.109.10; 3.40.50.360;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.1.38
BRENDA Enzyme Link: BRENDA 1.5.1.38
KEGG Enzyme Link: KEGG1.5.1.38
BioCyc Enzyme Link: BioCyc 1.5.1.38
ExPASy Enzyme Link: ExPASy1.5.1.38
EC2PDB Enzyme Link: EC2PDB 1.5.1.38
ExplorEnz Enzyme Link: ExplorEnz 1.5.1.38
PRIAM enzyme-specific profiles Link: PRIAM 1.5.1.38
IntEnz Enzyme Link: IntEnz 1.5.1.38
MEDLINE Enzyme Link: MEDLINE 1.5.1.38

EC number:1.5.1.38

MSA:

1.5.1.38;
Phylogenetic Tree:

1.5.1.38;
Uniprot:
M-CSA:
RHEA:21624 FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]:[nH;+0:10]:[c;H0;+0:11]1:[c;H0;+0:12](:[*:13])-[NH;+0:14]-[*:15]:[*:16]-[N;H0;+0:17]-1-[*:18]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]:[n;H0;+0:10]:[c;H0;+0:11]1:[n;H0;+0:17](-[*:18]):[*:16]:[*:15]:[n;H0;+0:14]:[c;H0;+0:12]-1:[*:13]
Reaction
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References

TitleAuthorsDatePubMed ID
Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase.Zenno S, Kobori T, Tanokura M, Saigo K1998 Oct9836433
Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase.Lei B, Tu SC1998 Oct 139772191
Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium.Liu M, Lei B, Ding Q, Lee JC, Tu SC1997 Jan 18990272
Flavin reductase P: structure of a dimeric enzyme that reduces flavin.Tanner JJ, Lei B, Tu SC, Krause KL1996 Oct 228885832
Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi.Jablonski E, DeLuca M1977 Jun 28880288
Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme.Lei B, Liu M, Huang S, Tu SC1994 Jun8206832
Specificities and properties of three reduced pyridine nucleotide-flavin mononucleotide reductases coupling to bacterial luciferase.Watanabe H, Hastings JW1982 May 146981058
Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases.Jablonski E, DeLuca M1978 Feb 2123827
Structure and function of YcnD from Bacillus subtilis, a flavin-containing oxidoreductase.Morokutti A, Lyskowski A, Sollner S, Pointner E, Fitzpatrick TB, Kratky C, Gruber K, Macheroux P2005 Oct 2516229462
Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi.Gerlo E, Charlier J1975 Sep 151175652
Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli.Eichhorn E, van der Ploeg JR, Leisinger T1999 Sep 1710480865