Biomaterial Database

Cloning and nucleotide sequence of the gene for NADH:FMN oxidoreductase from Vibrio harveyi. 1994

Y Izumoto, and T Mori, and K Yamamoto

Bio-technology Research Laboratory, Sekisui Chemical Co., Ltd., Osaka, Japan.

The gene encoding the enzyme NADH:FMN oxidoreductase (EC 1.6.99.3) from Vibrio harveyi has been isolated from a recombinant library of genomic DNA and sequenced. The deduced amino acid sequence, 237 amino acids long, shows 48% identity with E. coli NAD(P)H:flavin oxidoreductase and 40% identity with Vibrio harveyi luxG gene product.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009247	NADH, NADPH Oxidoreductases	A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.	Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D003001	Cloning, Molecular	The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.	Molecular Cloning
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596	Amino Acids	Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.	Amino Acid,Acid, Amino,Acids, Amino
D001483	Base Sequence	The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.	DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D014733	Vibrio	A genus of VIBRIONACEAE, made up of short, slightly curved, motile, gram-negative rods. Various species produce cholera and other gastrointestinal disorders as well as abortion in sheep and cattle.	Beneckea
D038181	FMN Reductase	An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29.	Flavin Mononucleotide Reductase,NAD(P)H-Flavin Oxidoreductase,FMN Oxidoreductase,NAD(P)H Dehydrogenase (FMN),NAD(P)H-FMN Oxidoreductase,NADH-FMN Oxidoreductase,NADH-Flavin Oxidoreductase,NADPH-Flavin Reductase,Mononucleotide Reductase, Flavin,NADH FMN Oxidoreductase,NADPH Flavin Reductase,Oxidoreductase, FMN,Oxidoreductase, NADH-FMN,Oxidoreductase, NADH-Flavin,Reductase, FMN,Reductase, Flavin Mononucleotide,Reductase, NADPH-Flavin