Abstract
The sequence of nitrate reductase (EC 1.6.6.1) mRNA from the plant Arabidopsis thaliana has been determined. A 3.0-kilobase-long cDNA was isolated from a lambda gt10 cDNA library of Arabidopsis leaf poly(A)+ RNA. The cDNA hybridized to a 3.2-kilobase mRNA whose level increased 15-fold in response to treatment of the plant with nitrate. An open reading frame encoding a 917 amino acid protein was found in the sequence. This protein is very similar to tobacco nitrate reductase, being greater than 80% identical within a section of 450 amino acids. By comparing the Arabidopsis protein sequence with other protein sequences, three functional domains were deduced: (i) a molybdenum-pterin-binding domain that is similar to the molybdenum-pterin-binding domain of rat liver sulfite oxidase, (ii) a heme-binding domain that is similar to proteins in the cytochrome b5 superfamily, and (iii) an FAD-binding domain that is similar to NADH-cytochrome b5 reductase.
Publication types
-
Comparative Study
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Base Sequence
-
Binding Sites
-
Cytochrome Reductases
-
Cytochrome b Group
-
Cytochrome-B(5) Reductase
-
Cytochromes b5
-
DNA / genetics
-
DNA / isolation & purification
-
Flavin-Adenine Dinucleotide / metabolism
-
Heme / metabolism
-
Molecular Sequence Data
-
Molybdenum / metabolism
-
Nitrate Reductase
-
Nitrate Reductases / genetics*
-
Nitrates / pharmacology*
-
Nucleic Acid Hybridization
-
Oxidoreductases Acting on Sulfur Group Donors
-
Plants / enzymology*
-
Plants / genetics
-
Pterins / metabolism
-
RNA, Messenger / biosynthesis
-
RNA, Messenger / genetics*
Substances
-
Cytochrome b Group
-
Nitrates
-
Pterins
-
RNA, Messenger
-
Flavin-Adenine Dinucleotide
-
Heme
-
Molybdenum
-
DNA
-
Cytochromes b5
-
Cytochrome Reductases
-
Cytochrome-B(5) Reductase
-
Nitrate Reductases
-
Nitrate Reductase
-
Oxidoreductases Acting on Sulfur Group Donors
Associated data
-
GENBANK/J03240
-
PIR/UNKNOWN
-
SWISSPROT/UNKNOWN