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Literature summary for 1.18.1.2 extracted from

  • Yeom, J.; Park, W.
    Biochemical characterization of ferredoxin-NADP(+) reductase interaction with flavodoxin in Pseudomonas putida (2012), BMB Rep., 45, 476-481.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of wild-type and mutants K259A, K259D. In the wild-type, the Lys259 residue is located close to the FAD cofactor. Lys258 makes van der Waals contacts to the ribose of FAD Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
K259A 50% decrease in catalytic efficiency compared to wild-type Pseudomonas putida
K259D 50% decrease in catalytic efficiency compared to wild-type Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida A0A166IXY4
-
-
Pseudomonas putida NBRC 14164 A0A166IXY4
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-

Synonyms

Synonyms Comment Organism
FprA
-
Pseudomonas putida
PP4_41290 ORF name Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
FAD
-
Pseudomonas putida

General Information

General Information Comment Organism
physiological function Phe256, which is important for binding to ferredoxin, and Lys259 are the crucial residues for electron transfer with ferredoxin Pseudomonas putida