Protein Family Models

The QueF monomer is made up of two ferredoxin-like domains aligned together with their beta-sheets that have additional embellishments. This subunit is composed of a three-stranded beta-sheet and two alpha-helices. QueF reduces a nitrile bond to a primary amine. The two monomer units together create suitable substrate-binding pockets [1]. [1]. 20875425. High-resolution structure of the nitrile reductase QueF combined with molecular simulations provide insight into enzyme mechanism. Kim Y, Zhou M, Moy S, Morales J, Cunningham MA, Joachimiak A;. J Mol Biol. 2010;404:127-137. (from Pfam)

Date:

2024-10-16

This protein is involved in the biosynthesis of queuosine. In some proteins this domain appears to be fused to Pfam:PF06508. [1]. 15767583. From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold. Van Lanen SG, Reader JS, Swairjo MA, de Crecy-Lagard V, Lee B, Iwata-Reuyl D;. Proc Natl Acad Sci U S A. 2005;102:4264-4269. (from Pfam)

Date:

2024-10-16

NADPH-dependent 7-cyano-7-deazaguanine reductase catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) in queuosine biosynthesis

Date:

2023-03-21

This enzyme catalyzes the 4-electron reduction of the cyano group of 7-cyano-7-deazaguanine (preQ0) to an amine. Although related to a large family of GTP cyclohydrolases (PF01227), the relationship is structural and not germane to the catalytic mechanism. This mode represents the longer, gram-negative version of the enzyme as found in E. coli. The enzymatic step represents the first point at which the biosynthesis of queuosine in bacteria and eukaryotes is distinguished from the biosynthesis of archaeosine in archaea.

Gene:

queF

Date:

2021-04-27