The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.
The QueF (NADPH-dependent 7-cyano-7-deazaguanine reductase) monomer is made up of two ferredoxin-like domains aligned together with their beta-sheets that have additional embellishments. QueF catalyzes the reduction of the nitrile group of 7-cyano-7-deazaguanine to 7-aminomethyl-7-deazaguanine. QueF reduces a nitrile bond to a primary amine. The two monomer units together create suitable substrate-binding pockets.
This superfamily entry consists of the C-terminal domain found in GTP cyclohydrolases I, which has been well conserved throughout evolution across bacterial and eukaryotic species. The C-terminal domain containing the regions relevant for oligomerisation and enzyme catalysis. The structure of the C-terminal domain of GTP-CH-I is topologically identical to PTPS, despite the lack of sequence homology with 6-pyruvoyl tetrahydropterin synthase (PTPS). The superfamily also includes the N-terminal domain from NADPH-dependent 7-cyano-7-deazaguanine reductase (QueF). The N-terminal domain is composed of a three-stranded beta-sheet and two alpha-helices.
|Domain clusters (>95% seq id):||18|
|Domain clusters (>35% seq id):||11|
|Structural Clusters (5A):||2|
|Structural Clusters (9A):||1|