Experimental and computational investigation of enzyme functional annotations uncovers misannotation in the EC 1.1.3.15 enzyme class
Fig 1
Sequence space of sequences annotated to EC 1.1.3.15.
Sequences listed in BRENDA and SwissProt as experimentally tested are encircled (A) Taxonomic origin of sequences. (B) Percentage of sequence identity to the closest experimentally tested or curated S-2-hydroxyacid oxidase. (C) Pfam domain architecture. (D) The mean alignment-based sequence identity between and within domain clusters. Pfam protein domains: FMN_dh (PF01070)—FMN-dependent dehydrogenase, DAO (PF01266)—FAD dependent oxidoreductase, Fer2_BFD (PF04324)—BFD-like [2Fe-2S] binding domain, FAD_binding_4 (PF01565)—FAD binding domain, FAD-oxidase_C (PF02913)—FAD linked oxidases C-terminal domain, CCG (PF02754)—cysteine-rich domain.