F420 (or 8-hydroxy-5-deazaflavin) is a coenzyme involved in redox reactions in methanogens. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. This subfamily within the PPOX family occurs in at least 19 distinct species of F420 producers and is likely to bind F420 rather than FMN (flavin mononucleotide or riboflavin-5'-phosphate). The member OxyR was shown in Streptomyces rimosusto use F420 to catalyze a C5a-C11a reduction in tetracycline or oxytetracycline biosynthesis [, ], and OxyR is also known as 5a,11a-dehydrotetracycline/5a,11a-dehydrooxytetracycline reductase.
A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [].
A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [].
A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [].
Members of this protein family are HugZ, a class of heme oxygenase that belongs to the PPOX family and lacks homology to the HmuO family. This enzyme releases iron during the conversion of heme to biliverdin [, ].
Members of this family are heme utilization proteins, typically designated HutZ. They are members of the PPOX family () and, except for the lack of an N-terminal extension, are closely related to one form of heme oxidase []. Members typically are found in a three-gene operon with radical SAM enzyme HutW and a protein of unknown function, HutX. In Vibrio cholerae, HugZ is involved in heme degradation [, , , ].
This entry represents a domain superfamily that can be found in a group of putative haem-iron utilisation proteins, such as HugZ, a class of heme oxygenase that belongs to the PPOX family and lacks homology to the HmuO family. This enzyme releases iron during the conversion of heme to biliverdin [, ]. This domain can also be found at the C terminus of the glutamyl-tRNA reductase-binding (GluTRBP) protein from Arabidopsis []. GluTRBP is involved in the regulation of glutamyl-tRNA reductase (GluTR) which is important for the synthesis and distribution of 5-aminolevulinate, a precursor in heme and chlorophyll biosynthesis []. GluTRBP is necessary for efficient photosynthetic electron transport in chloroplasts [, ].
