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HemN C-terminal domain
Members of this family are all oxygen-independent coproporphyrinogen-III oxidases (HemN). This enzyme catalyses the oxygen-independent conversion of coproporphyrinogen-III to protoporphyrinogen-IX [1], one of the last steps in haem biosynthesis. The function of this domain is unclear, but comparison to other proteins containing a radical SAM domain (Pfam:PF04055) suggest it may be a substrate binding domain. [1]. 12196143. Terminal steps of haem biosynthesis. Dailey HA;. Biochem Soc Trans 2002;30:590-595. [2]. 14633981. Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes. Layer G, Moser J, Heinz DW, Jahn D, Schubert WD;. EMBO J. 2003;22:6214-6224. (from Pfam)
radical SAM protein
Radical SAM proteins catalyse diverse reactions, including unusual methylations, isomerisation, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. [1]. 11222759. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE;. Nucleic Acids Res 2001;29:1097-1106. [2]. 17335281. Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification. Benjdia A, Leprince J, Guillot A, Vaudry H, Rabot S, Berteau O;. J Am Chem Soc. 2007;129:3462-3463. [3]. 16766528. A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes. Berteau O, Guillot A, Benjdia A, Rabot S;. J Biol Chem. 2006;281:22464-22470. (from Pfam)
similar to oxygen-independent coproporphyrinogen III oxidase
protein similar to oxygen-independent coproporphyrinogen III oxidase
oxygen-independent coproporphyrinogen III oxidase
This model represents HemN, the oxygen-independent coproporphyrinogen III oxidase that replaces HemF function under anaerobic conditions. Several species, including E. coli, Helicobacter pylori, and Aquifex aeolicus, have both a member of this family and the related protein HemW, a heme chaperone (see TIGR00539).
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