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Porphobilinogen deaminase, C-terminal domain
uroporphyrinogen-III synthase
This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyses the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as Swiss:Q59294 with Pfam:PF00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway [2]. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease [1]. [1]. 8829650. Molecular basis of congenital erythropoietic porphyria: mutations in the human uroporphyrinogen III synthase gene. Xu W, Astrin KH, Desnick RJ;. Hum Mutat 1996;7:187-192. [2]. 7597845. Isolation of the gene HEM4 encoding uroporphyrinogen III synthase in Saccharomyces cerevisiae. Amillet JM, Labbe-Bois R;. Yeast 1995;11:419-424. (from Pfam)
Porphobilinogen deaminase, dipyromethane cofactor binding domain
SAM-dependent methyltransferase
This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function, including Swiss:P45528. This family includes the methylase Dipthine synthase. (from Pfam)
uroporphyrinogen-III C-methyltransferase
This HMM represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities.
hydroxymethylbilane synthase
Catalyzes the transformation of porphobilinogen to hydroxymethylbilane in porphyrin biosynthesis
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