CATH Classification
Domain Context
CATH Clusters
Superfamily | Methyltransferase, Cobalt-precorrin-4 Transmethylase; Domain 2 |
Functional Family | Siroheme synthase |
Enzyme Information
2.1.1.107 |
Uroporphyrinogen-III C-methyltransferase.
based on mapping to UniProt P21631
2 S-adenosyl-L-methionine + uroporphyrinogen III = 2 S-adenosyl-L- homocysteine + precorrin-2.
-!- This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. -!- It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. -!- The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4). -!- In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. -!- In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction. -!- Also involved in the biosynthesis of cobalamin.
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UniProtKB Entries (1)
P21631 |
SUMT_SINSX
Sinorhizobium sp.
Uroporphyrinogen-III C-methyltransferase
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PDB Structure
PDB | 1S4D |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structure/Function Studies on a S-Adenosyl-l-methionine-dependent Uroporphyrinogen III C Methyltransferase (SUMT), a Key Regulatory Enzyme of Tetrapyrrole Biosynthesis
J.Mol.Biol.
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