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CATH Superfamily 3.40.1010.10

Tetrapyrrole methylase, N-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Cobalt-precorrin-4 Transmethylase; Domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 7260: Precorrin-2 C20-methyltransferase / cobalt-factor ...

There are 4 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Precorrin-2 C(20)-methyltransferase. [EC: 2.1.1.130]
S-adenosyl-L-methionine + precorrin-2 = S-adenosyl-L-homocysteine + precorrin-3A.
    		 124 A0A045JH32 A0A049EEE8 A0A071KSC6 A0A083W4R5 A0A086C065 A0A095FX07 A0A0A1FTF7 A0A0A8RHH0 A0A0D6IGR3 A0A0E0UGT8
    (114 more...)
    Precorrin-3B C(17)-methyltransferase. [EC: 2.1.1.131]
    S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine + precorrin-4.
    • In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A.
    • The first of the four steps is carried out by EC 1.14.13.83 (CobG), yielding precorrin-3B as the product.
    • This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin- 4, precorrin-5 and precorrin-6A, respectively.
    		 37 A0A045JH32 A0A049EEE8 A0A081HX54 A0A083W4R5 A0A0D6IGR3 A0A0E2WS29 A0A0G4E456 A0A0H2ZT64 A0A0H3LEN5 A0A0H3M7N3
    (27 more...)
    Cobalt-factor II C(20)-methyltransferase. [EC: 2.1.1.151]
    S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III.
    • Involved in the anaerobic biosynthesis of vitamin B12.
    		 18 A0A071KSC6 A0A0E1AVS1 A0A0H2ZCZ6 A0A0H3RAY3 A0A0N7LJ16 A0A157WTQ5 A0A1D5BWA6 A0A1E9CM46 A0A1F0J980 A0A1G5KSV9
    (8 more...)
    Uroporphyrinogen-III C-methyltransferase. [EC: 2.1.1.107]
    (1) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L- homocysteine + precorrin-1. (2) S-adenosyl-L-methionine + precorrin-1 = 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.
    		 1 A0A0B8N7C9