Summary
Cobalamin-independent synthase
The N-terminal and C-terminal cobalamin-independent synthase domains are structurally similar, adopting a TIM beta/alpha barrel. However, the two domain perform functionally different roles. The N-terminal domain and C-terminal domains both define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilise a loop from the C-terminal domain. The C-terminal domain contains the active site residues[1].
This clan contains 3 families and the total number of domains in the clan is 4282.
Literature references
- Ferrer JL, Ravanel S, Robert M, Dumas R; , J Biol Chem 2004;279:44235-44238.: Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate. 15326182
Members
This clan contains the following 3 member families:
Meth_synt_1 Meth_synt_2 URO-DDomain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
| Pfam family | Num. domains | Alignment |
|---|---|---|
| URO-D (PF01208) | 1722 (40.2%) | View |
| Meth_synt_2 (PF01717) | 1590 (37.1%) | View |
| Meth_synt_1 (PF08267) | 970 (22.7%) | View |
| Total: 3 | Total: 4282 | Clan alignment |
Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.
Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
Tree controls
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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Interactions
There are 5 interactions for this clan. More...
| Interacting families | |
|---|---|
| A | B |
| Meth_synt_1 | Meth_synt_2 |
| Meth_synt_1 | |
| Meth_synt_2 | Meth_synt_2 |
| Meth_synt_1 | |
| URO-D | URO-D |
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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