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56  structures 4455  species 5  interactions 12453  sequences 28  architectures

Clan: Methionine_synt (CL0160)

Summary

Cobalamin-independent synthase Add an annotation

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 12453. The clan was built by RD Finn.

Literature references

  1. 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. PUBMED:15326182 EPMC:15326182

Members

This clan contains the following 3 member families:

Meth_synt_1 Meth_synt_2 URO-D

Domain 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
Meth_synt_2 (PF01717) 4790 (38.5%) View
URO-D (PF01208) 4750 (38.1%) View
Meth_synt_1 (PF08267) 2913 (23.4%) View
Total: 3 Total: 12453 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

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This 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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