Summary: Cobalamin-independent synthase, N-terminal domain
Cobalamin-independent synthase, N-terminal domain Provide feedback
The N-terminal domain and C-terminal domains of cobalamin-independent synthases together 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 .
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
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This tab holds annotation information from the InterPro database.
InterPro entry IPR013215
Cobalamin-independent methionine synthase, MetE, catalyses the synthesis of the amino acid methionine by the transfer of a methyl group from methyltetrahydrofolate to homocysteine [PUBMED:15326182]. The N-terminal and C-terminal domains of MetE together 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 mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||zinc ion binding (GO:0008270)|
|5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity (GO:0003871)|
|Biological process||cellular amino acid biosynthetic process (GO:0008652)|
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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.
The clan contains the following 3 members:Meth_synt_1 Meth_synt_2 URO-D
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_553 (release 17.0)|
|Number in seed:||56|
|Number in full:||2913|
|Average length of the domain:||302.40 aa|
|Average identity of full alignment:||41 %|
|Average coverage of the sequence by the domain:||42.29 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Meth_synt_1 domain has been found. There are 25 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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