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InterPro: IPR013215 Cobalamin (vitamin B12)-independent methionine synthase MetE, N-terminal

Protein matchesHelp
UniProtKB
Matches:
1062 proteins
AccessionHelp IPR013215 Cbl-indep_Met_Synth_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR006276 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
GO Term annotationHelp
Process GO:0008652 cellular amino acid biosynthetic process
Function GO:0003871 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
GO:0008270 zinc ion binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Cobalamin-independent methionine synthase, MetE, catalyses the synthesis of the amino acid methionine by the transfer of a methyl group from methyltetrahydrofolate to homocysteine [1]. 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.

Structural linksHelp
SCOP: c.1.22.2
CATH: 3.20.20.210
Database linksHelp
Enzyme: EC:2.1.1.14
Blocks: IPB013215
Pfam Clan: CL0160.7

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR013215 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O50008 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

P05694 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

P82610 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

Q117R7 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

Q8CWX6 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013215 Cobalamin (vitamin B12)-independent methionine synthase MetE, N-terminal
IPR006276 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
IPR002629 Methionine synthase, vitamin-B12 independent
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Ferrer JL, Ravanel S, Robert M, Dumas R.
Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate.
J. Biol. Chem. 279 44235-8 2004 [PubMed: 15326182]
http://dx.doi.org/10.1074/jbc.C400325200

Additional ReadingHelp
Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML.
Metal active site elasticity linked to activation of homocysteine in methionine synthases.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 3286-91 [PubMed: 18296644]
http://dx.doi.org/10.1073/pnas.0709960105
Pejchal R, Ludwig ML.
Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication.
PLoS Biol. 3 2005 e31 [PubMed: 15630480]
http://dx.doi.org/10.1371/journal.pbio.0030031
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InterPro 23.1