A4H4V2 · A4H4V2_LEIBR

Function

function

Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

methylcob(III)alamin (UniProtKB | Rhea| CHEBI:28115 )

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site251Zn2+ (UniProtKB | ChEBI)
Binding site314Zn2+ (UniProtKB | ChEBI)
Binding site315Zn2+ (UniProtKB | ChEBI)
Binding site705methylcob(III)alamin (UniProtKB | ChEBI)
Binding site776-780methylcob(III)alamin (UniProtKB | ChEBI)
Binding site779Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site824methylcob(III)alamin (UniProtKB | ChEBI)
Binding site828methylcob(III)alamin (UniProtKB | ChEBI)
Binding site879methylcob(III)alamin (UniProtKB | ChEBI)
Binding site966S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1158S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1213-1214S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioncobalamin binding
Molecular Functionmethionine synthase activity
Molecular Functionzinc ion binding
Biological Processhomocysteine metabolic process
Biological Processmethylation
Biological Processtetrahydrofolate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine synthase
  • EC number
  • Alternative names
    • 5-methyltetrahydrofolate--homocysteine methyltransferase

Gene names

    • ORF names
      LBRM_07_0090

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MHOM/BR/75/M2904
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania > Leishmania braziliensis species complex

Accessions

  • Primary accession
    A4H4V2

Proteomes

Organism-specific databases

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-329Hcy-binding
Domain360-621Pterin-binding
Domain659-755B12-binding N-terminal
Domain766-900B12-binding
Domain915-1249AdoMet activation

Domain

Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,249
  • Mass (Da)
    138,231
  • Last updated
    2007-05-01 v1
  • Checksum
    23835D37B78CEA61
MRGERSPAFEELEELFQKRILILDGGMGTMLQRYKLEEADFRGEEFKNATKEVKGNNDLLCLTQPVKVWDVHYKYAVAGADILGTNTFNAQAVSQSDYETQHLVRRINLAAAKICRDAADQASCETGRRIFVAGVLGPLNRTASISPSVERPDYRNITYDEIVAAYTEQATALLEGGVDVLMVETIFDSLNAKAALFALNTLFDDAGYTRVPIMVSGTITDLSGRTLSGQTVEAFYLSMRHGNIISIGLNCALGCREMRPYIQRLAQISEGYVTCYPNAGLPNAMGGYDEPPEDMARDMNDFATNGWVNLVGGCCGTTPDHIHAMAMAVKSIPPRPKGQRSTTLAISGLEPLYFTNHIGFCNIGERCNLSGSLKFKRLVKEGKWEECLEVARKQVEEGAMVLDVNMDDGLIDGVAAMTRFLNLLASDPDVARVPVMIDSSKFHVIEAGLKCTQGTPIVNSISLKVGKEEFLRQARLIRRYGAAVVVMAFDENGQASDYDSKIRICKRAYDMLVADGFPAENIVFDPNVLTICTGMEEHNNYAVDFMNAAAWIKANLPGAKVSGGISNLSFSFRGFEVIRMAMHSAFLKKMIADGSLDMAIVNAGALPVYTDIEPGLLQLVEDAIYNRTPDSSERILEYADRLKAEAAARGGAEEAKVTKVDEWRNAPVEERLLHALIKGIVEFIENDVEEARTCGKYERPLHIIEGPLMDGMGKVGELFGSGKMFLPQVIKSARVMKKAVAVLVPYMEAEKLALIDSPKGKSVSRSKRVLMATVKGDVHDIGKNIVGVVLGCNSYEVIDLGVMVSCEKILAAAKEYDVDVIGLSGLITPSLDEMVHVAKEMKKMGFKIPLMVGGATTSKQHTAVKIQPHYHKTVHVLDASKSVVTVANMLGSNNEEFWEEVHETYQEIAEDYLANQKDRVYKPLAFCRENALKIDFVANPPAPRPRKLGTITISDYPLEKIVSRIDWSPFFSVWQVRGTYPNRGFPKLFNCPTVGVEAKRLFDDAQEMIKDIIATRSFRAKAVVKLMPVNSVGDDIEVYEDDTRVEKIATFFGLRQQAEKERGEPYLCISDFIAPKGVAPDYLGSLVVGIFGADKMSEQYEKDNDGYRSIMIKALADRFAEAFTEEVHRIIRTDLWGFVERETSETADLIQMQYQGIRPAPGYPSQPDHTEMATIWRLGEVEERTGVKLSESYAMMPAASVSALVFAHAQSKYFAVGKIQKDQAKDYAARKGWYLDRVESQLSSSLAYD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR798981
EMBL· GenBank· DDBJ
CAM41620.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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