K6BWK5 · K6BWK5_SCHAZ

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site227Zn2+ (UniProtKB | ChEBI)
Binding site290Zn2+ (UniProtKB | ChEBI)
Binding site291Zn2+ (UniProtKB | ChEBI)
Binding site722-726methylcob(III)alamin (UniProtKB | ChEBI)
Binding site725Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site770methylcob(III)alamin (UniProtKB | ChEBI)
Binding site826methylcob(III)alamin (UniProtKB | ChEBI)
Binding site1089S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1143-1144S-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
      BAZO_16649

Organism names

  • Taxonomic identifier
  • Strain
    • LMG 9581
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Calidifontibacillus/Schinkia group > Schinkia

Accessions

  • Primary accession
    K6BWK5

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-305Hcy-binding
Domain336-591Pterin-binding
Domain617-711B12-binding N-terminal
Domain712-847B12-binding
Domain860-1147AdoMet 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,147
  • Mass (Da)
    127,000
  • Last updated
    2013-01-09 v1
  • MD5 Checksum
    284DF0D7F1D4303D0A692ABF7F5BF271
MSHNTLQEQMQKKILIIDGAMGTMLQQANLAAADFGGELYEGCNEYLNLTAPHVIEWIHRSYFEAGADIVETNTFGATKLVLDDYELGAKAYEINKVAAELACKVRDEFSSAEWPRFVAGSMGPTTKSLSVTGGVTFDELVDNYMEQTRGLIDGGVDLLLLETSQDMRNVKAAFVGIEKARESSGKNIPLIISGTIEPMGTTLAGQSIEAFYISVEHMKPLAIGMNCATGPEFMRDHIRSLSDLSITGVSCYPNAGLPDEDGKYHESPESLAAKLAGFAEKGWLNMAGGCCGTTPDHIQALAEILKDYEPRQIPTETHHHVVSGIEPLLYDDSMRPLFVGERTNVIGSRKFKNLIIDGQLDEAAEIARAQVKNGAHVIDVCLANPDRDELEDMENFLDVLVKKIKVPLVIDSTDEKVIERALTYSQGKAIINSINLEDGEERFEKIVPLIHRYGAAVVVGTIDETGMAVTAERKLEVAERSYHLLVDKYGLSPEDIIFDPLVFPVGTGDEQYIGSANETVEGIRLIKEKMPRSLTILGVSNVSFGLPPVGREILNAVYLYHCTQAGLDYAIVNTEKLERFASIPKEEITLAEKLLFETTDEVLAEFTNLYRDKKKEVAVQKNDMTLEERLAYYIVEGTKEGLVPDLELALKEYDSPLDIINGPLMAGMAEVGRLFNENQLIVAEVLQSAEVMKASVSFLEPYMEATENDSGKGKVLLATVKGDVHDIGKNLVDIILTNNGFKVIDLGIKIAPADLIKAIKEEKPDIVGLSGLLVKSAQQMVLTAQDMKQANISVPLLVGGAALSRKFTDTRISPEYDGPVLYAKDAMNGLDLANRLQDAEERTKIINEKIEARNTAKVEEQQRNRSTILAENMRSTVSKDVPVFKPRDLEQHILKEYSIAHVEPYINMQMLLGHHLGLKGKVAKLLAEKNEKAVQLKETIDGLLTEAKTGDFLQPSAIYRFFPAQSNGDSVIIYDPDDVTKIIETFTFPRQHKEPYLCLADYLRSVDSGEMDYVGFLAVTAGKNVRKYSEKFKEEGNFLLSHAIQSLALETAEALAERVHQLIRDQWGIIDSTDLSIQDLFAAKYQGQRYSFGYPSCPEIEDQAKLFKLIRPEQIGIQLTEGFMMEPEASVTAIVFAHPEARYFNVL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJLR01000146
EMBL· GenBank· DDBJ
EKN63320.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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