A0A371BVB8 · A0A371BVB8_9MICC

  • Protein
    Methionine synthase
  • Gene
    metH
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site240Zn2+ (UniProtKB | ChEBI)
Binding site306Zn2+ (UniProtKB | ChEBI)
Binding site307Zn2+ (UniProtKB | ChEBI)
Binding site768-772methylcob(III)alamin (UniProtKB | ChEBI)
Binding site771Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site816methylcob(III)alamin (UniProtKB | ChEBI)
Binding site874methylcob(III)alamin (UniProtKB | ChEBI)
Binding site956S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1160S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1214-1215S-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

    • Name
      metH
    • ORF names
      DXK94_03195

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • RT-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Arthrobacter

Accessions

  • Primary accession
    A0A371BVB8

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain17-321Hcy-binding
Domain366-624Pterin-binding
Domain664-758B12-binding N-terminal
Domain758-895B12-binding
Domain909-1217AdoMet 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
    1,217
  • Mass (Da)
    131,992
  • Last updated
    2018-11-07 v1
  • Checksum
    55A413AE79D89128
MPRFALDIESVPRPARAQELLDAVNHRVVIADGAMGTMLQGRDLSLETDFQGLEGCNEILNDTRPDVLADIHDAYFATGIDAVETNTFGANWSNLSDYGIDDRIEELARKGAQIARERAEAAEKTDGRMRWVLGSMGPGTKLPSLGHTTYDYLKQTFALQAEGLIDGGADAFLIETSQDLLQTKAAVNGCKQAIVSRGIRLPIFVEVTVETTGTMLMGSEIGAALTALEPLGVDAIGLNCATGPDEMSEHLRHLSKQSSVAIACMPNAGLPVLGPNGAHYPLSPTELATAHEQFVREFGLGLVGGCCGTTPEHMAAVVERLAPFRTAAPGTEETKASNGTARTPTEREAGIASLYHHVPFDQDSAYLAIGERTNANGSKAFRQAMLEERWDDCVDIAREQVRVGAHLLDVCIDYVGRDGVADIKEVVSRFASASTLPLVIDSTEPPVLQAGLELIGGRPVVNSVNYEDGDGPNSRFARIMPLVKEHGTAVIALTINEEGQARTTEGKVAIASRLVDALVGEWGMRVEDIIVDALTFPIATGQEETRRDGIETIEAIRQITAKYPGINTTLGVSNVSFGLNPAARVVLNSVFLHEAAQAGLTSGIIDAAKIVPLASLPEEQRKVALDLVWDRREYDAEGNTTYDPLAVMLDMFAGVDTAALKDQRAAELAALPTGQRLERRIIDGEGKGLEEDLDLARSEGMTPLGIINDHLLEGMKVVGERFGAGEMQLPFVLQSAEVMKNAVALLEPHMEKSDSSGKGTMVIATVRGDVHDIGKNLVDIILTNNGYKVINIGIKQGIAEIMAAAEEHNADVIGMSGLLVKSTVVMKENLAELQSRGLAKKWPIILGGAALTRAYVEQDLAEQFDGVVRYAKDAFEGLALMEPLVRVARGESPDDVGLPPLKKRIHKGGAKFTVTEPEAMPGRSDVASDNPVPAPPFWGTRIVRGVALHDYAALLDERATFMGQWGLKPGRGEDGASYEELVEREGRPRLRYWLDRILAEGMLDASVAYGYFPVVSEGEQVVVLHHGEDHDGVLGAAGLLAPDGGSGGPIGTDRLRFDFPRQRRDRHLCLADFVKSRESGQIDVLPVQLVTAGSKIEEFTSKMFAANQYRDYYELNGLVMQLTEALAEFWHARIRKELGFAAEEPKDTAGYFKLDYRGARFSLGYPACPDMEDRRKVTELLKPERMGVVLSDELMLHPEQSTDAFVFHHPEAKYFKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QRGQ01000002
EMBL· GenBank· DDBJ
RDV12340.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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