A5WD09 · A5WD09_PSYWF

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 site289Zn2+ (UniProtKB | ChEBI)
Binding site352Zn2+ (UniProtKB | ChEBI)
Binding site353Zn2+ (UniProtKB | ChEBI)
Binding site739methylcob(III)alamin (UniProtKB | ChEBI)
Binding site801-805methylcob(III)alamin (UniProtKB | ChEBI)
Binding site804Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site849methylcob(III)alamin (UniProtKB | ChEBI)
Binding site853methylcob(III)alamin (UniProtKB | ChEBI)
Binding site906methylcob(III)alamin (UniProtKB | ChEBI)
Binding site993S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1183S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1238-1239S-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

    • Ordered locus names
      PsycPRwf_0595

Organism names

Accessions

  • Primary accession
    A5WD09

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-29Disordered
Compositional bias7-21Basic and acidic residues
Domain47-367Hcy-binding
Domain398-658Pterin-binding
Domain695-789B12-binding N-terminal
Domain791-927B12-binding
Domain943-1272AdoMet 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
    1,272
  • Mass (Da)
    140,989
  • Last updated
    2007-07-10 v1
  • Checksum
    EF63F634CBFEEDAB
MANCSHPEHNTKKDLPETAIKKGHNPDNFNLVPPAKFPFKEQQLTARQRIVEQLNQRILMLDGAMGTQIQTFKLGESDYRGERFADFTQDVQGNNDLLVLTQPELIKSIHRDHLTAGADIIETNSFNGTQISMADYAMEHLVPEINKEAARLAREVADEFTAQNPDKPRFVAGVIGPTSRTCSLSPDVNDPAYRNVTFDELVDNYTEALFALIEGGIDLVLIETIFDTLNAKAAIFAVTGVFETIGFELPIMISGTITDASGRTLSGQTAEAFYNSIRHAKPLSVGFNCALGADALKPHIQTLSDIADTYISAHPNAGLPNEFGEYDETPEQTAALLDGFGKSGLLNIVGGCCGTRPEHIKAIHDVMQKYPPRQIPTIAPACRLSGLEPFTITKDSLFVNVGERTNVTGSKKFLRLIKTGEFTEALDVARNQVDGGAQIVDINMDEGMLDSKGAMIHFLNLVAGEPDISRVPLMIDSSKWDIIEEGLKRTQGKSVVNSISLKEGYDEFVKHAKLCMRYGAAVIVMAFDEDGQADSYERKIQICQRSYDILVNEVGFPSEDIIFDPNIFAVATGITEHNNYGADFINATRWITDNLPNAMVSGGVSNVSFSFRGNPIREAINAVFLYHAIQAGLTMGIVNPAMLEVYDEIPKEARDAIEDVMLNRNQGESGQEATERLMTIAEAYVAGGKKNDGTIDLSWREQSVEKRIEHALVKGITTYIDEDTEEARLKYPKPLHVIEGPLMDGMNVVGDLFGAGKMFLPQVVKSARVMKRAVAVLNPYIEAEKVEGEVKGKVVMATVKGDVHDIGKNIVGVVLGCNGYDVVDLGVMVPCDKILDTAIAEKADIIGLSGLITPSLDEMVYVAKQMQERGMTLPLMIGGATTSKAHTAVKIEPNYQNDAVIYVSDASRSVGVVTKLLSQEHRVELLRETREEYQKVRERLANRKPKAAKLSYQESIEQGFKFDWDNYTPPVPNEQGQIIFDNYPIENLLPYIDWTPFFVSWGLVGKYPKIFDDEVVGAEAKDLFANAKALMQTFIDEQLVTPKGVFKIMPARRTDHDTVTVYDKEPSAGGQPTHVFEHLRQQSDKASGKPNYSLADFISPSEDYDDYLGGFTVSIVGAQELSDSYKEAGDDYNAIMVQALCDRLAEAFAEHLHELIRTKYWGYQPTEQLTNEELIKEKYVGIRPAPGYPACPEHTEKGKLFDWLDTTNAIGTYLTESFAMWPASSVSGFYYSHPESTYFNVGKIDRDQLEDYAKRKDWDIKTAEKWLNPNLT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias7-21Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000713
EMBL· GenBank· DDBJ
ABQ93550.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help