A0AAA9S438 · A0AAA9S438_BOVIN

  • Protein
    Methionine synthase
  • Gene
    MTR
  • 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 methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol. MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl group from 5-methyltetrahydrofolate. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine.

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 site260Zn2+ (UniProtKB | ChEBI)
Binding site323Zn2+ (UniProtKB | ChEBI)
Binding site324Zn2+ (UniProtKB | ChEBI)
Binding site649methylcob(III)alamin (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 site774methylcob(III)alamin (UniProtKB | ChEBI)
Binding site826methylcob(III)alamin (UniProtKB | ChEBI)
Binding site914S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1112S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1167-1168S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioncobalamin binding
Molecular Functionmethionine synthase activity
Molecular Functionzinc ion binding
Biological Processmethylation
Biological Processpteridine-containing compound 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
      MTR

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    A0AAA9S438

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain19-338Hcy-binding
Domain371-649Pterin-binding
Domain602-699B12-binding N-terminal
Domain712-847B12-binding
Domain863-1205AdoMet 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
    1,205
  • Mass (Da)
    133,714
  • Last updated
    2024-05-29 v1
  • Checksum
    14A45DD9750AF361
MAPTLQDLTPSAGMKKTLQDEIEAILQERIMVLDGGMGTMIQQHKLSEEDFRGQEFKDHARPLKGNNDILSITQPSVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMCSAGVARKAAEDISLQTGIKRYVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYKEQAKGLLDGGVDILLIETIFDTANAKAALFAVQKLFEEEYVPRPVFISGTIVDKSGRTLSGQTGEAFVISVSHADPLCIGLNCALGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPHVMAMHLKDFAVDGLVNIVGGCCGTTPDHIREIAEAVKNCKPRVPPATVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRRFAKLIMAGNYEEALSVAKMQVEMGAQVLDINMDDGMLDGPSAMTRFCNFIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKFGAAVVVMAFDEEGQETLPGAKVSGGLSNLSFSFRGMEAIREAMHGVFLYHAIKFGMDMGIVNAGSLPVYDDIHKELLQLCEDLIWNRDPEATEKLLHYAQTQGKGGKKVIQTDEWRNGPLEERLEYALVKGIEKYIIEDTEEARLNQEKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETKVLTGKIEDEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDEYFEEILEEYEDIRQDHYESLKERRYLTLRQARENGFHIDWLSEPPPVKPTFLGTRVFEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFDDKTVGEEAKKVYDDAQNMLQALISQKKLQARGVVGFWPAQSIQDDIHLYAEGAVPQASEPIATFYGLRQQAEKDSASSDPYLCLSDFIAPLHSGIPDYLGLFAVACFGVEELSKAYEEECDDYSSIMVKALGDRLAEAFAEELHERVRRELWGYCSGEQLAVADLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLADVEQRTGIRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQIEDYASRKNMSVAEVEKWLGPILGYDTD

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A3Q1MEQ8A0A3Q1MEQ8_BOVINMTR1264
A0AAA9SRP9A0AAA9SRP9_BOVINMTR263
A0AAA9TNH8A0AAA9TNH8_BOVINMTR1202
F1N0S3F1N0S3_BOVINMTR1245
A0AAA9TZN1A0AAA9TZN1_BOVINMTR1119
A0A3Q1M346A0A3Q1M346_BOVINMTR1214

Keywords

Genome annotation databases

Similar Proteins

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