A0A8T1PUH5 · A0A8T1PUH5_CARIL

Function

function

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.

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:
Co2+ (UniProtKB | Rhea| CHEBI:48828 )

K+ (UniProtKB | Rhea| CHEBI:29103 )

Note: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Note: Binds 2 divalent ions per subunit. The metal ions interact primarily with the substrate. Can utilize magnesium, manganese or cobalt (in vitro).

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionmethionine adenosyltransferase activity
Biological Processone-carbon metabolic process
Biological ProcessS-adenosylmethionine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    S-adenosylmethionine synthase
  • EC number

Gene names

    • ORF names
      CIPAW_07G034900
      , I3842_07G035200

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fagales > Juglandaceae > Carya

Accessions

  • Primary accession
    A0A8T1PUH5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-101S-adenosylmethionine synthetase N-terminal
Domain117-238S-adenosylmethionine synthetase central
Domain240-381S-adenosylmethionine synthetase C-terminal

Sequence similarities

Belongs to the AdoMet synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    393
  • Mass (Da)
    43,209
  • Last updated
    2022-10-12 v1
  • Checksum
    9D5560B8292315C2
MDTFLFTSESVNEGHPDKLCDQISDAVLDACLEHDPESKVACETCTKTNMVMVFGEITTETNVDYEKIVRDTCRSIGFISNDVGLDADNCKVLVNIEQQSPDIAQGVHGHLTKRPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTDVRKSGTCPWLRPDGKTQVTVEYYNDHGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVANGLARRCIVQVSYAIGVPEPLSVFVDTYCTGKIPDKEILKIVKENFDFRPGMISINLDLKRGGNGRFLKTAAYGHFGRDDPDFTWEVVKPLKWDKPLE

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8T1PRM6A0A8T1PRM6_CARILCIPAW_07G034900398

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM031815
EMBL· GenBank· DDBJ
KAG6646825.1
EMBL· GenBank· DDBJ
Genomic DNA
CM031831
EMBL· GenBank· DDBJ
KAG6702469.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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