Q8Y1G1 · GLYA1_RALN1

Function

function

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

One-carbon metabolism; tetrahydrofolate interconversion.
Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site122(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site126-128(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Site229Plays an important role in substrate specificity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioncobalt ion binding
Molecular Functionglycine hydroxymethyltransferase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functionserine binding
Molecular Functionzinc ion binding
Biological Processfolic acid metabolic process
Biological Processglycine biosynthetic process from serine
Biological ProcessL-serine catabolic process
Biological Processtetrahydrofolate interconversion

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine hydroxymethyltransferase 1
  • EC number
  • Short names
    SHMT 1
    ; Serine methylase 1

Gene names

    • Name
      glyA1
    • ORF names
      RS05124
    • Ordered locus names
      RSc0729

Organism names

Accessions

  • Primary accession
    Q8Y1G1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00001136441-415Serine hydroxymethyltransferase 1
Modified residue230N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the SHMT family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    415
  • Mass (Da)
    44,973
  • Last updated
    2002-03-27 v1
  • Checksum
    95406607D6B9388E
MFERNRYTIDQIDPEVFAAIQQENQRQEDHIELIASENYTSPAVMAAQGSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAANVQPNSGSQANQGVFFAMLKPGDTIMGMSLAEGGHLTHGMALNMSGKWFNVVSYGLNAQEDIDYDALEALAQEKKPKLIIAGASAFALRIDFERIAKVAKAVGAYFMVDMAHYAGLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMKAEHEKAINSAIFPGIQGGPLMHVIAGKAVAFKEAQSPTFKAYQEQVVKNARAMAETLMARGLRIVSGRTESHVMLVDLRAKSITGKEAEKVLGDAHITVNKNAIPNDPEKPFVTSGIRLGSPAMTTRGFKEGEAVKVAHLIADVLDNPHDEANIAAVRAKVAELTKQFPVYA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL646052
EMBL· GenBank· DDBJ
CAD14259.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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