Q0SRQ2 · GLYA_CLOPS

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.

TypeIDPosition(s)Description
Binding site119(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site123-125(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Site227Plays an important role in substrate specificity
Binding site351-353(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)

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
  • EC number
  • Short names
    SHMT
    ; Serine methylase

Gene names

    • Name
      glyA
    • Ordered locus names
      CPR_1895

Organism names

Accessions

  • Primary accession
    Q0SRQ2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10000062411-410Serine hydroxymethyltransferase
Modified residue228N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the SHMT family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    410
  • Mass (Da)
    45,205
  • Last updated
    2006-09-05 v1
  • Checksum
    2CB29FB1A86B3F19
MNFDNLEREDEQIAHLVQKEKERQENSIELIASENFVSKAVMEAMGSYLTNKYAEGYPSKRYYGGCHVVDEVEDLARERVKKLFGAEHANVQPHSGSQANMAVYFSILESGDTVLGMDLSHGGHLTHGSPVNFSGRLFNFVSYGVDKETETINYETVRELALKHKPKLIVAGASAYSRIIDFKTLREIADEVGAYLMVDIAHIAGLVATGLHPSPVPYADFVTSTTHKTLRGPRGGLILCKEKFAKVLDKNIFPGIQGGPLMHIIAAKAVCFKEALEPSFKTYMEQVVKNAHVLAEALESYGFKLVSNGTDNHLILVDLTNKDITGKDAEILLDSIGITLNKNTVPNETRSPFVTSGVRIGTPAITTRGFKEEEMKEIASIINDAIKEKDGDLEPLKARVKALCAKYPLY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000312
EMBL· GenBank· DDBJ
ABG85878.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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