Q0SFQ5 · Q0SFQ5_RHOJR

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

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

Pathway

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

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site135(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site139-141(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Site243Plays an important role in substrate specificity
Binding site259(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioncobalt ion binding
Molecular Functionglycine hydroxymethyltransferase activity
Molecular Functionmethyltransferase 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 Processmethylation
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
    • Synonyms
      glyA1
    • Ordered locus names
      RHA1_ro01820

Organism names

Accessions

  • Primary accession
    Q0SFQ5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue244N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-404Serine hydroxymethyltransferase-like

Sequence similarities

Belongs to the SHMT family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    441
  • Mass (Da)
    47,330
  • Last updated
    2006-09-05 v1
  • MD5 Checksum
    2EDCE2D45DB02C96126BE827499E06AB
MTVDTAHLTEAAAANPTLTHSLADLDPAVHQAIAAELGRQQGTLEMIASENFAPLAVMQAQGSVLTNKYAEGYPGRRYYGGCEHVDVIEQLAIDRLTALFGAKFANVQPHSGAQANAAAMSALLEPGDGILGLDLAHGGHLTHGMKLNFSGKLYDVAAYHVREDDHLVDMDEVEHLAREHRPKLILAGWSAYTRQLDFAAFRRIADEVGAYLMVDMAHFAGLVAAGLHPSPVPHAHVVTSTTHKTLGGPRGGVILTNDEALAKKFNSSVFPGQQGGPLEHVIAGKAVSFKLAAEPEFRERQERTLAGAKILADRLLKDDSRQAGINVVSGGTDVHLVLVDLRESELDGKQAEDRLHRVGITVNRNAVPFDPRPPMVSSGVRIGTPALATRGFDLDAFTEVADIISYALRPATDEAGLDELRGRVDALALRFPLYPDLTEAN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000431
EMBL· GenBank· DDBJ
ABG93631.1
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