M3FQ95 · M3FQ95_9ACTN

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 site125(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site129-131(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Site233Plays an important role in substrate specificity
Binding site249(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
    • ORF names
      SBD_3957

Organism names

Accessions

  • Primary accession
    M3FQ95

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue234N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-380Serine hydroxymethyltransferase-like

Sequence similarities

Belongs to the SHMT family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    412
  • Mass (Da)
    43,349
  • Last updated
    2013-05-01 v1
  • Checksum
    2559BCD9AEB4963D
MSVTPVLEADVLRRQDPELADVLLGEQDRQATTLQLVAAENFTSPAVLAALGSPLANKYAEGYPGARHHGGCEMVDVAERLAVERARSLFGAEHANVQSHSGSSAVLAAYAALLRPGDTVLAMGLHFGGHLTHGSPANFSGRWFDFVGYGVEAESGLIDREQVRTLARTHRPKALVCGSISYPRHIDYAFFREVADEVGAYLIVDAAHPIGLVAGGAAPNPVPYADIVCATTHKVLRGPRGGMLLCGDELAERVDRAVFPFTQGGAQMHTIAAKAVAFGEAATPAFTAYAHQVVANARVLARGLAEEGLVVVTGGTDTHLLTVDPAPLGVDGRTARGRLAAAGMVLDCCALPHDDARGLRLGTAALTTQGMGETEMARLAVLFAGALRDGGNGKRTREEVRELAGRFPPYPR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KB405078
EMBL· GenBank· DDBJ
EMF54289.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
FeedbackHelp