A0A2V5JZU7 · A0A2V5JZU7_UNCVE

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 active site, binding site, site.

TypeIDPosition(s)Description
Active site8Nucleophile
Active site14
Active site122Proton donor
Binding site301(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site305-307(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Site409Plays an important role in substrate specificity
Binding site424(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 Functionprotein tyrosine phosphatase 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 Processprotein dephosphorylation
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
      DMC57_00195
      , DME29_00435

Organism names

Accessions

  • Primary accession
    A0A2V5JZU7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue410N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain2-151Phosphotyrosine protein phosphatase I
Compositional bias158-183Polar residues
Region158-189Disordered

Sequence similarities

Belongs to the SHMT family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    595
  • Mass (Da)
    64,391
  • Last updated
    2018-09-12 v1
  • Checksum
    17387679908BF51B
MKSVLFVCTGNVCRSPIAEGLFRRLLGNRKDIEVASAGVHAVRGQPPSSHAVDVCAEEGADIGNLRSQPLAGALVERATHIFAMTGAHVEAIQMLFPNAADKTFLLREFEEAGATCWRDVPDPIGLGRDVYNSCAETIKNALPSVLAFVEQSEVAVRSSGRSGGSSTYLMSDISHSTEPSLSAPSGGLGKVDPEIYDAVAAEEKRQRENIELIASENFTSRAVMEAQGSVLTNKYAEGYPGKRWYGGCENVDTVESLAIDRARRLFGAEHVNVQPHSGSQANMAVYFSTLKVGDKILTMNLAHGGHLTHGHPANFSGKFYQVTHYGVAEKTEQIDYDALEKLANETKPAMITAGASAYPRTLDFPRLRHIADACGALLFIDMAHIAGLVAGGQHPSPIPHAQFVTTTTHKSLRGPRGGIVLCQEKYAKQIDSMVFPGIQGGPLMHVIAAKAVCFHEALQPQFRAYQKQVVTNAKALAAGLSKHGYRIVSGGTDNHLMLVDLRHKEINGKQAQEVLDRAGITVNKNAIPFDTYPIFKPGGIRVGTPAVTTRGMREEEMLEIADLVAEALQNRDDNAALERIRGKVRELTRRFPLPS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias158-183Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QHMN01000008
EMBL· GenBank· DDBJ
PYI45137.1
EMBL· GenBank· DDBJ
Genomic DNA
QHQU01000007
EMBL· GenBank· DDBJ
PYL45890.1
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