B9IRU8 · GLYA_BACCQ

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 site117(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site121-123(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Site225Plays an important role in substrate specificity
Binding site239(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site349-351(6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglycine hydroxymethyltransferase activity
Molecular Functionpyridoxal phosphate binding
Biological Processglycine biosynthetic process from serine
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
      BCQ_5156

Organism names

Accessions

  • Primary accession
    B9IRU8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10001954321-413Serine hydroxymethyltransferase
Modified residue226N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the SHMT family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    413
  • Mass (Da)
    45,178
  • Last updated
    2009-03-24 v1
  • Checksum
    139F161843D3EABC
MDHLKRQDEKVFAAIEAELGRQRSKIELIASENFVSEAVMEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVEDIARDRVKEIFGAEHVNVQPHSGAQANMAVYFTILEQGDTVLGMNLSHGGHLTHGSPVNFSGVQYNFVEYGVDAESHRINYDDVLAKAKEHKPKLIVAGASAYPRVIDFKRFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGGMILCEEQFAKQIDKSIFPGIQGGPLMHVIAAKAVAFGEALQDDFKTYAQNIINNANRLAEGLQKEGLTLVSGGTDNHLILIDVRNLEITGKVAEHVLDEVGITVNKNTIPFETASPFVTSGVRIGTAAVTSRGFGLEEMDEIASLIAYTLKNHENEAALEEARKRVEALTSKFPMYTDL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000227
EMBL· GenBank· DDBJ
ACM15556.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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