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PROSITE documentation PDOC00090

Serine hydroxymethyltransferase pyridoxal-phosphate attachment site

Description:

Serine hydroxymethyltransferase (EC 2.1.2.1) (SHMT) [1] catalyzes the transfer of the hydroxymethyl group of serine to tetrahydrofolate to form 5,10-methylenetetrahydrofolate and glycine. In vertebrates, it exists in a cytoplasmic and a mitochondrial form whereas only one form is found in prokaryotes. Serine hydroxymethyltransferase is a pyridoxal-phosphate containing enzyme. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme.

Last update:

April 2006 / Pattern revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

SHMT, PS00096; Serine hydroxymethyltransferase pyridoxal-phosphate attachment site  (PATTERN)
Consensus pattern: [DEQHY]-[LIVMFYA]-x-[GSTMVA]-[GSTAV]-[ST]-[STVM]-[HQ]-K-[STG]-[LFMI]-x-[GAS]-[PGAC]-[RQ]-[GSARH]-[GA]
K is the pyridoxal-P attachment site
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE
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• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00096
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• Scan Swiss-Prot/TrEMBL entries against PS00096
• view ligand binding statistics
Matching PDB structures: 1BJ4 1CJ0 1DFO 1EJI ... [ALL]

Reference:

1 AuthorsUsha R., Savithri H.S., Rao N.A.
TitleThe primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases.
SourceBiochim. Biophys. Acta 1204:75-83(1994).
PubMed ID8305478

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