PROSITE documentation PDOC00090

{PDOC00090}
{PS00096; SHMT}
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* Serine hydroxymethyltransferase pyridoxal-phosphate attachment site *
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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.

-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.
-Last update: April 2006 / Pattern revised.

[ 1] Usha R., Savithri H.S., Rao N.A.
     "The primary structure of sheep liver cytosolic serine
     hydroxymethyltransferase and an analysis of the evolutionary
     relationships among serine hydroxymethyltransferases."
     Biochim. Biophys. Acta 1204:75-83(1994).
     PubMed=8305478

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