5VMB

Crystal structure of a glycine hydroxymethyltransferase from Acinetobacter baumannii

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004372	molecular_function	glycine hydroxymethyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006545	biological_process	glycine biosynthetic process
A	0006565	biological_process	L-serine catabolic process
A	0006730	biological_process	one-carbon metabolic process
A	0008168	molecular_function	methyltransferase activity
A	0008270	molecular_function	zinc ion binding
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0019264	biological_process	glycine biosynthetic process from serine
A	0030170	molecular_function	pyridoxal phosphate binding
A	0032259	biological_process	methylation
A	0035999	biological_process	tetrahydrofolate interconversion
A	0046653	biological_process	tetrahydrofolate metabolic process
A	0046655	biological_process	folic acid metabolic process
A	0050897	molecular_function	cobalt ion binding
A	0070905	molecular_function	serine binding

Functional Information from PROSITE/UniProt

site_id	PS00096
Number of Residues	17
Details	SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DVtTTTTHKTLrGPRSG

Chain	Residue	Details
A	ASP221-GLY237

---