3ISL

Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucG) from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000256	biological_process	allantoin catabolic process
A	0004760	molecular_function	L-serine-pyruvate transaminase activity
A	0005777	cellular_component	peroxisome
A	0006144	biological_process	purine nucleobase metabolic process
A	0008453	molecular_function	alanine-glyoxylate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0016740	molecular_function	transferase activity
A	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
A	0019752	biological_process	carboxylic acid metabolic process
B	0000256	biological_process	allantoin catabolic process
B	0004760	molecular_function	L-serine-pyruvate transaminase activity
B	0005777	cellular_component	peroxisome
B	0006144	biological_process	purine nucleobase metabolic process
B	0008453	molecular_function	alanine-glyoxylate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0016740	molecular_function	transferase activity
B	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
B	0019752	biological_process	carboxylic acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP A 419

Chain	Residue
A	THR72
B	HIS268
B	THR269
A	SER73
A	ARG74
A	PHE99
A	GLY147
A	THR149
A	ASP174
A	GLN199
A	LYS200

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP B 419

Chain	Residue
A	THR269
B	THR72
B	SER73
B	ARG74
B	PHE99
B	GLY147
B	THR149
B	ASP174
B	GLN199
B	LYS200

---

Functional Information from PROSITE/UniProt

site_id	PS00595
Number of Residues	21
Details	AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDAAigGTQKclsvpsGmApI

Chain	Residue	Details
A	ILE191-ILE211

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20852637

Chain	Residue	Details
A	LYS200
B	LYS200

---