4ADD

Structural and functional study of succinyl-ornithine transaminase from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A	0006520	biological_process	amino acid metabolic process
A	0006525	biological_process	arginine metabolic process
A	0006526	biological_process	arginine biosynthetic process
A	0006527	biological_process	arginine catabolic process
A	0006593	biological_process	ornithine catabolic process
A	0008483	molecular_function	transaminase activity
A	0016740	molecular_function	transferase activity
A	0019544	biological_process	arginine catabolic process to glutamate
A	0019545	biological_process	arginine catabolic process to succinate
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042450	biological_process	arginine biosynthetic process via ornithine
A	0042802	molecular_function	identical protein binding
A	0043825	molecular_function	succinylornithine transaminase activity
B	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B	0006520	biological_process	amino acid metabolic process
B	0006525	biological_process	arginine metabolic process
B	0006526	biological_process	arginine biosynthetic process
B	0006527	biological_process	arginine catabolic process
B	0006593	biological_process	ornithine catabolic process
B	0008483	molecular_function	transaminase activity
B	0016740	molecular_function	transferase activity
B	0019544	biological_process	arginine catabolic process to glutamate
B	0019545	biological_process	arginine catabolic process to succinate
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042450	biological_process	arginine biosynthetic process via ornithine
B	0042802	molecular_function	identical protein binding
B	0043825	molecular_function	succinylornithine transaminase activity
C	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
C	0006520	biological_process	amino acid metabolic process
C	0006525	biological_process	arginine metabolic process
C	0006526	biological_process	arginine biosynthetic process
C	0006527	biological_process	arginine catabolic process
C	0006593	biological_process	ornithine catabolic process
C	0008483	molecular_function	transaminase activity
C	0016740	molecular_function	transferase activity
C	0019544	biological_process	arginine catabolic process to glutamate
C	0019545	biological_process	arginine catabolic process to succinate
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042450	biological_process	arginine biosynthetic process via ornithine
C	0042802	molecular_function	identical protein binding
C	0043825	molecular_function	succinylornithine transaminase activity
D	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
D	0006520	biological_process	amino acid metabolic process
D	0006525	biological_process	arginine metabolic process
D	0006526	biological_process	arginine biosynthetic process
D	0006527	biological_process	arginine catabolic process
D	0006593	biological_process	ornithine catabolic process
D	0008483	molecular_function	transaminase activity
D	0016740	molecular_function	transferase activity
D	0019544	biological_process	arginine catabolic process to glutamate
D	0019545	biological_process	arginine catabolic process to succinate
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042450	biological_process	arginine biosynthetic process via ornithine
D	0042802	molecular_function	identical protein binding
D	0043825	molecular_function	succinylornithine transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP A 410

Chain	Residue
A	SER104
A	LYS252
A	SUO411
A	HOH2070
A	HOH2095
A	HOH2115
A	HOH2116
A	HOH2117
B	THR281
A	GLY105
A	ALA106
A	PHE138
A	HIS139
A	GLU190
A	ASP223
A	VAL225
A	GLN226

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE SUO A 411

Chain	Residue
A	TYR18
A	PHE138
A	ARG141
A	GLU195
A	LYS252
A	PLP410
A	HOH2004
A	HOH2072
A	HOH2087
A	HOH2115
A	HOH2118
B	ASN76
B	GLY77
B	GLY279
B	THR280
B	THR281

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 410

Chain	Residue
A	THR281
A	HOH2057
A	HOH2099
B	SER104
B	GLY105
B	ALA106
B	PHE138
B	HIS139
B	GLU190
B	ASP223
B	VAL225
B	GLN226
B	LYS252
B	SUO411
B	HOH2048
B	HOH2055
B	HOH2079

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SUO B 411

Chain	Residue
A	GLY279
A	THR280
A	HOH2038
B	TYR18
B	PHE138
B	ARG141
B	GLU195
B	LYS252
B	PLP410
B	HOH2079

---

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PLP C 410

Chain	Residue
C	SER104
C	GLY105
C	ALA106
C	PHE138
C	HIS139
C	GLY140
C	GLU190
C	ASP223
C	VAL225
C	GLN226
C	LYS252
C	SUO411
C	HOH2049
C	HOH2054
C	HOH2061
C	HOH2071
C	HOH2072
C	HOH2073
D	THR281

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SUO C 411

Chain	Residue
C	TYR18
C	PHE138
C	ARG141
C	GLU195
C	LYS252
C	PLP410
C	HOH2071
D	ASN76
D	GLY77
D	GLY279
D	THR280
D	THR281

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PLP D 410

Chain	Residue
D	PHE138
D	HIS139
D	GLU190
D	ASP223
D	VAL225
D	GLN226
D	LYS252
D	SUO411
D	HOH2030
D	HOH2034
C	THR281
C	HOH2039
C	HOH2040
C	HOH2066
D	SER104
D	GLY105
D	ALA106
D	ASN109

---

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SUO D 411

Chain	Residue
C	GLY279
C	THR280
C	HOH2027
D	TYR18
D	PHE138
D	ARG141
D	GLU195
D	LYS252
D	PLP410
D	HOH2002
D	HOH2036
D	HOH2050

---

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVqt.GVgRtGelyaymhygvtp....DLLttAKalgGG

Chain	Residue	Details
A	LEU220-GLY257

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250

Chain	Residue	Details
A	LYS252
B	LYS252
C	LYS252
D	LYS252

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