7JH3

Crystal structure of 4-aminobutyrate aminotransferase PuuE from Escherichia coli in complex with PLP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003867	molecular_function	4-aminobutyrate transaminase activity
A	0005829	cellular_component	cytosol
A	0008483	molecular_function	transaminase activity
A	0009447	biological_process	putrescine catabolic process
A	0009448	biological_process	gamma-aminobutyric acid metabolic process
A	0009450	biological_process	gamma-aminobutyric acid catabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
B	0003867	molecular_function	4-aminobutyrate transaminase activity
B	0005829	cellular_component	cytosol
B	0008483	molecular_function	transaminase activity
B	0009447	biological_process	putrescine catabolic process
B	0009448	biological_process	gamma-aminobutyric acid metabolic process
B	0009450	biological_process	gamma-aminobutyric acid catabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
C	0003867	molecular_function	4-aminobutyrate transaminase activity
C	0005829	cellular_component	cytosol
C	0008483	molecular_function	transaminase activity
C	0009447	biological_process	putrescine catabolic process
C	0009448	biological_process	gamma-aminobutyric acid metabolic process
C	0009450	biological_process	gamma-aminobutyric acid catabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
D	0003867	molecular_function	4-aminobutyrate transaminase activity
D	0005829	cellular_component	cytosol
D	0008483	molecular_function	transaminase activity
D	0009447	biological_process	putrescine catabolic process
D	0009448	biological_process	gamma-aminobutyric acid metabolic process
D	0009450	biological_process	gamma-aminobutyric acid catabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
E	0003867	molecular_function	4-aminobutyrate transaminase activity
E	0005829	cellular_component	cytosol
E	0008483	molecular_function	transaminase activity
E	0009447	biological_process	putrescine catabolic process
E	0009448	biological_process	gamma-aminobutyric acid metabolic process
E	0009450	biological_process	gamma-aminobutyric acid catabolic process
E	0030170	molecular_function	pyridoxal phosphate binding
E	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
F	0003867	molecular_function	4-aminobutyrate transaminase activity
F	0005829	cellular_component	cytosol
F	0008483	molecular_function	transaminase activity
F	0009447	biological_process	putrescine catabolic process
F	0009448	biological_process	gamma-aminobutyric acid metabolic process
F	0009450	biological_process	gamma-aminobutyric acid catabolic process
F	0030170	molecular_function	pyridoxal phosphate binding
F	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MIaDEVqs.GFaRtGklfamdhyadkp....DLMtmAKslaGG

Chain	Residue	Details
A	MET235-GLY272

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY110
D	GLY110
D	ASP238
D	THR296
E	GLY110
E	ASP238
E	THR296
F	GLY110
F	ASP238
F	THR296
A	ASP238
A	THR296
B	GLY110
B	ASP238
B	THR296
C	GLY110
C	ASP238
C	THR296

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site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250

Chain	Residue	Details
A	LLP267
B	LLP267
C	LLP267
D	LLP267
E	LLP267
F	LLP267

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