7SZP

Crystal Structure of Histidinol-phosphate aminotransferase from Klebsiella pneumoniae subsp. pneumoniae (strain HS11286)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0004400	molecular_function	histidinol-phosphate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0000105	biological_process	L-histidine biosynthetic process
B	0004400	molecular_function	histidinol-phosphate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
C	0000105	biological_process	L-histidine biosynthetic process
C	0004400	molecular_function	histidinol-phosphate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
D	0000105	biological_process	L-histidine biosynthetic process
D	0004400	molecular_function	histidinol-phosphate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PROSITE/UniProt

site_id	PS00599
Number of Residues	10
Details	AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLSKAFALAG

Chain	Residue	Details
A	THR208-GLY217

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255\|HAMAP-Rule:MF_01023