3RUY

Crystal Structure of the Ornithine-oxo acid transaminase RocD from Bacillus anthracis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004587	molecular_function	ornithine aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0006561	biological_process	proline biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0010121	biological_process	arginine catabolic process to proline via ornithine
A	0019544	biological_process	arginine catabolic process to glutamate
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0055129	biological_process	L-proline biosynthetic process
B	0004587	molecular_function	ornithine aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0006561	biological_process	proline biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0010121	biological_process	arginine catabolic process to proline via ornithine
B	0019544	biological_process	arginine catabolic process to glutamate
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
B	0055129	biological_process	L-proline biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FVaDEIqt.GLgRtGkvfacdwdnvtp....DMYilGKalgGG

Chain	Residue	Details
A	PHE223-GLY260

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01689

Chain	Residue	Details
A	LLP255
B	LLP255

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