1Z7D

Ornithine aminotransferase PY00104 from Plasmodium Yoelii

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004587	molecular_function	ornithine aminotransferase activity
A	0005737	cellular_component	cytoplasm
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	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
C	0004587	molecular_function	ornithine aminotransferase activity
C	0005737	cellular_component	cytoplasm
C	0008483	molecular_function	transaminase activity
C	0010121	biological_process	arginine catabolic process to proline via ornithine
C	0019544	biological_process	arginine catabolic process to glutamate
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
C	0055129	biological_process	L-proline biosynthetic process
D	0004587	molecular_function	ornithine aminotransferase activity
D	0005737	cellular_component	cytoplasm
D	0008483	molecular_function	transaminase activity
D	0010121	biological_process	arginine catabolic process to proline via ornithine
D	0019544	biological_process	arginine catabolic process to glutamate
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding
D	0055129	biological_process	L-proline biosynthetic process
E	0004587	molecular_function	ornithine aminotransferase activity
E	0005737	cellular_component	cytoplasm
E	0008483	molecular_function	transaminase activity
E	0010121	biological_process	arginine catabolic process to proline via ornithine
E	0019544	biological_process	arginine catabolic process to glutamate
E	0030170	molecular_function	pyridoxal phosphate binding
E	0042802	molecular_function	identical protein binding
E	0055129	biological_process	L-proline biosynthetic process
F	0004587	molecular_function	ornithine aminotransferase activity
F	0005737	cellular_component	cytoplasm
F	0008483	molecular_function	transaminase activity
F	0010121	biological_process	arginine catabolic process to proline via ornithine
F	0019544	biological_process	arginine catabolic process to glutamate
F	0030170	molecular_function	pyridoxal phosphate binding
F	0042802	molecular_function	identical protein binding
F	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. FVaDEVqt.GLgRtGkllcvhhynvkp....DVIllGKalsGG

Chain	Residue	Details
A	PHE229-GLY266

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P04181

Chain	Residue	Details
A	LYS261
B	LYS261
C	LYS261
D	LYS261
E	LYS261
F	LYS261

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	LYS261
A	ASP232

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site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
D	ASP232

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site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
E	ASP232

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site_id	CSA12
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
F	ASP232

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	PHE173
B	LYS261
B	ASP232

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	LYS261
C	ASP232

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
D	LYS261
D	ASP232

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site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
E	LYS261
E	ASP232

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site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
F	LYS261
F	ASP232

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site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ASP232

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site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	PHE173
B	ASP232

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site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	ASP232

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