6F77

Crystal structure of the prephenate aminotransferase from Rhizobium meliloti

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0006520	biological_process	amino acid metabolic process
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
A	0033854	molecular_function	glutamate-prephenate aminotransferase activity
B	0003824	molecular_function	catalytic activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0006520	biological_process	amino acid metabolic process
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
B	0033854	molecular_function	glutamate-prephenate aminotransferase activity
C	0003824	molecular_function	catalytic activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0005737	cellular_component	cytoplasm
C	0006520	biological_process	amino acid metabolic process
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
C	0033854	molecular_function	glutamate-prephenate aminotransferase activity
D	0003824	molecular_function	catalytic activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0005737	cellular_component	cytoplasm
D	0006520	biological_process	amino acid metabolic process
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
D	0033854	molecular_function	glutamate-prephenate aminotransferase activity
E	0003824	molecular_function	catalytic activity
E	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
E	0005737	cellular_component	cytoplasm
E	0006520	biological_process	amino acid metabolic process
E	0008483	molecular_function	transaminase activity
E	0009058	biological_process	biosynthetic process
E	0016740	molecular_function	transferase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0033854	molecular_function	glutamate-prephenate aminotransferase activity
F	0003824	molecular_function	catalytic activity
F	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
F	0005737	cellular_component	cytoplasm
F	0006520	biological_process	amino acid metabolic process
F	0008483	molecular_function	transaminase activity
F	0009058	biological_process	biosynthetic process
F	0016740	molecular_function	transferase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0033854	molecular_function	glutamate-prephenate aminotransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue PLP A 600

Chain	Residue
A	GLY99
A	TYR207
A	SER239
A	LYS240
A	ARG248
A	HOH761
B	TYR64
B	HOH688
A	GLY100
A	LYS101
A	TRP125
A	TYR128
A	ASN171
A	ASN175
A	ASP204
A	MET206

---

site_id	AC2
Number of Residues	14
Details	binding site for residue PLP C 600

Chain	Residue
C	GLY99
C	GLY100
C	LYS101
C	TRP125
C	ASN171
C	ASN175
C	ASP204
C	MET206
C	TYR207
C	SER239
C	LYS240
C	ARG248
C	HOH743
D	TYR64

---

site_id	AC3
Number of Residues	14
Details	binding site for residue PLP D 600

Chain	Residue
C	TYR64
D	GLY99
D	GLY100
D	LYS101
D	TRP125
D	ASN171
D	ASN175
D	ASP204
D	MET206
D	TYR207
D	SER239
D	LYS240
D	ARG248
D	HOH723

---

site_id	AC4
Number of Residues	14
Details	binding site for residue PLP E 600

Chain	Residue
E	GLY99
E	GLY100
E	LYS101
E	TRP125
E	ASN171
E	ASN175
E	ASP204
E	MET206
E	TYR207
E	SER239
E	LYS240
E	ARG248
E	HOH793
F	TYR64

---

site_id	AC5
Number of Residues	22
Details	binding site for Di-peptide PLP F 600 and LYS F 240

Chain	Residue
E	TYR64
E	HOH861
F	GLY39
F	PRO41
F	GLY99
F	GLY100
F	LYS101
F	TRP125
F	ASN171
F	ASN175
F	ASP204
F	MET206
F	TYR207
F	VAL238
F	SER239
F	ALA241
F	TYR242
F	ALA243
F	ARG248
F	HOH743
F	HOH794
F	HOH846

---

Functional Information from PROSITE/UniProt

site_id	PS00105
Number of Residues	14
Details	AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GVSKayAMtGWRIG

Chain	Residue	Details
B	GLY237-GLY250
A	GLY237-GLY250

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q56232","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Site: {"description":"Important for prephenate aminotransferase activity","evidences":[{"source":"PubMed","id":"30771275","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"Q56232","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---