2JJ4

The complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC7942

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003991	molecular_function	acetylglutamate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	L-arginine biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0042450	biological_process	L-arginine biosynthetic process via ornithine
A	0042802	molecular_function	identical protein binding
B	0000166	molecular_function	nucleotide binding
B	0003991	molecular_function	acetylglutamate kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	L-arginine biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0042450	biological_process	L-arginine biosynthetic process via ornithine
B	0042802	molecular_function	identical protein binding
C	0000166	molecular_function	nucleotide binding
C	0003991	molecular_function	acetylglutamate kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	L-arginine biosynthetic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0042450	biological_process	L-arginine biosynthetic process via ornithine
C	0042802	molecular_function	identical protein binding
D	0000166	molecular_function	nucleotide binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0006808	biological_process	regulation of nitrogen utilization
D	0030234	molecular_function	enzyme regulator activity
D	0042802	molecular_function	identical protein binding
E	0000166	molecular_function	nucleotide binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005829	cellular_component	cytosol
E	0006808	biological_process	regulation of nitrogen utilization
E	0030234	molecular_function	enzyme regulator activity
E	0042802	molecular_function	identical protein binding
F	0000166	molecular_function	nucleotide binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005829	cellular_component	cytosol
F	0006808	biological_process	regulation of nitrogen utilization
F	0030234	molecular_function	enzyme regulator activity
F	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NLG A 1292

Chain	Residue
A	GLY69
A	GLY70
A	GLY71
A	ILE74
A	LEU91
A	ARG92
A	SER174
A	ASN185
A	ALA188

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NLG B 1292

Chain	Residue
B	GLY69
B	GLY70
B	GLY71
B	ILE74
B	GLY90
B	LEU91
B	ARG92
B	ASN185
B	ALA188

---

Functional Information from PROSITE/UniProt

site_id	PS00496
Number of Residues	6
Details	PII_GLNB_UMP P-II protein uridylation site. YRGSEY

Chain	Residue	Details
D	TYR46-TYR51

---

site_id	PS00638
Number of Residues	14
Details	PII_GLNB_CTER P-II protein C-terminal region signature. TgeiGDGKIFVspV

Chain	Residue	Details
D	THR83-VAL96

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7592328","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"O-UMP-tyrosine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00675","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
A	GLY38
A	LYS35
A	LYS248
A	GLY71

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
B	GLY38
B	LYS35
B	LYS248
B	GLY71

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
C	GLY38
C	LYS35
C	LYS248
C	GLY71

---