4MB8

Evolutionary history and metabolic insights of ancient mammalian uricases

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004846	molecular_function	urate oxidase activity
A	0005777	cellular_component	peroxisome
A	0006144	biological_process	purine nucleobase metabolic process
A	0006145	biological_process	purine nucleobase catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0019628	biological_process	urate catabolic process
B	0004846	molecular_function	urate oxidase activity
B	0005777	cellular_component	peroxisome
B	0006144	biological_process	purine nucleobase metabolic process
B	0006145	biological_process	purine nucleobase catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0019628	biological_process	urate catabolic process
C	0004846	molecular_function	urate oxidase activity
C	0005777	cellular_component	peroxisome
C	0006144	biological_process	purine nucleobase metabolic process
C	0006145	biological_process	purine nucleobase catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0019628	biological_process	urate catabolic process
D	0004846	molecular_function	urate oxidase activity
D	0005777	cellular_component	peroxisome
D	0006144	biological_process	purine nucleobase metabolic process
D	0006145	biological_process	purine nucleobase catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0019628	biological_process	urate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT B 401

Chain	Residue
A	SER46
A	GLN109
B	LYS291

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT D 401

Chain	Residue
C	THR68
D	PHE170
D	ARG187
D	HOH555

---

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACT D 402

Chain	Residue
D	LYS291

---

Functional Information from PROSITE/UniProt

site_id	PS00366
Number of Residues	28
Details	URICASE Uricase signature. LkVLKTTqSgFegFikdqFttLpevkdR

Chain	Residue	Details
A	LEU160-ARG187

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:D0VWQ1

Chain	Residue	Details
A	LYS23
A	THR68
A	HIS264
B	LYS23
B	THR68
B	HIS264
C	LYS23
C	THR68
C	HIS264
D	LYS23
D	THR68
D	HIS264

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q00511

Chain	Residue	Details
C	PHE170
C	ARG187
C	VAL235
C	GLN236
C	ASN262
D	THR68
D	ASP69
D	PHE170
D	ARG187
D	VAL235
D	GLN236
D	ASN262
B	THR68
B	PHE170
B	ARG187
B	VAL235
B	GLN236
B	ASN262
C	THR68
C	ASP69
B	ASP69
A	THR68
A	ASP69
A	PHE170
A	ARG187
A	VAL235
A	GLN236
A	ASN262

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P25688

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P25688

Chain	Residue	Details
A	LYS10
A	LYS23
A	LYS221
A	LYS228
B	LYS10
B	LYS23
B	LYS221
B	LYS228
C	LYS10
C	LYS23
C	LYS221
C	LYS228
D	LYS10
D	LYS23
D	LYS221
D	LYS228

---

site_id	SWS_FT_FI5
Number of Residues	32
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P25688

Chain	Residue	Details
A	LYS27
A	LYS36
A	LYS118
A	LYS122
A	LYS164
A	LYS175
A	LYS185
A	LYS278
B	LYS27
B	LYS36
B	LYS118
B	LYS122
B	LYS164
B	LYS175
B	LYS185
B	LYS278
C	LYS27
C	LYS36
C	LYS118
C	LYS122
C	LYS164
C	LYS175
C	LYS185
C	LYS278
D	LYS27
D	LYS36
D	LYS118
D	LYS122
D	LYS164
D	LYS175
D	LYS185
D	LYS278

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P25688

Chain	Residue	Details
A	SER39
A	SER63
A	SER232
B	SER39
B	SER63
B	SER232
C	SER39
C	SER63
C	SER232
D	SER39
D	SER63
D	SER232

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P25688

Chain	Residue	Details
A	TYR289
B	TYR289
C	TYR289
D	TYR289

---