Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RU6

1.8 Angstrom resolution crystal structure of orotidine 5'-phosphate decarboxylase (pyrF) from Campylobacter jejuni subsp. jejuni NCTC 11168

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004590	molecular_function	orotidine-5'-phosphate decarboxylase activity
A	0005829	cellular_component	cytosol
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0044205	biological_process	'de novo' UMP biosynthetic process
B	0004590	molecular_function	orotidine-5'-phosphate decarboxylase activity
B	0005829	cellular_component	cytosol
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0044205	biological_process	'de novo' UMP biosynthetic process
C	0004590	molecular_function	orotidine-5'-phosphate decarboxylase activity
C	0005829	cellular_component	cytosol
C	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
C	0006221	biological_process	pyrimidine nucleotide biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0044205	biological_process	'de novo' UMP biosynthetic process
D	0004590	molecular_function	orotidine-5'-phosphate decarboxylase activity
D	0005829	cellular_component	cytosol
D	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
D	0006221	biological_process	pyrimidine nucleotide biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0044205	biological_process	'de novo' UMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 280

Chain	Residue
A	LYS91
D	ASN123
D	HOH352

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 281

Chain	Residue
A	LEU59
D	LEU59

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 282

Chain	Residue
A	LYS103
A	ARG207

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 284

Chain	Residue
A	GLY175

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 285

Chain	Residue
A	THR117

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 286

Chain	Residue
A	ARG100
A	LYS103

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 287

Chain	Residue
A	PHE179

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 280

Chain	Residue
B	THR117

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 281

Chain	Residue
B	PHE179

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD B 282

Chain	Residue
B	ARG100
B	LYS103
B	ARG207

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 283

Chain	Residue
B	LEU59
C	LEU59

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 284

Chain	Residue
B	LYS103
B	ARG207

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 285

Chain	Residue
B	GLY175

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 286

Chain	Residue
B	ARG196

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD B 287

Chain	Residue
B	LYS12
B	LYS42
B	GLU46

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 280

Chain	Residue
B	ASN123
B	HOH292
C	LYS91

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 281

Chain	Residue
B	GLY90
B	LYS91
C	ASN123
C	SER126
C	HOH303

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD C 282

Chain	Residue
C	THR117
C	HOH366

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD C 283

Chain	Residue
C	GLY175

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD C 286

Chain	Residue
C	ARG100
C	LYS103

site_id	CC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD C 287

Chain	Residue
C	LYS12

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 280

Chain	Residue
D	ALA193
D	ARG196
D	LYS225

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD D 281

Chain	Residue
D	GLY175

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 282

Chain	Residue
D	ARG100
D	LYS103

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 283

Chain	Residue
D	ARG177
D	PHE179

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 284

Chain	Residue
D	LYS103
D	ARG177

site_id	CC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 285

Chain	Residue
D	THR117
D	HOH342

Functional Information from PROSITE/UniProt

site_id	PS00156
Number of Residues	14
Details	OMPDECASE Orotidine 5'-phosphate decarboxylase active site. IFlDlKfhDIPnTM

Chain	Residue	Details
A	ILE55-MET68

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01200","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01200","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)