1ULI

Biphenyl dioxygenase (BphA1A2) derived from Rhodococcus sp. strain RHA1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0016491	molecular_function	oxidoreductase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0005515	molecular_function	protein binding
B	0016491	molecular_function	oxidoreductase activity
B	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
B	0019380	biological_process	3-phenylpropionate catabolic process
B	0051213	molecular_function	dioxygenase activity
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0016491	molecular_function	oxidoreductase activity
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0005515	molecular_function	protein binding
D	0016491	molecular_function	oxidoreductase activity
D	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
D	0019380	biological_process	3-phenylpropionate catabolic process
D	0051213	molecular_function	dioxygenase activity
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0005515	molecular_function	protein binding
E	0016491	molecular_function	oxidoreductase activity
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
E	0046872	molecular_function	metal ion binding
E	0051213	molecular_function	dioxygenase activity
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0005515	molecular_function	protein binding
F	0016491	molecular_function	oxidoreductase activity
F	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
F	0019380	biological_process	3-phenylpropionate catabolic process
F	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 A 600

Chain	Residue
A	GLN217
A	HIS224
A	HIS230
A	ASP378
A	HOH770

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 C 600

Chain	Residue
C	HOH755
C	GLN217
C	HIS224
C	HIS230
C	ASP378

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 E 600

Chain	Residue
E	GLN217
E	HIS224
E	HIS230
E	ASP378
E	HOH771

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE2 B 700

Chain	Residue
B	HIS24
B	HOH741
B	HOH743
D	HIS24
D	HOH234
F	HIS24

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A 500

Chain	Residue
A	CYS98
A	HIS100
A	ARG101
A	CYS118
A	HIS121
A	TRP123

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES C 500

Chain	Residue
C	CYS98
C	HIS100
C	ARG101
C	MET103
C	CYS118
C	HIS121
C	TRP123

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES E 500

Chain	Residue
E	CYS98
E	HIS100
E	ARG101
E	CYS118
E	HIS121
E	TRP123

---

Functional Information from PROSITE/UniProt

site_id	PS00570
Number of Residues	24
Details	RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricradgGNaksftCsYH

Chain	Residue	Details
A	CYS98-HIS121

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	327
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	21
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15342255","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ULI","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1ULJ","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	39
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15342255","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
A	HIS121
C	ASP221
C	HIS224

---

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

Chain	Residue	Details
C	HIS121
E	ASP221
E	HIS224

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
A	ASP221
A	HIS224
E	HIS121

---