7NF4

Structure of A. niger Fdc T395M R435P P438W variant (AnFdcII) in complex with prFMN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006744	biological_process	ubiquinone biosynthetic process
A	0008694	molecular_function	3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
A	0009074	biological_process	aromatic amino acid family catabolic process
A	0016831	molecular_function	carboxy-lyase activity
A	0018966	biological_process	styrene metabolic process
A	0030145	molecular_function	manganese ion binding
A	0033494	biological_process	ferulate metabolic process
A	0042802	molecular_function	identical protein binding
A	0046281	biological_process	cinnamic acid catabolic process
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006744	biological_process	ubiquinone biosynthetic process
B	0008694	molecular_function	3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
B	0009074	biological_process	aromatic amino acid family catabolic process
B	0016831	molecular_function	carboxy-lyase activity
B	0018966	biological_process	styrene metabolic process
B	0030145	molecular_function	manganese ion binding
B	0033494	biological_process	ferulate metabolic process
B	0042802	molecular_function	identical protein binding
B	0046281	biological_process	cinnamic acid catabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_03196, ECO:0000305\|PubMed:26083754

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_03196, ECO:0000269\|PubMed:26083754

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_03196