##gff-version 3
P04175	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3099837;Dbxref=PMID:3099837	
P04175	UniProtKB	Chain	2	678	.	.	.	ID=PRO_0000167598;Note=NADPH--cytochrome P450 reductase	
P04175	UniProtKB	Topological domain	2	22	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Transmembrane	23	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Topological domain	44	678	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Domain	80	224	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Domain	279	521	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	86	91	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	138	141	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	173	182	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	208	208	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	298	298	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	424	424	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	454	457	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	472	474	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	478	478	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	488	491	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	535	535	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	596	597	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	602	606	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	639	639	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Binding site	677	677	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
P04175	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylglycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3099837;Dbxref=PMID:3099837	
P04175	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16435	
P04175	UniProtKB	Sequence conflict	55	55	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	164	164	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	175	175	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	340	340	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	379	379	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	401	401	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	447	447	.	.	.	Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	503	503	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	509	509	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P04175	UniProtKB	Sequence conflict	675	675	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305