##gff-version 3
P0AEA8	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000150378;Note=Siroheme synthase	
P0AEA8	UniProtKB	Region	4	204	.	.	.	Note=Precorrin-2 dehydrogenase /sirohydrochlorin ferrochelatase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P0AEA8	UniProtKB	Region	216	448	.	.	.	Note=Uroporphyrinogen-III C-methyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Active site	248	248	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Active site	270	270	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	22	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	43	44	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	225	225	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	301	303	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	306	306	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	331	332	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	382	382	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Binding site	411	411	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Modified residue	128	128	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01646	
P0AEA8	UniProtKB	Mutagenesis	21	21	.	.	.	Note=It has methyltransferase and ferrochelatase activities but a greatly reduced dehydrogenase activity. It is able to bind AdoMet. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461500;Dbxref=PMID:9461500	
P0AEA8	UniProtKB	Mutagenesis	224	224	.	.	.	Note=It abolishes methyltransferase activity%2C but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461500;Dbxref=PMID:9461500	
P0AEA8	UniProtKB	Mutagenesis	227	227	.	.	.	Note=It has all activities of CysG. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461500;Dbxref=PMID:9461500	
P0AEA8	UniProtKB	Mutagenesis	248	248	.	.	.	Note=It abolishes methyltransferase activity%2C but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet. D->A	
P0AEA8	UniProtKB	Mutagenesis	270	270	.	.	.	Note=It has all activities of CysG. It is able to bind AdoMet. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461500;Dbxref=PMID:9461500	
P0AEA8	UniProtKB	Mutagenesis	298	298	.	.	.	Note=It abolishes methyltransferase activity%2C but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461500;Dbxref=PMID:9461500	
P0AEA8	UniProtKB	Mutagenesis	303	303	.	.	.	Note=It has all activities of CysG. It is able to bind AdoMet. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461500;Dbxref=PMID:9461500	
P0AEA8	UniProtKB	Mutagenesis	309	309	.	.	.	Note=It abolishes methyltransferase activity%2C but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461500;Dbxref=PMID:9461500	
P0AEA8	UniProtKB	Sequence conflict	26	26	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P0AEA8	UniProtKB	Sequence conflict	90	91	.	.	.	Note=SE->RQ;Ontology_term=ECO:0000305;evidence=ECO:0000305