##gff-version 3
P21631	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000150372;Note=Uroporphyrinogen-III C-methyltransferase	
P21631	UniProtKB	Binding site	24	24	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15522295,ECO:0007744|PDB:1S4D;Dbxref=PMID:15522295	
P21631	UniProtKB	Binding site	100	102	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15522295,ECO:0007744|PDB:1S4D;Dbxref=PMID:15522295	
P21631	UniProtKB	Binding site	130	131	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15522295,ECO:0007744|PDB:1S4D;Dbxref=PMID:15522295	
P21631	UniProtKB	Binding site	184	184	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15522295,ECO:0007744|PDB:1S4D;Dbxref=PMID:15522295	
P21631	UniProtKB	Binding site	213	213	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15522295,ECO:0007744|PDB:1S4D;Dbxref=PMID:15522295	
P21631	UniProtKB	Binding site	241	241	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15522295,ECO:0007744|PDB:1S4D;Dbxref=PMID:15522295	
P21631	UniProtKB	Mutagenesis	47	47	.	.	.	Note=Reduces S-adenosyl-L-methionine binding by about 75%25. Causes accumulation of precorrin-1. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522295;Dbxref=PMID:15522295	
P21631	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Reduces S-adenosyl-L-methionine binding by about 50%25. Causes slow synthesis of precorrin-2 and accumulation of precorrin-1. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522295;Dbxref=PMID:15522295	
P21631	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522295;Dbxref=PMID:15522295	
P21631	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Strongly reduces S-adenosyl-L-methionine binding. Causes slow synthesis of precorrin-2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522295;Dbxref=PMID:15522295	
P21631	UniProtKB	Mutagenesis	183	183	.	.	.	Note=Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522295;Dbxref=PMID:15522295	
P21631	UniProtKB	Mutagenesis	184	184	.	.	.	Note=Strongly reduces S-adenosyl-L-methionine binding. Causes drastic effects on enzyme activity. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522295;Dbxref=PMID:15522295	
P21631	UniProtKB	Beta strand	17	21	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	23	25	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	32	40	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	42	46	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	54	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	78	90	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	95	101	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	105	108	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	109	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Turn	118	120	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	123	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Turn	131	133	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	134	138	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	150	156	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	170	174	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	178	184	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	189	198	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	206	212	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	219	224	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Turn	225	227	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	228	235	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Beta strand	239	246	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	247	251	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	252	255	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D	
P21631	UniProtKB	Helix	257	261	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S4D