##gff-version 3
P32173	UniProtKB	Chain	1	194	.	.	.	ID=PRO_0000134887;Note=Molybdenum cofactor guanylyltransferase	
P32173	UniProtKB	Binding site	12	14	.	.	.	.	
P32173	UniProtKB	Binding site	25	25	.	.	.	.	
P32173	UniProtKB	Binding site	53	53	.	.	.	.	
P32173	UniProtKB	Binding site	71	71	.	.	.	.	
P32173	UniProtKB	Binding site	101	101	.	.	.	.	
P32173	UniProtKB	Binding site	101	101	.	.	.	.	
P32173	UniProtKB	Mutagenesis	12	14	.	.	.	Note=7.5-fold decrease in affinity for GTP and nearly no effect on catalytic activity. Displays a 3-fold decrease in activity with GTP and gains a low activity with CTP as substrate%3B when associated with 79-LLTS-82. LAG->TAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21081498;Dbxref=PMID:21081498	
P32173	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Complete loss of catalytic activity. Still capable of binding MPT and MGD and interacting with both MoeA and MobB. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Slight reduction in catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Nearly no effect on catalytic activity. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Nearly no effect on catalytic activity. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	79	82	.	.	.	Note=11-fold decrease in affinity for GTP and nearly no effect on catalytic activity. Displays a 3-fold decrease in activity with GTP and gains a low activity with CTP as substrate%3B when associated with 12-TAA-14. PLAG->LLTS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21081498;Dbxref=PMID:21081498	
P32173	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Slight reduction in catalytic activity. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Complete loss of catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Nearly no effect on catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	180	180	.	.	.	Note=Nearly no effect on catalytic activity. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Nearly no effect on catalytic activity. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12719427;Dbxref=PMID:12719427	
P32173	UniProtKB	Helix	3	5	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FR9	
P32173	UniProtKB	Beta strand	6	12	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	18	20	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Helix	25	27	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Helix	35	46	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Helix	58	62	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FR9	
P32173	UniProtKB	Helix	79	89	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	92	99	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Helix	109	115	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Turn	116	119	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FR9	
P32173	UniProtKB	Beta strand	121	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	131	139	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Helix	142	151	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Helix	157	163	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Beta strand	167	170	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Turn	175	178	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K	
P32173	UniProtKB	Helix	184	188	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E5K