##gff-version 3
P77555	UniProtKB	Chain	1	349	.	.	.	ID=PRO_0000083822;Note=Ureidoglycolate dehydrogenase (NAD(+))	
P77555	UniProtKB	Active site	116	116	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Binding site	140	140	.	.	.	Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:23284870,ECO:0007744|PDB:4H8A;Dbxref=PMID:23284870	
P77555	UniProtKB	Binding site	174	176	.	.	.	Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:23284870,ECO:0007744|PDB:4H8A;Dbxref=PMID:23284870	
P77555	UniProtKB	Binding site	224	224	.	.	.	Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:23284870,ECO:0007744|PDB:4H8A;Dbxref=PMID:23284870	
P77555	UniProtKB	Binding site	306	308	.	.	.	Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:23284870,ECO:0007744|PDB:4H8A;Dbxref=PMID:23284870	
P77555	UniProtKB	Site	48	48	.	.	.	Note=Plays a crucial role in stabilizing the binding of (S)-ureidoglycolate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	43	43	.	.	.	Note=4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate%2C respectively. Strong decrease of the catalytic efficiency. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	44	44	.	.	.	Note=16-fold decrease of the affinity for (S)-ureidoglycolate%2C but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Loss of dehydrogenase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	52	52	.	.	.	Note=2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate%2C respectively. Strong decrease of the catalytic efficiency. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Loss of dehydrogenase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	140	140	.	.	.	Note=2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate%2C respectively. Strong decrease of the catalytic efficiency. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	141	141	.	.	.	Note=5-fold decrease of the affinity for (S)-ureidoglycolate%2C but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	141	141	.	.	.	Note=14-fold decrease of the affinity for (S)-ureidoglycolate%2C but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	141	141	.	.	.	Note=6-fold decrease of the affinity for (S)-ureidoglycolate%2C but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	251	251	.	.	.	Note=2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate%2C respectively. Slight decrease of the catalytic efficiency. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Mutagenesis	259	259	.	.	.	Note=2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate%2C respectively. Slight decrease of the catalytic efficiency. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23284870;Dbxref=PMID:23284870	
P77555	UniProtKB	Helix	5	19	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	23	39	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	42	44	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	46	48	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	49	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	76	80	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	86	104	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	105	114	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	121	129	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	132	138	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	149	151	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	159	164	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	170	175	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	177	180	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	182	191	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	199	201	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Turn	211	213	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XRH	
P77555	UniProtKB	Turn	220	222	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	223	236	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	245	247	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Turn	251	253	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XRH	
P77555	UniProtKB	Beta strand	261	268	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	270	272	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	276	291	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Helix	307	319	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A	
P77555	UniProtKB	Beta strand	321	323	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XRH	
P77555	UniProtKB	Helix	325	331	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8A