MF7001002 Ureidoglycolate hydrolase (AllA) (Escherichia coli O157:H7) 1yqc X-ray 1.71 Homodimer Escherichia coli O157:H7 16114032 Raymond S, Tocilj A, Ajamian E, Li Y, Hung MN, Matte A, Cygler M Proteins 2005 2 61 454-9 GO:0004848 ureidoglycolate hydrolase activity GO:0050385 ureidoglycolate lyase activity GO:0000256 allantoin catabolic process GO:0006145 purine nucleobase catabolic process 2 1 Homooligomeric enzymes Homodimeric enzymes All chains according to the most probable oligomerization state stored in PDBe were considered. A Ureidoglycolate lyase Escherichia coli O157:H7 P63486 1 160 100% MKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDRTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA 160 secondary structure helix 9 14 secondary structure helix 48 51 secondary structure strand 2 7 secondary structure strand 17 20 secondary structure strand 27 30 secondary structure strand 35 43 secondary structure strand 53 59 secondary structure strand 67 73 secondary structure strand 79 83 secondary structure strand 90 94 secondary structure strand 106 109 secondary structure strand 115 118 secondary structure strand 123 124 secondary structure strand 134 140 secondary structure strand 148 158 pfam PF04115 Ureidoglycolate lyase 2 154 B Ureidoglycolate lyase Escherichia coli O157:H7 P63486 1 160 100% MKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDRTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA 160 secondary structure helix 9 14 secondary structure helix 101 105 secondary structure strand 2 7 secondary structure strand 17 20 secondary structure strand 27 30 secondary structure strand 35 43 secondary structure strand 53 59 secondary structure strand 67 73 secondary structure strand 79 83 secondary structure strand 90 94 secondary structure strand 106 109 secondary structure strand 115 118 secondary structure strand 123 124 secondary structure strand 134 140 secondary structure strand 148 158 pfam PF04115 Ureidoglycolate lyase 2 154 Indirect evidence The full structure participates in mutual synergistic folding. - Domain-swapped dimer with beta sheet augmentation and an extensive interface. Face-to-face interactions of 5-stranded b-sheets of the two monomers. Both monomers contribute to the putative active site (PMID:16114032). A N/A B N/A