MF7000763 Catechol 1,2-dioxygenase with 4-methylcatechol (Acinetobacter sp. ADP1) 1dmh X-ray 1.70 Homodimer Acinetobacter baylyi 10801478 Vetting MW, Ohlendorf DH Structure 2000 4 8 429-40 GO:0018576 catechol 1,2-dioxygenase activity GO:0008199 ferric iron binding GO:0042952 beta-ketoadipate pathway GO:0019614 catechol-containing compound catabolic process 2 1 Homooligomeric enzymes Homodimeric enzymes All chains according to the most probable oligomerization state stored in PDBe were considered. A Catechol 1,2-dioxygenase Acinetobacter baylyi P07773 3 311 99% MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV 311 secondary structure helix 8 19 secondary structure helix 27 48 secondary structure helix 51 68 secondary structure helix 70 78 secondary structure helix 79 95 secondary structure helix 206 215 secondary structure helix 270 277 secondary structure strand 111 112 secondary structure strand 116 118 secondary structure strand 120 122 secondary structure strand 133 141 secondary structure strand 152 156 secondary structure strand 179 183 secondary structure strand 189 195 secondary structure strand 200 201 secondary structure strand 220 221 secondary structure strand 224 230 secondary structure strand 237 243 secondary structure strand 262 263 secondary structure strand 266 268 secondary structure strand 283 287 secondary structure strand 290 291 secondary structure strand 309 310 pfam PF04444 Catechol dioxygenase N terminus 27 94 B Catechol 1,2-dioxygenase Acinetobacter baylyi P07773 3 311 99% MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV 311 secondary structure helix 8 19 secondary structure helix 27 48 secondary structure helix 51 68 secondary structure helix 70 78 secondary structure helix 79 95 secondary structure helix 206 215 secondary structure helix 270 277 secondary structure strand 111 112 secondary structure strand 116 118 secondary structure strand 120 122 secondary structure strand 133 141 secondary structure strand 152 156 secondary structure strand 179 183 secondary structure strand 189 195 secondary structure strand 224 230 secondary structure strand 237 243 secondary structure strand 262 263 secondary structure strand 266 268 secondary structure strand 283 287 secondary structure strand 290 291 secondary structure strand 309 310 pfam PF04444 Catechol dioxygenase N terminus 27 94 Indirect evidence Only some parts of the structure participates in mutual synergistic folding. Dioxygenase A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). A N/A B N/A MF7000760 MF7000761 MF7000762 MF7000763 MF7000764 MF7000765 MF7000766 MF7000767 MF7000768 MF7000769 MF7000770 MF7000771