##gff-version 3 P49424 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00303,ECO:0000305|PubMed:8973192;Dbxref=PMID:8973192 P49424 UniProtKB Chain 28 423 . . . ID=PRO_0000012173;Note=Mannan endo-1%2C4-beta-mannosidase P49424 UniProtKB Domain 56 409 . . . Note=GH26;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01100 P49424 UniProtKB Active site 212 212 . . . Note=Proton donor;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12203498,ECO:0000305|PubMed:12841226,ECO:0000305|PubMed:19441796,ECO:0000305|PubMed:8973192;Dbxref=PMID:12203498,PMID:12841226,PMID:19441796,PMID:8973192 P49424 UniProtKB Active site 320 320 . . . Note=Nucleophile;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12203498,ECO:0000305|PubMed:8973192;Dbxref=PMID:12203498,PMID:8973192 P49424 UniProtKB Binding site 121 121 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12203498,ECO:0000269|PubMed:12841226;Dbxref=PMID:12203498,PMID:12841226 P49424 UniProtKB Binding site 143 143 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12203498,ECO:0000269|PubMed:12841226,ECO:0000269|PubMed:19441796;Dbxref=PMID:12203498,PMID:12841226,PMID:19441796 P49424 UniProtKB Binding site 162 162 . . . Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:12203498,ECO:0000305|PubMed:11382747;Dbxref=PMID:11382747,PMID:12203498 P49424 UniProtKB Binding site 217 217 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Binding site 285 285 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12841226,ECO:0000269|PubMed:19441796;Dbxref=PMID:12841226,PMID:19441796 P49424 UniProtKB Binding site 360 361 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12203498,ECO:0000269|PubMed:12841226,ECO:0000269|PubMed:19441796;Dbxref=PMID:12203498,PMID:12841226,PMID:19441796 P49424 UniProtKB Binding site 377 377 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12203498,ECO:0000269|PubMed:12841226,ECO:0000269|PubMed:19441796;Dbxref=PMID:12203498,PMID:12841226,PMID:19441796 P49424 UniProtKB Site 211 211 . . . Note=Plays an important role in maintaining the position of the catalytic nucleophile;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11382747,ECO:0000305|PubMed:12203498;Dbxref=PMID:11382747,PMID:12203498 P49424 UniProtKB Mutagenesis 121 121 . . . Note=Strong decrease of mannanase activity against both oligosaccharides and polysaccharides. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19441796;Dbxref=PMID:19441796 P49424 UniProtKB Mutagenesis 143 143 . . . Note=Very low mannanase activity against both mannans and mannooligosaccharides. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Mutagenesis 156 156 . . . Note=Similar to the wild-type. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Mutagenesis 162 162 . . . Note=The mannanase activity is 95%2C 70%2C and 30-fold less active than the wild-type against mannotriose%2C mannotetraose and mannohexaose%2C respectively. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Mutagenesis 211 211 . . . Note=Causes a 100- and 700-fold decrease in mannanase activity against carob galactomannans and mannotetraose%2C respectively%2C but only a 6-fold reduction in mannanase activity against 2%2C4-DNPM. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Mutagenesis 212 212 . . . Note=Causes a dramatic decrease in the catalytic efficiency against carob galactomannan%2C azo-carob galactomannan%2C mannotetraose and 2%2C4-DNPM. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11382747,ECO:0000269|PubMed:8973192;Dbxref=PMID:11382747,PMID:8973192 P49424 UniProtKB Mutagenesis 212 212 . . . Note=10-fold decrease of the catalytic efficiency against 2%2C4-DNPM. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8973192;Dbxref=PMID:8973192 P49424 UniProtKB Mutagenesis 217 217 . . . Note=Lack of mannanase activity against both mannotriose and mannotetraose. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Mutagenesis 278 278 . . . Note=Retains significant activity against mannotetraose and azo-carob galactomannan. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8973192;Dbxref=PMID:8973192 P49424 UniProtKB Mutagenesis 278 278 . . . Note=Retains significant activity against mannotetraose and azo-carob galactomannan. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8973192;Dbxref=PMID:8973192 P49424 UniProtKB Mutagenesis 283 283 . . . Note=Retains significant activity against mannotetraose and azo-carob galactomannan. Lack of activity against all substrates%3B when associated with A-320. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11382747,ECO:0000269|PubMed:8973192;Dbxref=PMID:11382747,PMID:8973192 P49424 UniProtKB Mutagenesis 283 283 . . . Note=Retains significant activity against mannotetraose and azo-carob galactomannan. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8973192;Dbxref=PMID:8973192 P49424 UniProtKB Mutagenesis 285 285 . . . Note=Reduction of the catalytic efficiency with carob galactomannan and 2%2C4-DNPM. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Mutagenesis 320 320 . . . Note=Does not alter the affinity against carob galactomannan%2C azo-carob galactomannan%2C mannotetraose and 2%2C4-DNPM. Lack of activity against all substrates%3B when associated with A-283. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11382747,ECO:0000269|PubMed:8973192;Dbxref=PMID:11382747,PMID:8973192 P49424 UniProtKB Mutagenesis 320 320 . . . Note=Causes a dramatic decrease in the catalytic efficiency against mannotetraose. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8973192;Dbxref=PMID:8973192 P49424 UniProtKB Mutagenesis 320 320 . . . Note=Lack of activity against all substrates. E->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12841226,ECO:0000269|PubMed:19441796;Dbxref=PMID:12841226,PMID:19441796 P49424 UniProtKB Mutagenesis 360 360 . . . Note=Lack of activity against all substrates. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382747;Dbxref=PMID:11382747 P49424 UniProtKB Mutagenesis 361 361 . . . Note=Strong decrease of mannanase activity against oligosaccharides%2C while the reduction in the rate of polysaccharide hydrolysis is more modest. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units%3B when associated with A-377. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19441796;Dbxref=PMID:19441796 P49424 UniProtKB Mutagenesis 377 377 . . . Note=100-fold decrease in the activity of the mannanase against mannotetraose and 4-nitrophenyl-beta-D-Man2. It hydrolyzes polysaccharides only 10-20-fold less efficiently than the wild-type. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units%3B when associated with A-361. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19441796;Dbxref=PMID:19441796 P49424 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WHM P49424 UniProtKB Helix 56 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 73 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Turn 79 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 96 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 106 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 125 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 137 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Turn 147 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Turn 156 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 178 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WHM P49424 UniProtKB Helix 227 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 249 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 264 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Turn 274 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 283 286 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 288 290 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 292 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 320 323 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 325 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 337 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 351 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 355 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 385 389 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 392 401 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Helix 408 410 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ODZ P49424 UniProtKB Beta strand 419 421 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WHM