IED ID | IndEnz0009000010 |
Enzyme Type ID | chitinase000010 |
Protein Name |
Endochitinase B1 EC 3.2.1.14 Chitinase B1 |
Gene Name | chiB1 |
Organism | Neosartorya fumigata (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) |
Enzyme Sequence | MRFATSTIVKVALLLSSLCVDAAVMWNRDTSSTDLEARASSGYRSVVYFVNWAIYGRNHNPQDLPVERLTHVLYAFANVRPETGEVYMTDSWADIEKHYPGDSWSDTGNNVYGCIKQLYLLKKQNRNLKVLLSIGGWTYSPNFAPAASTDAGRKNFAKTAVKLLQDLGFDGLDIDWEYPENDQQANDFVLLLKEVRTALDSYSAANAGGQHFLLTVASPAGPDKIKVLHLKDMDQQLDFWNLMAYDYAGSFSSLSGHQANVYNDTSNPLSTPFNTQTALDLYRAGGVPANKIVLGMPLYGRSFANTDGPGKPYNGVGQGSWENGVWDYKALPQAGATEHVLPDIMASYSYDATNKFLISYDNPQVANLKSGYIKSLGLGGAMWWDSSSDKTGSDSLITTVVNALGGTGVFEQSQNELDYPVSQYDNLRNGMQT |
Enzyme Length | 433 |
Uniprot Accession Number | Q873X9 |
Absorption | |
Active Site | ACT_SITE 177; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
Activity Regulation | ACTIVITY REGULATION: Methylxanthine drugs surch as theophylline, caffeine and pentoxifylline, as well as the two cyclic peptide natural products argifin and argadin, act as specific inhibitors. {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:16183021, ECO:0000269|PubMed:16844689, ECO:0000269|PubMed:18355729}. |
Binding Site | BINDING 52; /note="Caffeine; inhibitor"; /evidence="ECO:0000269|PubMed:16183021, ECO:0007744|PDB:2A3B"; BINDING 137; /note="Caffeine; inhibitor"; /evidence="ECO:0000269|PubMed:16183021, ECO:0007744|PDB:2A3B"; BINDING 178; /note="Chitooligosaccharide"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"; BINDING 245; /note="Caffeine; inhibitor"; /evidence="ECO:0000269|PubMed:16183021, ECO:0007744|PDB:2A3B"; BINDING 251; /note="Caffeine; inhibitor"; /evidence="ECO:0000269|PubMed:16183021, ECO:0007744|PDB:2A3B"; BINDING 384; /note="Caffeine; inhibitor"; /evidence="ECO:0000269|PubMed:16183021, ECO:0007744|PDB:2A3B"; BINDING 384; /note="Chitooligosaccharide"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:14523125, ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:16096835, ECO:0000269|PubMed:16183021, ECO:0000269|PubMed:18975073}; |
DNA Binding | |
EC Number | 3.2.1.14 |
Enzyme Function | FUNCTION: Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity). {ECO:0000250}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:18975073}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-7.0. {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:18975073}; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (17); Binding site (7); Chain (1); Domain (1); Glycosylation (1); Helix (22); Mutagenesis (11); Region (3); Signal peptide (1); Turn (3) |
Keywords | 3D-structure;Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal |
Interact With | |
Induction | INDUCTION: Induced during batch culture. {ECO:0000269|PubMed:16096835}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14523125, ECO:0000269|PubMed:16096835}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (14) |
Cross Reference PDB | 1W9P; 1W9U; 1W9V; 1WNO; 2A3A; 2A3B; 2A3C; 2A3E; 2IUZ; 3CH9; 3CHC; 3CHD; 3CHE; 3CHF; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 47,622 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19.9 uM for 4-methylumbelliferyl beta-D-N,N'-diacetylchitobiose {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:18975073}; KM=2.94 mg/ml for chitosan {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:18975073}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |