IED ID | IndEnz0009000217 |
Enzyme Type ID | chitinase000217 |
Protein Name |
Chitodextrinase EC 3.2.1.202 Endo-chitodextinase |
Gene Name | endo I |
Organism | Vibrio furnissii |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio furnissii |
Enzyme Sequence | MRLHRAKVSKSVFTLSTLTASCLMAFNSYAAVDCSALAEWQSDTIYTGGDQVQYNGSAYQANYWTQNNDPEQFSGDYAQWKLLDACTTDGGDDNQAPNATLTSPSASDVLTTGDVVTLAASASDNDGTIARVDFLVDGVVVAQASSAPYSATWTAVAGTHQISAIAYDDKALASTASQVSVSVTDSTQPGNEAPTVDITLSASQVDVGDVVTLTANAADADGSVDKVDFYVAGSLVGTVASTPYTLDYTTTRSGRWLCLRARLITSARQRIRPRRRLTVAAGPWSVPVVLMVCIKPKGQCAVLYGVREDGREKMGADHPRRVIGYFTSWRAGDDDQTAYLVKDIPWEQLTHINYAFVSIGSDGKVNVGDVNDANNAAVGKEWDGVEIDPTLGFKGHFGALATYKQKYGVKTLISIGGWAETGGHFDNDGNRVADGGFYTMTTNADGSINQQGIETFADSAVEMMRKYRFDGLDIDLRISNIDGGTGNPDDTAFSESRRAYLMNSYHELMRVLREKLDVASAQDGVHYMLTIAAPSSAYLLRGMETMAVTQYLDYVNIMSYDLHGAWNDHVGHNAALYDTGKDSELAQWNVYGTAQYGGIGYLNTDWAFHYFRGSMPAGRINIGVPYYTRGWQGVTGGDNGLWGARLAKSKRVSNRYGEGEKNNCGYGATGLDNMWHDVNAAGDEMGAGSNPMWHAKNLEHGIWGSYLAVYGLDPTTAPLVGTYARNYDSVAIAPWLWNAEKKVFLSTEDKQSIDVKADYVIDKEIGGIMFWELAGDYNCYVLDANGQRTSIDSTEQACESGQGEYHMGNTMTKAIYDKFKAATPYGNTVATGAVPSETVDIAVSIGGFKVGDQNYPINPKVTFTNNTGVDIPGGTAFQFDIPVSAPDNAKDQSGGGLSVIASGHTRADNIGGLDGTMHRVAFSLPAWKTLPAGDTYELDMVYYLPISGPANYSVNINGVDYAFKFEQPDLPLADLSSGNGGGTGGGDTGGGTTEPGDVVEWVPGSTQVSDGTTVTYNGKCFVAQNSPGVWESPTQTNWFWEEVTCP |
Enzyme Length | 1046 |
Uniprot Accession Number | P96156 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by (GlcNAc)4, (GlcNAc)5, (GlcNAc)6, and PNP-(GlcNAc)3. {ECO:0000269|PubMed:8969204}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of chitodextrins, releasing N,N'-diacetylchitobiose and small amounts of N,N',N''-triacetylchitotriose.; EC=3.2.1.202; Evidence={ECO:0000269|PubMed:8969204}; |
DNA Binding | |
EC Number | 3.2.1.202 |
Enzyme Function | FUNCTION: Hydrolyzes chitin oligosaccharides; (GlcNAc)4 to (GlcNAc)2 and (GlcNAc)5,6 to (GlcNAc)2 and (GlcNAc)3. Inactive towards chitin, glucosamine oligosaccharides, glycoproteins and glycopeptides containing (GlcNAc)2. {ECO:0000269|PubMed:8969204}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-37 degrees Celsius. {ECO:0000269|PubMed:8969204}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:8969204}; |
Pathway | PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305|PubMed:8969204}. |
nucleotide Binding | |
Features | Chain (1); Domain (1); Region (1); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Chitin degradation;Direct protein sequencing;Glycosidase;Hydrolase;Periplasm;Polysaccharide degradation;Signal |
Interact With | |
Induction | INDUCTION: By (GlcNAc)2. {ECO:0000269|PubMed:8969204}. |
Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:8969204}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000269|PubMed:8969204 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 112,380 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.202; |