| IED ID | IndEnz0009000252 | 
| Enzyme Type ID | chitinase000252 | 
| Protein Name | 
                        
                            
                                Lectin/endochitinase 1  EC 3.2.1.14 Agglutinin UDA chia5.1.1 Cleaved into: Lectin 1  | 
                    
| Gene Name | UDA1 | 
| Organism | Urtica dioica (Great nettle) (Stinging nettle) | 
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Rosales Urticaceae Urtica Urtica dioica (Great nettle) (Stinging nettle) | 
| Enzyme Sequence | MMMRFLSAVVIMSSAMAVGLVSAQRCGSQGGGGTCPALWCCSIWGWCGDSEPYCGRTCENKCWSGERSDHRCGAAVGNPPCGQDRCCSVHGWCGGGNDYCSGSKCQYRCSSSVRGPRVALSGNSTANSIGNVVVTEPLFDQMFSHRKDCPSQGFYSYHSFLVAAESFPAFGTIGDVATRKREVAAFLAHISQATSGERSDVENPHAWGLCHINTTTVTENDFCTSSDWPCAAGKKYSPRGPIQLTHNFNYGLAGQAIGEDLIQNPDLVEKDPIISFKTALWFWMSQHDNKPSCHDIVLNANSAANRIPNKGVIGNIISRAFGHDDFAVRSSSIGFYKRYCDMLGVSYGHDLKYWFDNTPSSEFQRIQMRVAA | 
| Enzyme Length | 372 | 
| Uniprot Accession Number | P11218 | 
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 24; /note=Substrate; via amide nitrogen | 
| 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; | 
| DNA Binding | |
| EC Number | 3.2.1.14 | 
| Enzyme Function | FUNCTION: Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties. {ECO:0000269|PubMed:10873861}. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (6); Binding site (1); Chain (2); Disulfide bond (8); Domain (2); Glycosylation (1); Helix (7); Metal binding (2); Modified residue (1); Region (3); Sequence conflict (1); Signal peptide (1) | 
| Keywords | 3D-structure;Antimicrobial;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Fungicide;Glycoprotein;Glycosidase;Hydrolase;Lectin;Metal-binding;Plant defense;Polysaccharide degradation;Pyrrolidone carboxylic acid;Repeat;Signal;Zinc | 
| Interact With | Q75760 | 
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 24; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:1544484 | 
| Post Translational Modification | PTM: Proteolytically processed to yield a very small protein (8.5 kDa, 86 AA) containing only the two chitin-binding domains. | 
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:1544484 | 
| Structure 3D | X-ray crystallography (3) | 
| Cross Reference PDB | 1EN2; 1ENM; 1IQB; | 
| Mapped Pubmed ID | 23454641; | 
| Motif | |
| Gene Encoded By | |
| Mass | 40,542 | 
| Kinetics | |
| Metal Binding | METAL 70; /note=Zinc 1; shared with dimeric partner; METAL 90; /note=Zinc 2; shared with dimeric partner | 
| Rhea ID | |
| Cross Reference Brenda |