Detail Information for IndEnz0009000252
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