| IED ID | IndEnz0009000113 |
| Enzyme Type ID | chitinase000113 |
| Protein Name |
Acidic endochitinase SP2 EC 3.2.1.14 |
| Gene Name | SP2 |
| Organism | Beta vulgaris (Sugar beet) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae Caryophyllales Chenopodiaceae Betoideae Beta Beta vulgaris (Sugar beet) |
| Enzyme Sequence | MTLLLKNTLYLALIISVISSFPTSLFAQNCGCAPNLCCSNFGFCGTGTPYCGVGNCQSGPCEGGTPTTPTTPTTPTTPGTGGGGSSVSDIVSQAFFDGIIGQAAASCPGKNFYTRAAFLSAVDPKFGNEGSSDDNKREIAAFFAHISHETTNLCHIEERDGDVGDAYCDQDKAAQYPCAAGKKYYGRGPLQLSWNYNYALAGQAIGFDGLGNPEKVATDVNTSFKAAMWFWMTNVHSVMNQGFGATTKAINGALECNGQNQDQANDRIQFYKKYCADFGVAPGDNLTC |
| Enzyme Length | 288 |
| Uniprot Accession Number | P42820 |
| Absorption | |
| Active Site | ACT_SITE 149; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P29022 |
| Activity Regulation | |
| Binding Site | |
| 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: Defense against chitin-containing fungal pathogens. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (7); Domain (1); Modified residue (5); Region (4); Repeat (4); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Hydroxylation;Plant defense;Polysaccharide degradation;Pyrrolidone carboxylic acid;Repeat;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: By infection with Cercospora beticola. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | MOD_RES 28; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000305|PubMed:8018873; MOD_RES 66; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 69; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 72; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 75; /note=4-hydroxyproline; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: O-glycosylated on hydroxyprolines; contains xylose. |
| Signal Peptide | SIGNAL 1..27 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,417 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |