ID CHIB_PEA Reviewed; 23 AA. AC P21227; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 24-JAN-2024, entry version 89. DE RecName: Full=Endochitinase B; DE EC=3.2.1.14; DE Flags: Fragment; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=cv. Birte; TISSUE=Leaf; RA Vad K., Mikkelsen J.D., Collinge D.B.; RT "Induction, purification and characterization of chitinase isolated from RT pea leaves inoculated with Ascochyta pisi."; RL Planta 184:24-29(1991). CC -!- FUNCTION: Defense against chitin-containing fungal pathogens. CC -!- CATALYTIC ACTIVITY: CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; CC -!- INDUCTION: By infection with the fungal pathogen Ascochyta pisi. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase CC class I subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; P21227; -. DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW. DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC. DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.60.10; Endochitinase-like; 1. DR InterPro; IPR001002; Chitin-bd_1. DR InterPro; IPR036861; Endochitinase-like_sf. DR Pfam; PF00187; Chitin_bind_1; 1. DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; KW Direct protein sequencing; Glycosidase; Hydrolase; Plant defense; KW Polysaccharide degradation. FT CHAIN 1..>23 FT /note="Endochitinase B" FT /id="PRO_0000124829" FT NON_TER 23 SQ SEQUENCE 23 AA; 2424 MW; 05CF70DA4261BC61 CRC64; EQCGRQAGGA TCPNNLCCSQ YGY //