ID   CHIT_AVESA              Reviewed;         200 AA.
AC   P86181;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Fragments;
OS   Avena sativa (Oat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Aveninae; Avena.
OX   NCBI_TaxID=4498;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Adamo; TISSUE=Seed;
RX   PubMed=19224400; DOI=10.1007/s12010-009-8557-4;
RA   Sorensen H.P., Madsen L.S., Petersen J., Andersen J.T., Hansen A.M.,
RA   Beck H.C.;
RT   "Oat (Avena sativa) seed extract as an antifungal food preservative through
RT   the catalytic activity of a highly abundant class I chitinase.";
RL   Appl. Biochem. Biotechnol. 160:1573-1584(2010).
CC   -!- FUNCTION: This protein functions as a defense against chitin-containing
CC       fungal pathogens. {ECO:0000269|PubMed:19224400}.
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         Evidence={ECO:0000269|PubMed:19224400};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86181; -.
DR   SMR; P86181; -.
DR   BRENDA; 3.2.1.14; 588.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00182; Glyco_hydro_19; 2.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Carbohydrate metabolism; Chitin degradation;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Glycosidase;
KW   Hydrolase; Plant defense; Polysaccharide degradation.
FT   CHAIN           <1..>200
FT                   /note="Endochitinase"
FT                   /id="PRO_0000365620"
FT   ACT_SITE        58
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        ?..193
FT                   /evidence="ECO:0000250|UniProtKB:Q9FRV1"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000305"
FT   NON_CONS        71..72
FT                   /evidence="ECO:0000305"
FT   NON_CONS        79..80
FT                   /evidence="ECO:0000305"
FT   NON_CONS        188..189
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         200
SQ   SEQUENCE   200 AA;  21728 MW;  725479B5CF16A1CB CRC64;
     VSSVISSSLF EKMLLHRGFY TYDAFIAAAK SFPAFATTGS TDVRKREVAA FLAQTSHETT
     GGWPTAPDGP YELGSTSDYF GRGPIQISYN YNYGAAGKAI GVDLLRNPDL VTSDNTVEFK
     TALWFWMTPQ SPKPSSHDVI TGRWSPSSTD KAAGRVPGYG VLTNIIDGGV ECGKGQESHV
     ADRIGYYKDN LDCYNQKPFA