ID   CHIT_DIOJA              Reviewed;         250 AA.
AC   P80052;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Acidic endochitinase;
DE            EC=3.2.1.14;
OS   Dioscorea japonica (Japanese yam).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC   Dioscorea.
OX   NCBI_TaxID=4673;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Aerial tuber;
RX   PubMed=1400311; DOI=10.1016/s0021-9258(19)88648-9;
RA   Araki T., Funatsu J., Kuramoto M., Konno H., Torikata T.;
RT   "The complete amino acid sequence of yam (Dioscorea japonica) chitinase. A
RT   newly identified acidic class I chitinase.";
RL   J. Biol. Chem. 267:19944-19947(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-53, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   TISSUE=Aerial tuber;
RX   PubMed=1623187; DOI=10.1007/bf00027360;
RA   Araki T., Funatsu J., Kuramoto M., Torikata T.;
RT   "Amino acid sequence of the N-terminal domain of yam (Dioscorea japonica)
RT   aerial tuber acidic chitinase. Evidence for the presence of a wheat germ
RT   agglutinin domain in matured acidic chitinase from unstressed tuber.";
RL   Plant Mol. Biol. 19:351-354(1992).
RN   [3]
RP   DISULFIDE BONDS IN CATALYTIC DOMAIN.
RX   PubMed=8914841; DOI=10.1006/abbi.1996.0488;
RA   Araki T., Kuramoto M., Torikata T.;
RT   "Positions of disulfide bonds in yam (Dioscorea japonica) acidic class IL
RT   (class IV) chitinase.";
RL   Arch. Biochem. Biophys. 335:118-122(1996).
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   -!- 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   PIR; A44039; A44039.
DR   AlphaFoldDB; P80052; -.
DR   SMR; P80052; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
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   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Plant defense; Polysaccharide degradation; Pyrrolidone carboxylic acid.
FT   CHAIN           1..250
FT                   /note="Acidic endochitinase"
FT                   /id="PRO_0000124826"
FT   DOMAIN          1..36
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1623187"
FT   DISULFID        3..12
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        5..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        11..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        29..34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        66..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:8914841"
FT   DISULFID        128..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:8914841"
FT   DISULFID        218..250
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:8914841"
SQ   SEQUENCE   250 AA;  27908 MW;  958E0816553C4985 CRC64;
     QNCQCDTTIY CCSQHGYCGN SYDYCGPGCQ AGPCWDPCEG DGTLTVSDIV TQEFWDGIAS
     QAAANCPGKS FYTRSNFLEA VSAYPGFGTK CTDEDRKREI AAYFAHVTHE TGHLCYIEER
     DGHANNYCQE SQQYPCNPNK EYFGRGPMQL SWNYNYIDAG KELHFDGLND PDIVGRDPII
     SFKTSLWFWI RKGVQYVILD PNQGFGATIR IINGGQECDG HNTAQMMARV GYYQEYCAQL
     GVSPGNNLPC