ID   Q40667_ORYSA            Unreviewed;       319 AA.
AC   Q40667;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
OS   Oryza sativa (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4530 {ECO:0000313|EMBL:CAA82849.1};
RN   [1] {ECO:0000313|EMBL:CAA82849.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim Y., Baek J., Park H., Choi Y., Kim S.;
RT   "Isolation and characterization of the cDNA clones encoding class I
RT   chitinase in suspension cultures of rice cell.";
RL   Biosci. Biotechnol. Biochem. 0:0-0(1994).
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:0000256|ARBA:ARBA00000822};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000256|ARBA:ARBA00009373}.
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DR   EMBL; Z29961; CAA82849.1; -; mRNA.
DR   PIR; JC2252; JC2252.
DR   AlphaFoldDB; Q40667; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
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:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 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   PANTHER; PTHR22595:SF79; BASIC ENDOCHITINASE B; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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   2: Evidence at transcript level;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW   ProRule:PRU00261};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR001060-2};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..319
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004231483"
FT   DOMAIN          20..61
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-1"
FT   DISULFID        23..38
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        32..44
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        55..59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        98..160
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
FT   DISULFID        174..182
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
FT   DISULFID        279..311
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
SQ   SEQUENCE   319 AA;  33600 MW;  C990572C114FC0A9 CRC64;
     MRALAVVVVA TRFAVVAVPP EQCGSQAGGA LCPNCLCCSQ YGWCGSTSAY CGSGCQSQCS
     GSCGGGADPA SGGASGVASI VSRSLFDQML LHRNDAACPA KNFYTYDAFV AAANAYPDFA
     TTGDAATRKR EVAAFLAQTS HETTGGWATA PDGPYSWGYC FKEENNGNVG SDYCVQSSQC
     RCAGKKYYGR GPIQISYNYN YGPACQAIGS NLLSNPDLVA SDAISFKTAF WFWMTPQSPK
     PSCHAVMTGQ WTPNGNDQAA GRVPGYGVVT NIINGGVECG HGADSRVADR IGFYKRYCDM
     LGVSYGANLD CYNQRPFNS
//