ID   CHI2_BRANA              Reviewed;         322 AA.
AC   Q09023;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Endochitinase CH25;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8310072; DOI=10.1104/pp.101.4.1403;
RA   Hamel F., Bellemare G.;
RT   "Nucleotide sequence of a Brassica napus endochitinase gene.";
RL   Plant Physiol. 101:1403-1403(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Westar;
RX   PubMed=7548207; DOI=10.1016/0167-4781(95)00099-3;
RA   Hamel F., Bellemare G.;
RT   "Characterization of a class I chitinase gene and of wound-inducible, root
RT   and flower-specific chitinase expression in Brassica napus.";
RL   Biochim. Biophys. Acta 1263:212-220(1995).
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   -!- TISSUE SPECIFICITY: High expression in roots, moderate in floral
CC       tissues and low in stems and leaves. {ECO:0000269|PubMed:7548207}.
CC   -!- INDUCTION: In roots by wounding and ethephon.
CC       {ECO:0000269|PubMed:7548207}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; M95835; AAA32986.1; -; Genomic_DNA.
DR   PIR; S59953; S59953.
DR   RefSeq; XP_013731720.1; XM_013876266.1.
DR   AlphaFoldDB; Q09023; -.
DR   SMR; Q09023; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   EnsemblPlants; CDY42151; CDY42151; GSBRNA2T00074333001.
DR   GeneID; 106435387; -.
DR   Gramene; CDY42151; CDY42151; GSBRNA2T00074333001.
DR   KEGG; bna:106435387; -.
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: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; 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; 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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..322
FT                   /note="Endochitinase CH25"
FT                   /id="PRO_0000005290"
FT   DOMAIN          21..62
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        136
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        23..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        32..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        56..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        92..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        166..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        273..305
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   322 AA;  34816 MW;  E62EE4B17211DBCD CRC64;
     MKSCLLLFLI FSFLLSFSLA EQCGRQAGGA LCPNGLCCSE FGWCGDTEAY CKQPGCQSQC
     GGTPPGPTGD LSGIISRSQF DDMLKHRNDN ACPARGFYTY DAFINAAKSF PGFGTTGDTA
     TRKKEIAAFF GQTSHETTGG WATAPDGPYS WGYCFKQEQN PSSNYCSPSA EWPCASGKSY
     YGRGPMQLSW NYNYGQCGRA IGSDLLNNPD LVSNDPVIAF KAAIWFWMTP QSPKPSCHAV
     IVGQWQPSDA DRAAGRVPGY GVITNIINGG LECGRGQDAR VADRIGFYQR YCNILGVNPG
     GNLDCYNQRS FASVNFFLDA AI