ID   CHI2_PEA                Reviewed;         324 AA.
AC   P21226;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Endochitinase A2;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHI2;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Alcan;
RX   PubMed=7787175; DOI=10.1007/bf00042042;
RA   Chang M.M., Horovitz D., Culley D., Hadwiger L.A.;
RT   "Molecular cloning and characterization of a pea chitinase gene expressed
RT   in response to wounding, fungal infection and the elicitor chitosan.";
RL   Plant Mol. Biol. 28:105-111(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-36.
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}.
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DR   EMBL; L37876; AAA75196.1; -; Genomic_DNA.
DR   PIR; S56694; S56694.
DR   AlphaFoldDB; P21226; -.
DR   SMR; P21226; -.
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   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; CHITINASE-RELATED; 1.
DR   PANTHER; PTHR22595:SF143; ENDOCHITINASE 1; 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   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; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           21..309
FT                   /note="Endochitinase A2"
FT                   /id="PRO_0000005308"
FT   PROPEP          310..324
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005309"
FT   DOMAIN          21..61
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        133
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        55..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        151..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        269..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   324 AA;  34678 MW;  540F0DA5EC1DC2FA CRC64;
     MSKLRIPILL VLFIVSCCSA EQCGTQAGGA LCPGGLCCSK FGWCGSTSEY CGDGCQSQCS
     GSSGGGTLSS LISGDTFNNM LKHRNDNACQ GKPFYTYDAF LSAAKAFPNF ANKGDTATKK
     REIAAFLGQT SHETTGGWPT APDGPYAWGY CFLREQNPST YCQASSEFPC ASGKQYYGRG
     PIQISWNYNY GQCGRAIGVD LLNNPDLVAT DPVISFKTAL WFWMTPQSPK PSCHDVITGG
     WTPSSADRAA GRLPGYGTVT NIINGGLECG RGQDSRVQDR IGFYKRYCDI FGIGYGDNLD
     CYSQRPFGSS LPLSSILLDT VAAA
//