ID   CHIA_PHAAN              Reviewed;         298 AA.
AC   P29024;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Acidic endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7517787;
RA   Ishige F., Mori H., Yamazaki K., Imaseki H.;
RT   "Cloning of a complementary DNA that encodes an acidic chitinase which is
RT   induced by ethylene and expression of the corresponding gene.";
RL   Plant Cell Physiol. 34:103-111(1993).
CC   -!- FUNCTION: This protein functions as a defense against chitin containing
CC       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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- INDUCTION: By ethylene.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01948.1; Type=Erroneous initiation; Evidence={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   EMBL; D11335; BAA01948.1; ALT_INIT; mRNA.
DR   PIR; S36932; S36932.
DR   RefSeq; NP_001316758.1; NM_001329829.1.
DR   AlphaFoldDB; P29024; -.
DR   SMR; P29024; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GeneID; 108339599; -.
DR   KEGG; var:108339599; -.
DR   OrthoDB; 923272at2759; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..298
FT                   /note="Acidic endochitinase"
FT                   /id="PRO_0000011917"
FT   DOMAIN          30..298
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        156
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        49..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        185..214
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   298 AA;  31702 MW;  3B382DE1C07656A9 CRC64;
     MKPNMACLKQ VSALLLPLLF ISFFKPSHAG GISVYWGQNG NEGSLADACN TGNYKYVNIA
     FLFTFGGGQT PQLNLAGHCN PSINNCNVFS DQIKECQSKD IKVLLSLGGA SGSYSLTSAD
     DATQVANYIW NNFLGGQSSS RPLGDAILDG VDFDIESGTG EHWDDLARAL KGFNSQLLLT
     AAPQCPIPDA HLDTAIKTGL FDIVWVQFYN NPPCQYSSGN TNDLISSWNQ WTSSQAKQLF
     LGVPASTAAA GSGFIPADVL TSQVLPTIKG SSKYGGVMLW DRFNDGQSGY SGAIIGSV