ID   CHIA_CICAR              Reviewed;         293 AA.
AC   P36908;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Acidic endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
OS   Cicer arietinum (Chickpea) (Garbanzo).
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; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. ILC 3279;
RX   PubMed=8208854; DOI=10.1104/pp.103.1.297;
RA   Vogelsang R., Barz W.;
RT   "Cloning of a class III acidic chitinase from chickpea.";
RL   Plant Physiol. 103:297-298(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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; X70660; CAA49998.1; -; mRNA.
DR   PIR; S31763; S31763.
DR   RefSeq; NP_001296619.1; NM_001309690.1.
DR   AlphaFoldDB; P36908; -.
DR   SMR; P36908; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GeneID; 101502863; -.
DR   KEGG; cam:101502863; -.
DR   Proteomes; UP000087171; Chromosome Ca4.
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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..293
FT                   /note="Acidic endochitinase"
FT                   /id="PRO_0000011915"
FT   DOMAIN          24..293
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        150
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        43..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        179..208
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  31230 MW;  F7C7DFC17A5720F4 CRC64;
     MEKCFNIIPS LLLISLLIKS SNAAGIAVYW GQNGNEGSLQ DACNTNNYQF VNIAFLSTFG
     NGQNPQINLA GHCDPSTNGC TKFSPEIQAC QAKGIKVLLS LGGGAGSYSL NSAEEATTLA
     NYLWNNFLGG TSTSRPLGDA VLDGIDFDIE SGGQHYDELA KALNGFSQQK VYLSAAPQCP
     YPDAHLDSAI QTGLFDYVWV QFYNNPQCQY SNGNINNLVN AWNQWTSSQA KQVFLGVPAS
     DAAAPSGGLI PADVLTSQVL PAIKTSPKYG GVMIWDRFND AQSGYSNAIK GSV