CHIT3_VITVI
ID CHIT3_VITVI Reviewed; 301 AA.
AC P51614;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Acidic endochitinase;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=CHIT3;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Pinot;
RX PubMed=9390436; DOI=10.1104/pp.115.3.1029;
RA Busam G., Kassemeyer H.H., Matern U.;
RT "Differential expression of chitinases in Vitis vinifera L. responding to
RT systemic acquired resistance activators or fungal challenge.";
RL Plant Physiol. 115:1029-1038(1997).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; Z68123; CAA92207.1; -; mRNA.
DR RefSeq; NP_001268048.1; NM_001281119.1.
DR AlphaFoldDB; P51614; -.
DR SMR; P51614; -.
DR STRING; 29760.VIT_16s0050g02220.t01; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PRIDE; P51614; -.
DR GeneID; 100233088; -.
DR KEGG; vvi:100233088; -.
DR eggNOG; KOG4701; Eukaryota.
DR OrthoDB; 923272at2759; -.
DR ExpressionAtlas; P51614; differential.
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; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..301
FT /note="Acidic endochitinase"
FT /id="PRO_0000011921"
FT DOMAIN 26..301
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 45..92
FT /evidence="ECO:0000250"
FT DISULFID 75..82
FT /evidence="ECO:0000250"
FT DISULFID 187..216
FT /evidence="ECO:0000250"
SQ SEQUENCE 301 AA; 32351 MW; 54E3A59E8E2E007B CRC64;
MARTPQSTPL LISLSVLALL QTSYAGGIAI YWGQNGNEGT LTQTCNTGKY SYVNIAFLNK
FGNGQTPEIN LAGHCNPASN GCTSVSTGIR NCQNRGIKVM LSIGGGAGSY SLSSSNDAQN
VANYLWNNFL GGQSSSRPLG DAVLDGIDFD IELGSTLHWD DLARALSRIE FQQERGRKVY
LTAAPQCPFP DKVPGTALNT GLFDYVWVQF YNNPPCQYSS GNTNNLLNSW NRWTSSINST
GSFMGLPASS AAAGRGFIPA NVLTSQILPV IKRSPKYGGV MLWSKYYDDQ SGYSSSIKSS
V