CHI3_TOBAC
ID CHI3_TOBAC Reviewed; 334 AA.
AC P29059;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Endochitinase 3;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=CHN14;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Havana 425; TISSUE=Leaf;
RX PubMed=1588915; DOI=10.1007/bf00266251;
RA van Buuren M., Neuhaus J.-M., Shinshi H., Ryals J., Meins F. Jr.;
RT "The structure and regulation of homeologous tobacco endochitinase genes of
RT Nicotiana sylvestris and N. tomentosiformis origin.";
RL Mol. Gen. Genet. 232:460-469(1992).
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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}. Note=Vacuolar and
CC protoplast. {ECO:0000305}.
CC -!- PTM: The 4-hydroxyproline residues are not glycosylated in this plant
CC vacuolar protein. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; X64518; CAA45821.1; -; Genomic_DNA.
DR PIR; S20982; S20982.
DR RefSeq; XP_016461053.1; XM_016605567.1.
DR AlphaFoldDB; P29059; -.
DR SMR; P29059; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PRIDE; P29059; -.
DR GeneID; 107784434; -.
DR KEGG; nta:107784434; -.
DR OMA; TRICIGS; -.
DR OrthoDB; 1132954at2759; -.
DR PhylomeDB; P29059; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
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:0050832; P:defense response to fungus; IBA:GO_Central.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycosidase; Hydrolase; Hydroxylation; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..23
FT CHAIN 24..327
FT /note="Endochitinase 3"
FT /id="PRO_0000005334"
FT PROPEP 328..334
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000005335"
FT DOMAIN 24..65
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 64..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT MOD_RES 73
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 26..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 35..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 40..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 59..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 106..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 180..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 287..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 334 AA; 36221 MW; 4F684CE1FBD432FB CRC64;
MRLLEFTALS SLLVLFLLLA VSAEQCGKQA GGARCPSGMC CSNFGWCGNT QDYCGPGKCQ
SQCPSGPGPT PRPPTPTPGP STGDISNIIS SSMFDQMLKH RNDNTCQGKS FYTYNAFITA
ARSFRGFGTT GDTTRRKREV AAFFAQTSHE TTGGWDTAPD GRYAWGYCYL REQGNPPSYC
VQSSQWPCAP GQKYYGRGPI QISYNYNYGP CGRAIGQNLL NNPDLVATNA VVSFKSAIWF
WMTAQSPKPS CHDVITGRWT PSAADRAANR LPGYGVITNI INGGLECGHG SDARVQDRIG
FYRRYCSILG VSPGDNIDCG NQKSFNSGLL LETM
