CHI46_TRIHA
ID CHI46_TRIHA Reviewed; 430 AA.
AC A6N6J0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Endochitinase 46;
DE EC=3.2.1.14;
DE AltName: Full=46 kDa endochitinase;
DE AltName: Full=Chitinase 46;
DE Flags: Precursor;
GN Name=chit46;
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IABT1015;
RA Bhat G.S., Bhat S., Kuruvinashetti M.S.;
RT "Cloning and functional characterization of endochitinase gene from
RT Trichoderma spp.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION, AND
RP BIOTECHNOLOGY.
RX PubMed=20213103; DOI=10.1007/s00284-010-9611-8;
RA Monteiro V.N., do Nascimento Silva R., Steindorff A.S., Costa F.T.,
RA Noronha E.F., Ricart C.A., de Sousa M.V., Vainstein M.H., Ulhoa C.J.;
RT "New insights in Trichoderma harzianum antagonism of fungal plant pathogens
RT by secreted protein analysis.";
RL Curr. Microbiol. 61:298-305(2010).
CC -!- FUNCTION: Secreted chitinase involved in the degradation of chitin, a
CC component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Plays a morphogenetic role
CC during apical growth, cell division and differentiation (cell wall
CC morphogenesis). Acts also as an antifungal agent. Involved in the
CC degradation and further assimilation of phytopathogenic fungi, namely
CC mycoparasitism, the major mechanism accounting for the antagonistic
CC activity against phytopathogenic fungi displayed by Trichoderma.
CC {ECO:0000269|PubMed:20213103}.
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 {ECO:0000269|PubMed:20213103}.
CC -!- BIOTECHNOLOGY: The antagonistic activity of Trichoderma harzianum is
CC used for the control of several soil borne plant pathogenic fungi.
CC {ECO:0000269|PubMed:20213103}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; EF613224; ABR21205.1; -; Genomic_DNA.
DR AlphaFoldDB; A6N6J0; -.
DR SMR; A6N6J0; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PRIDE; A6N6J0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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 Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
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 SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Cleavage on pair of basic residues; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..35
FT /evidence="ECO:0000250"
FT /id="PRO_0000429892"
FT CHAIN 36..430
FT /note="Endochitinase 46"
FT /id="PRO_0000429893"
FT DOMAIN 39..408
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 103..104
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 130..133
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 173
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 238..241
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 385
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 430 AA; 46380 MW; CB09A51FBACFB31B CRC64;
MLSFLGKSVA LLAALQATLS SASPLATEER SIEKRANGYA NSVYFTNWGI YDRNFQPADL
VASDVTHVIY SFMNLQADGT VVSGDTYADF EKHYADDSWN DVGTNAYGCA KQLFKVKKAN
RGLKVLLSIG GWTWSTNFPS AASTDANRKN FAKTAITFMK DWGFDGIDVD WEYPADATQA
SNMVLLLKEV RSQLDAYAAQ YAPGYHFLLT IAAPAGKDNY SKLRLADLGQ VLDYINLMAY
DYAGSFSPLT GHDANLFANP SNPNATPFNT DSAVKDYIKG GVPANKIVLG MPIYGRSFQN
TAGIGQTYNG VGGGGGGSTG SWEAGIWDYK ALPKAGATIQ YDSVAKGYYS YNAGTKELIS
FDTPDMINTK VAYLKSLGLG GSMFWEASAD KKGADSLIGT SHRALGGLDT TQNLLSYPNS
KYDNIRNGLN
