CHI33_TRIHA
ID CHI33_TRIHA Reviewed; 321 AA.
AC Q12713;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Endochitinase 33;
DE EC=3.2.1.14;
DE AltName: Full=33 kDa endochitinase;
DE AltName: Full=Chitinase 33;
DE Flags: Precursor;
GN Name=chit33;
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 [MRNA], AND INDUCTION.
RC STRAIN=2413;
RX PubMed=8575023; DOI=10.1007/bf00310819;
RA Limon M.C., Lora J.M., Garcia I., de la Cruz J., Llobell A., Benitez T.,
RA Pintor-Toro J.A.;
RT "Primary structure and expression pattern of the 33-kDa chitinase gene from
RT the mycoparasitic fungus Trichoderma harzianum.";
RL Curr. Genet. 28:478-483(1995).
RN [2]
RP INDUCTION, SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1606968; DOI=10.1111/j.1432-1033.1992.tb16994.x;
RA de la Cruz J., Hidalgo-Gallego A., Lora J.M., Benitez T., Pintor-Toro J.A.,
RA Llobell A.;
RT "Isolation and characterization of three chitinases from Trichoderma
RT harzianum.";
RL Eur. J. Biochem. 206:859-867(1992).
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). May be involved in the degradation and further
CC assimilation of phytopathogenic fungi, namely mycoparasitism, the major
CC mechanism accounting for the antagonistic activity against
CC phytopathogenic fungi displayed by Trichoderma.
CC {ECO:0000269|PubMed:1606968}.
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 Evidence={ECO:0000269|PubMed:1606968};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mg/ml for colloidal chitin {ECO:0000269|PubMed:1606968};
CC KM=0.85 mM for p-nitrophenyl-N-N'-diacetylchitobiose
CC {ECO:0000269|PubMed:1606968};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:1606968};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1606968}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1606968}.
CC -!- INDUCTION: Specifically induced by chitin and strongly repressed by
CC glucose. {ECO:0000269|PubMed:1606968, ECO:0000269|PubMed:8575023}.
CC -!- BIOTECHNOLOGY: The antagonistic activity of Trichoderma harzianum is
CC used for the control of several soil borne plant pathogenic fungi.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; X80006; CAA56315.1; -; mRNA.
DR PIR; S60371; S60371.
DR AlphaFoldDB; Q12713; -.
DR SMR; Q12713; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18C_TRIHA; -.
DR PRIDE; Q12713; -.
DR BRENDA; 3.2.1.14; 6445.
DR SABIO-RK; Q12713; -.
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 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..321
FT /note="Endochitinase 33"
FT /id="PRO_0000429895"
FT DOMAIN 27..321
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 321 AA; 34348 MW; 6F465B9057E2B5D9 CRC64;
MPSLTALASL LALVPSALAG WNVNSKQNIA VYWGQNSANS QSTQQRLSFY CNDANINVID
IAFLNGITPP MTNFANAGDR CTPFSDNPWL LQCPEIEADI KTCQANGKTI LLSLGGDSYT
QGGWSSTGAA QSAADQVWAM FGPVQSGSSV HRPFGSAVVD GFDFDFEATT NNLAAFGAQL
KSRTNAAGGK KYYFSAAPQC FFPDAAVGAL INAVPMDWIQ IQFYNNPCGV SGFTPGTSTQ
NNYNYQTWEN WAKTSPNPNV KLLVGIPAGP GAGRGYVSGS QLTSVFQYSK GFSTFAGAMM
WDMSQLYQNT GFETQVVNAL R
