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 18-SEP-2019, entry version 73. 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; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; OC 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., RA Benitez T., Pintor-Toro J.A.; RT "Primary structure and expression pattern of the 33-kDa chitinase gene RT from the mycoparasitic fungus Trichoderma harzianum."; RL Curr. Genet. 28:478-483(1995). RN [2] RP INDUCTION, SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, CATALYTIC RP ACTIVITY, AND 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., RA Pintor-Toro J.A., 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 CC chitin, a component of the cell walls of fungi and exoskeletal CC elements of some animals (including worms and arthropods). Plays a CC morphogenetic role during apical growth, cell division and CC differentiation (cell wall morphogenesis). May be involved in the CC degradation and further assimilation of phytopathogenic fungi, CC namely mycoparasitism, the major mechanism accounting for the CC antagonistic activity against phytopathogenic fungi displayed by CC Trichoderma. {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 CC by glucose. {ECO:0000269|PubMed:1606968, CC ECO:0000269|PubMed:8575023}. CC -!- BIOTECHNOLOGY: The antagonistic activity of Trichoderma harzianum CC is used for the control of several soil borne plant pathogenic CC fungi. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase CC class III subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X80006; CAA56315.1; -; mRNA. DR PIR; S60371; S60371. DR SMR; Q12713; -. DR CAZy; GH18; Glycoside Hydrolase Family 18. DR mycoCLAP; 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:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. 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; CHITINASE_18; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal; KW Virulence. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 321 Endochitinase 33. FT /FTId=PRO_0000429895. FT ACT_SITE 167 167 Proton donor. {ECO:0000255|PROSITE- FT ProRule:PRU10053}. 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 //