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 28-JUN-2023, entry version 83. 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}. 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 PDB; 7ZY9; X-ray; 1.60 A; A=19-321. DR PDB; 7ZYA; X-ray; 1.12 A; A=19-321. DR PDBsum; 7ZY9; -. DR PDBsum; 7ZYA; -. DR AlphaFoldDB; Q12713; -. DR SMR; Q12713; -. DR CAZy; GH18; Glycoside Hydrolase Family 18. DR CLAE; CHI18C_TRIHA; -. 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 Gene3D; 3.20.20.80; Glycosidases; 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 PANTHER; PTHR45708; ENDOCHITINASE; 1. DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1. DR Pfam; PF00704; Glyco_hydro_18; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS01095; GH18_1; 1. DR PROSITE; PS51910; GH18_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding; KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal; KW 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" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 47..50 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 58..66 FT /evidence="ECO:0007829|PDB:7ZYA" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 75..80 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 94..105 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 109..115 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 127..141 FT /evidence="ECO:0007829|PDB:7ZYA" FT TURN 153..156 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 173..186 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:7ZYA" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 208..213 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 217..222 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 245..252 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 261..269 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 279..289 FT /evidence="ECO:0007829|PDB:7ZYA" FT STRAND 295..301 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 303..308 FT /evidence="ECO:0007829|PDB:7ZYA" FT HELIX 312..320 FT /evidence="ECO:0007829|PDB:7ZYA" 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 //