ID CHI37_TRIHA Reviewed; 337 AA.
AC Q8NJQ5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 22-FEB-2023, entry version 67.
DE RecName: Full=Endochitinase 37;
DE EC=3.2.1.14;
DE AltName: Full=37 kDa endochitinase;
DE AltName: Full=Chitinase 37;
DE Flags: Precursor;
GN Name=chit37;
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=ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150;
RA Viterbo A., Montero M., Ramot O., Friesem D., Monte E., Llobell A.,
RA Chet I.;
RT "Expression regulation of the endochitinase chit36 from Trichoderma
RT asperellum (T. harzianum T-203).";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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=0.5 mg/ml for colloidal chitin {ECO:0000269|PubMed:1606968};
CC KM=0.7 mM for p-nitrophenyl-N-N'-diacetylchitobiose
CC {ECO:0000269|PubMed:1606968};
CC Temperature dependence:
CC Optimum temperature is 45-50 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.
CC {ECO:0000269|PubMed:1606968}.
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 V subfamily. {ECO:0000305}.
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DR EMBL; AF525753; AAM93195.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NJQ5; -.
DR SMR; Q8NJQ5; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18B_TRIHA; -.
DR GlyCosmos; Q8NJQ5; 1 site, No reported glycans.
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; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
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 SMART; SM00636; Glyco_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 Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..337
FT /note="Endochitinase 37"
FT /id="PRO_0000429894"
FT DOMAIN 38..337
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 337 AA; 35478 MW; 0C9B50F416897EF1 CRC64;
MTRLLDASFL LLPVIASTLF GTASAQSTCA TKGKPAGKVL QGYWENWDGS ANGVHPGFGW
TPIENPVIAQ NGYNVINAAF PVILSDGTAL WEDGMDATVK VATPAEMCQA KAAGATILMS
IGGATAGIDL SSSTVADKFI STIVPILKQY NFDGIDIDIE TGLVGSGSIG TLSTSQANLI
RIIDGVLAQM PANFGLTMAP ETAYVTGGSV VYGSIWGSYL PIIKKYVDNG RLWWLNMQYY
NGDMYGCSGD SYAAGTVQGF TAQTDCLNNG ITIQGTTIKV PYNMQVPGLP AQSGAGGGYM
TPALVGQAWD HYNGALKGLM TWSINWDGSK NWTFGDN
//
