CHI42_TRIHA
ID CHI42_TRIHA Reviewed; 423 AA.
AC P48827;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Endochitinase 42;
DE EC=3.2.1.14;
DE AltName: Full=42 kDa endochitinase;
DE AltName: Full=Chitinase 42;
DE Flags: Precursor;
GN Name=chit42;
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 PROTEIN SEQUENCE OF 35-52; 93-107; 371-385
RP AND 397-414.
RX PubMed=7750151; DOI=10.1007/bf00326583;
RA Garcia I., Lora J.M., de la Cruz J., Benitez T., Llobell A.,
RA Pintor-Toro J.A.;
RT "Cloning and characterization of a chitinase (chit42) cDNA from the
RT mycoparasitic fungus Trichoderma harzianum.";
RL Curr. Genet. 27:83-89(1994).
RN [2]
RP INDUCTION, SUBCELLULAR LOCATION, 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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=T4;
RX PubMed=22744980; DOI=10.1002/pmic.201200048;
RA da Silva A.J., Gomez-Mendoza D.P., Junqueira M., Domont G.B.,
RA Ximenes Ferreira Filho E., de Sousa M.V., Ricart C.A.;
RT "Blue native-PAGE analysis of Trichoderma harzianum secretome reveals
RT cellulases and hemicellulases working as multienzymatic complexes.";
RL Proteomics 12:2729-2738(2012).
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: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=0.3 mg/ml for colloidal chitin {ECO:0000269|PubMed:1606968};
CC Temperature dependence:
CC Optimum temperature is 45-50 degrees Celsius.
CC {ECO:0000269|PubMed:1606968};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1606968,
CC ECO:0000269|PubMed:22744980}.
CC -!- INDUCTION: Specifically induced by chitin and is catabolite repressed.
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; S78423; AAB34355.1; -; mRNA.
DR PIR; S51369; S51369.
DR PDB; 6EPB; X-ray; 1.75 A; A=1-423.
DR PDB; 6YLJ; X-ray; 1.75 A; A=1-423.
DR PDB; 6YN4; X-ray; 1.82 A; A=1-423.
DR PDB; 7AKQ; X-ray; 2.32 A; A=1-423.
DR PDBsum; 6EPB; -.
DR PDBsum; 6YLJ; -.
DR PDBsum; 6YN4; -.
DR PDBsum; 7AKQ; -.
DR AlphaFoldDB; P48827; -.
DR SMR; P48827; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18D_TRIHA; -.
DR PRIDE; P48827; -.
DR BRENDA; 3.2.1.14; 6445.
DR SABIO-RK; P48827; -.
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 3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..34
FT /evidence="ECO:0000269|PubMed:7750151"
FT /id="PRO_0000011934"
FT CHAIN 35..423
FT /note="Endochitinase 42"
FT /id="PRO_0000011935"
FT DOMAIN 38..401
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 102..103
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 129..132
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 172
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 237..240
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 378
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6YLJ"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 176..200
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7AKQ"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:6EPB"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:6EPB"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:6EPB"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 390..398
FT /evidence="ECO:0007829|PDB:6EPB"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:6EPB"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:6EPB"
SQ SEQUENCE 423 AA; 46057 MW; DF90378EED1C30BE CRC64;
MLSFLGKSVA LLAALQATLS SPKPGHRRAS VEKRANGYAN SVYFTNWGIY DRNFQPADLV
ASDVTHVIYS FMNLQADGTV ISGDTYADYE KHYADDSWND VGTNAYGCVK QLFKVKKANR
GLKVLLSIGG WTWSTNFPSA ASTDANRKNF AKTAITFMKD WGFDGIDIDW EYPADATQAS
NMILLLKEVR SQRDAYAAQY APGYHFLLTI AAPAGKDNYS KLRLADLGQV LDYINLMAYD
YAGSFSPLTG HDANLFNNPS NPNATPFNTD SAVKDYINGG VPANKIVLGM PIYGRSFQNT
AGIGQTYNGV GSGSWEAGIW DYKALPKAGA TVQYDSVAKG YYSYNSATKE LISFDTPDMI
NTKVAYLKSL GLGGSMFWEA SADKKGADSV IGTSHRALGG LDTTQNLLSY PNSKYDNIKN
GLN
