CHI1_METAN
ID CHI1_METAN Reviewed; 423 AA.
AC O14456;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Endochitinase 1;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase 1;
DE Flags: Precursor;
GN Name=chit1; Synonyms=chit42;
OS Metarhizium anisopliae (Entomophthora anisopliae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=5530;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=E6;
RX PubMed=9732526; DOI=10.1007/s002849900368;
RA Bogo M.R., Rota C.A., Pinto H. Jr., Ocampos M., Correa C.T.,
RA Vainstein M.H., Schrank A.;
RT "A chitinase encoding gene (chit1 gene) from the entomopathogen Metarhizium
RT anisopliae: isolation and characterization of genomic and full-length
RT cDNA.";
RL Curr. Microbiol. 37:221-225(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14735222; DOI=10.1139/w03-085;
RA Baratto C.M., da Silva M.V., Santi L., Passaglia L., Schrank I.S.,
RA Vainstein M.H., Schrank A.;
RT "Expression and characterization of the 42 kDa chitinase of the biocontrol
RT fungus Metarhizium anisopliae in Escherichia coli.";
RL Can. J. Microbiol. 49:723-726(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=19593671; DOI=10.1007/s12010-009-8701-1;
RA Kern M.F., Maraschin Sde F., Vom Endt D., Schrank A., Vainstein M.H.,
RA Pasquali G.;
RT "Expression of a chitinase gene from Metarhizium anisopliae in tobacco
RT plants confers resistance against Rhizoctonia solani.";
RL Appl. Biochem. Biotechnol. 160:1933-1946(2010).
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). Participates in the infection
CC process and directly acts in the penetration process of the host
CC cuticle. {ECO:0000269|PubMed:14735222, ECO:0000269|PubMed:19593671}.
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:14735222, ECO:0000269|PubMed:19593671};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- BIOTECHNOLOGY: When expressed in tobacco plants, chit1 confers
CC resistance against Rhizoctonia solani. {ECO:0000269|PubMed:19593671}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; AF027497; AAB81998.1; -; mRNA.
DR EMBL; AF027498; AAB81999.1; -; Genomic_DNA.
DR AlphaFoldDB; O14456; -.
DR SMR; O14456; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18A_METAN; -.
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 Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..423
FT /note="Endochitinase 1"
FT /id="PRO_0000429864"
FT DOMAIN 39..401
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 380..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 103..104
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 130..133
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 173
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 238..241
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 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 423 AA; 45945 MW; 3123E41808F783AE CRC64;
MPSLFAQSLA IIATLQATLG LATPVSAPDT VIGKHAGGYV NAVYFTNWGI YGRNYQPADL
PASQISHVLY SFLNLSNNGT VYSGDSWADI DKHYPNDSWN DVGTNVYGCV KQLYLLKKAN
RNMKTMLSIG GWTWSTNFPA AASTAATRSN FAKSAVTIMK DWGFDGIDVD WEYPADDVQA
TNMVLLLQAI REELDAYAAK FAQGYHFQLS IAAPAGPANY NKLHLGDLGK VLDYINLMAY
DFSGSWSNSS AHNANLYAIR ANLNAPFNTD HAVNDYIKGG VPASKIVLAL PIYGNSFQKT
NGIGKPFSGA GDGSWENGIW DYKVHSKAGA DGIYDDGDKG YYSYDPSVKE LISIDTPDIT
KDKVTYLKSK GLGGSMFWEA SSDRSGSQSL IGTSSNKLGG PDSTENLLNY PDSKYDNMRK
QMA
