CHI3_METAN
ID CHI3_METAN Reviewed; 296 AA.
AC Q6QDR4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Endochitinase 3;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase 3;
DE Flags: Fragment;
GN Name=chi3; Synonyms=CHIT30;
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 [MRNA], SUBCELLULAR LOCATION, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=E6;
RX DOI=10.1139/m97-045;
RA Pinto A.S., Barreto C.C., Schrank A., Ulhoa C.J., Vainstein M.H.;
RT "Purification and characterization of an extracellular chitinase from the
RT entomopathogen Metarhizium anisopliae.";
RL Can. J. Microbiol. 43:322-327(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=E6;
RX PubMed=15808943; DOI=10.1016/j.resmic.2004.10.013;
RA da Silva M.V., Santi L., Staats C.C., da Costa A.M., Colodel E.M.,
RA Driemeier D., Vainstein M.H., Schrank A.;
RT "Cuticle-induced endo/exoacting chitinase CHIT30 from Metarhizium
RT anisopliae is encoded by an ortholog of the chi3 gene.";
RL Res. Microbiol. 156:382-392(2005).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=23452951; DOI=10.1016/j.funbio.2012.12.006;
RA Staats C.C., Kmetzsch L., Lubeck I., Junges A., Vainstein M.H., Schrank A.;
RT "Metarhizium anisopliae chitinase CHIT30 is involved in heat-shock stress
RT and contributes to virulence against Dysdercus peruvianus.";
RL Fungal Biol. 117:137-144(2013).
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. Involved in heat-shock adaptation.
CC {ECO:0000269|PubMed:15808943, ECO:0000269|PubMed:23452951,
CC ECO:0000269|Ref.1}.
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:15808943, ECO:0000269|PubMed:23452951,
CC ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.537 mM for p-nitrophenyl beta-N-diacetylchitobiose
CC {ECO:0000269|Ref.1};
CC Vmax=4.86 nmol/min/mg enzyme toward p-nitrophenyl beta-N-
CC diacetylchitobiose {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 4.5-5.0. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: Induced by chitin and cuticle and repressed by glucose.
CC Protein expression is increased after host tick Boophilus microplus
CC infection. Accumulates also in response to heat-shock stress
CC conditions. {ECO:0000269|PubMed:15808943, ECO:0000269|PubMed:23452951}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased endochitinase and exochitinase
CC activities following heat-shock treatment.
CC {ECO:0000269|PubMed:23452951}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; AY545982; AAS55554.1; -; mRNA.
DR AlphaFoldDB; Q6QDR4; -.
DR SMR; Q6QDR4; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18C_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 CDD; cd02877; GH18_hevamine_XipI_class_III; 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 Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 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; Virulence.
FT CHAIN 1..296
FT /note="Endochitinase 3"
FT /id="PRO_0000429868"
FT DOMAIN 12..296
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 296 AA; 31762 MW; 50520FA62D8DD850 CRC64;
QAAPDEGRAS GHKLTVYWGA EDDTTTLDDV CNDSSYDVVN LAFLSHFFSA GGYPKMSIGN
LDGPSQAQKK AGATGLQDGS SLVKSIKNCQ SKGKPVILSM GGATDYSDVQ LNSDAQGQQI
ANTVWNLFLG GTDHKELRPF GDVKLDGVDL DNETNDGTGY LAMTKQFKAN FQKDTSKKYY
ITAAPQCPYP DQSEPLDVCQ LLDWVQVQFY NNGNCNIAQR GFAKAVKNWS KGIGSGVQLY
IGALASGADG DEGYVHAATL NRAVNQVKAM NLPNFGGAML WEAHSAVKNG QLPEED
