ID A0A371DWR4_9APHY Unreviewed; 458 AA.
AC A0A371DWR4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=OH76DRAFT_1334741 {ECO:0000313|EMBL:RDX56992.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX56992.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX56992.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX56992.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC {ECO:0000256|RuleBase:RU004453}.
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DR EMBL; KZ857379; RDX56992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DWR4; -.
DR STRING; 139420.A0A371DWR4; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd12215; ChiC_BD; 1.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
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; PF02839; CBM_5_12; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..458
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016786081"
FT DOMAIN 31..331
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 330..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 47917 MW; 9EFAD39144B099CC CRC64;
MASLWLASAL SVLAIGALRG AAFDISRQDN VRLHSYWGQN SYGATHSDQA NWQKTLSTYC
QDDSIDTIPL AFLNVFFGAG GAPSLDLANI CNAVDDSVFP GTSLPQCSFL ASDIQFCQSK
GKIVTLSLGG ATGAASFSSD AQASAFGDTI WNMFLGGSSS TRPFGAAVLD GIDLDIEGGG
TTYFATFINR IRTLAAGSPK KYYFTAAPQC PFPDAYLSTV LNAVAFDAVY VQFYNNYCGV
INYPNSNDWN FDQWDTWAKT VAVNKNVKIY IGAPASSTAG GGYVDLTTLS NIALSTRSQF
SSFGGVMLWD ASQAYANGRF DQGIKNAIRQ NGNGGTTSTP ITVSTPTTSK TSTTSKSTTT
TTTKPTTTTT SPGSTTTVSS GSCAGVGSWV GNVAYNGGDR VIYNGHLWTA KWWSYGDTPG
GAAGDWTDNG VCSSFAAAIP TAHVAQMSAK SPAASPTA
//