ID B8NU09_ASPFN Unreviewed; 450 AA.
AC B8NU09;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=AFLA_101800 {ECO:0000313|EMBL:EED46516.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED46516.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED46516.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- FUNCTION: GPI-anchored chitinase involved in the degradation of chitin,
CC a component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Required to reshape the cell
CC wall at the sites where cell wall remodeling and/or cell wall
CC maturation actively take place such as sites of conidia formation.
CC {ECO:0000256|ARBA:ARBA00024658}.
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000256|ARBA:ARBA00025727}.
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DR EMBL; EQ963484; EED46516.1; -; Genomic_DNA.
DR RefSeq; XP_002384052.1; XM_002384011.1.
DR AlphaFoldDB; B8NU09; -.
DR STRING; 332952.B8NU09; -.
DR EnsemblFungi; EED46516; EED46516; AFLA_101800.
DR VEuPathDB; FungiDB:AFLA_010430; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_007818_1_1_1; -.
DR OMA; GTTCFAY; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR005089; CBM_fam19.
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; PF03427; CBM_19; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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 Cell wall {ECO:0000256|ARBA:ARBA00022512};
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 Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..450
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002878436"
FT DOMAIN 30..325
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 325..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 47160 MW; 502DC1FE8FA8E5C5 CRC64;
MSSSKTVALF TLALASFKGA LAALRLNSPN NIAVYWGKYH AKRIICAITD MTSQVYQISF
LTRINGAGGV PEVNFANAGD NCTAFPGTQL LDCPQIAEDI KECQSLGRTI LLSIGGATYN
EGGFTNEAAA TAGAKMIWET FGPVSNPSVK RPFGDAVVDG FDFDFEATVN NMPAFANQLR
SYYASDTSKK YYTTAAPQCP YPDAADGPML DGAVYFDAIW IQFYNNYCGL QAFVPGSAAQ
NNFNFDVWDK WARETSLNKN AKVFLGVPGN QGAAGTGYQP ISTVSEIIKY VKQFSSFGGV
MVWDASQVYA NTGFLSGLRS ALGGGGTTPA PTTSPTTTPT TSLTTTSKTT SPTPTTKSTS
TSTTLTTTTK SSTASPTSSK PTASPTSTVC PIAGQTCPTS GAFSCNGSQF GICDNGRWVM
QQCPAGLVCA QSGSGVYCDY PGSTGVAPCS
//
