ID A0A100IAW6_ASPNG Unreviewed; 512 AA.
AC A0A100IAW6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=ABL_02355 {ECO:0000313|EMBL:GAQ37864.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ37864.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ37864.1}.
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DR EMBL; BCMY01000003; GAQ37864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IAW6; -.
DR PaxDb; 5061-CADANGAP00004088; -.
DR VEuPathDB; FungiDB:An04g04670; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1177639; -.
DR VEuPathDB; FungiDB:ATCC64974_80160; -.
DR VEuPathDB; FungiDB:M747DRAFT_295848; -.
DR OMA; RWKGEWI; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; cd06548; GH18_chitinase; 1.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.10.350.10; LysM domain; 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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
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}.
FT DOMAIN 2..47
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 122..487
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 34..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 56509 MW; 0376435F590BCCCF CRC64;
MSTYTIASGD SLWKISQDHG VTLDALRAAN PQITNPDLIY PGQQLNIPGS DQSQPPPPES
RGITNDGASH FSPSDPPIHL AVCPPGPPVV PSAAGGAPPA VPPRPPMARP PPPWINVGRP
GYKTVGYFTN WGVYGRNYQP QDIPAEYITH ILYSFANIRP TGEVFLTDTY SDLEKHYPND
SWSEPGTNAY GCIKQLYLLK QQHRHLKTLL SIGGWTYSPN FAAPASTPRG RETFARSAVH
LLADLGFDGI DIDWEYPADA SQAKDFVILL KDVRRVLDEY SATHLGGKRL LLTIAAPCGP
DNIRKLRIGD MDPYLDFWNL MCYDFSGSWD KNSGHMANVF HSGRGEITPF CADGAVTMYL
NGGVRDPRKI IFGLPLYGRA FEGTDGPGGG FQGVGEGSWE NGVWDYKDLP LKGSREVVDP
RLMASWCHDP VNRKMVSYDT PEVAAMKTDY VANRHLGGAM WWELSGDHHV SHERSLVRRT
AERLGRLGGL DGTENTLYYP LSRFENLRRG CA
//
