ID   A0A117E230_ASPNG        Unreviewed;       239 AA.
AC   A0A117E230;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Chitin deacetylase {ECO:0000313|EMBL:GAQ44992.1};
GN   ORFNames=ABL_07653 {ECO:0000313|EMBL:GAQ44992.1};
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:GAQ44992.1, 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   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
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:GAQ44992.1}.
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DR   EMBL; BCMY01000014; GAQ44992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117E230; -.
DR   PaxDb; 5061-CADANGAP00009699; -.
DR   VEuPathDB; FungiDB:An12g04480; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_45285; -.
DR   VEuPathDB; FungiDB:ATCC64974_37750; -.
DR   VEuPathDB; FungiDB:M747DRAFT_309984; -.
DR   OMA; IVLFHNN; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10951; CE4_ClCDA_like; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR   PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..239
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007147871"
FT   DOMAIN          40..221
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   239 AA;  26466 MW;  38ECACEC1F37FC0D CRC64;
     MFKSLALIAL AAISPSAICA PITSRDIPFG QVITTCTTPN TIALTFDDGP SSYTPQLLDL
     LSEYKVRATF FVLGEASQTN PQIIQRIRQE GHQVGSHTYD HTSLPTLNYD QIVQEMTSLE
     SVLQSSMGEI PTYMRPPYFD VNDLTLQVMK DLGYHVITAS IDTKDYNHNS PELISQSYDK
     FVTELNNGGN LCLAHDTKEQ TVVTLAKMML DETKSRGLTV TTVGDCLGDP EASWYRSSR
//