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Database: UniProt
Entry: A0A0C7N8E9_9SACH
LinkDB: A0A0C7N8E9_9SACH
Original site: A0A0C7N8E9_9SACH 
ID   A0A0C7N8E9_9SACH        Unreviewed;       329 AA.
AC   A0A0C7N8E9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE            EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN   ORFNames=LALA0_S10e03796g {ECO:0000313|EMBL:CEP64160.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64160.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP64160.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64160.1,
RC   ECO:0000313|Proteomes:UP000054304};
RA   Neuveglise Cecile;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate +
CC         chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-
CC         COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57704; EC=3.5.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00023996};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC         Evidence={ECO:0000256|ARBA:ARBA00023996};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; LN736369; CEP64160.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7N8E9; -.
DR   STRING; 1245769.A0A0C7N8E9; -.
DR   HOGENOM; CLU_030200_1_0_1; -.
DR   OrthoDB; 1343935at2759; -.
DR   Proteomes; UP000054304; Unassembled WGS sequence.
DR   GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:UniProt.
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; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..329
FT                   /note="chitin deacetylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002195471"
FT   DOMAIN          125..315
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   329 AA;  37466 MW;  1F6460EA273DF5A8 CRC64;
     MKSSIFFRLQ ALHAFHLALA YTESSQNEST LPQSVGQPVG QPVGGFVSVR AGRKQTPFPQ
     WLSDFTGLKE WPGIDPPYIP MDFINFSEIP DYKRYEQGVC GVNPRESCSF DCDRCLAPDD
     IFTCHKLSQT FDDGPSLATE RLLNSLNHKT TFFNLGINIV NFPDMYQKIL DNGHLVGTHT
     WSHPFMPSLT NEQIIAQLQW SIWAMNATGN HLPKWFRPPY GAIDNRVRSI SRMFGLQAVL
     WDHDTFDWQL LTEDQTARTE EDIYREIQDW KRRGTGLILE HDGSFRTVQV GINVDKILGD
     DQLTVAECVE GIDYIKTFPS TKKSSVAIE
//
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