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Database: UniProt
Entry: A0A1Q3ELQ2_LENED
LinkDB: A0A1Q3ELQ2_LENED
Original site: A0A1Q3ELQ2_LENED 
ID   A0A1Q3ELQ2_LENED        Unreviewed;       349 AA.
AC   A0A1Q3ELQ2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, 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=LENED_010170 {ECO:0000313|EMBL:GAW08125.1};
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW08125.1, ECO:0000313|Proteomes:UP000188533};
RN   [1] {ECO:0000313|EMBL:GAW08125.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW08125.1,
RC   ECO:0000313|Proteomes:UP000188533};
RG   Lentinula edodes genome sequencing consortium;
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW08125.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW08125.1,
RC   ECO:0000313|Proteomes:UP000188533};
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RT   "A genome survey and senescence transcriptome analysis in Lentinula
RT   edodes.";
RL   Submitted (FEB-2017) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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:GAW08125.1}.
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DR   EMBL; BDGU01000586; GAW08125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3ELQ2; -.
DR   STRING; 5353.A0A1Q3ELQ2; -.
DR   Proteomes; UP000188533; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:UniProt.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10952; CE4_MrCDA_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; PTHR10587:SF98; CHITIN DEACETYLASE; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..349
FT                   /note="chitin deacetylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010344596"
FT   DOMAIN          119..317
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          59..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  38891 MW;  FCCC5A87738480DD CRC64;
     MQFPVLFHVR LLSTLICLQL LLHAGNAATI DRTSEQGEAA ITDPDQECTP YDYAPVTNQM
     NSFPERPLQS GTPYRLTSPQ TSPRSYSSSD PDCWWTYGQC TTPKLADLPP DITAAPEPST
     LGYGFDDGPN CSHNAFYDFL QSQNQKATFY FIGSNVADFP LEAQRALTDG HEICAHTWSH
     PYMTTFASED AFAELWYSVR MQMIKLVVGV TPTCWRPPYG DVDDRIRAIA NALGLQTIMW
     EYDTADASVD GKTITDQTVV DNYNSFIQKA EGGAFNSTGT ILLTHELNNF TMSEAVSFYP
     QLKSVFQYLV PVGVSLNKTQ PYLETNYSLP TFEQYISVNL APPQIQPTA
//
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