ID   A0A2X0L1A1_9BASI        Unreviewed;       422 AA.
AC   A0A2X0L1A1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE            EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN   ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR5-2G07869
GN   {ECO:0000313|EMBL:SCZ92451.1};
OS   Microbotryum saponariae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ92451.1, ECO:0000313|Proteomes:UP000249723};
RN   [1] {ECO:0000313|Proteomes:UP000249723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMWP01000018; SCZ92451.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0L1A1; -.
DR   STRING; 289078.A0A2X0L1A1; -.
DR   Proteomes; UP000249723; 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   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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
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:ARBA00022622};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249723};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..422
FT                   /note="chitin deacetylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030060133"
FT   DOMAIN          109..301
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   422 AA;  44804 MW;  F011E48660012F4A CRC64;
     MFSHVTLLLV VASVVTASTP HPLYERQSRT YPEPLKVGPQ PLQVWIDTYN QAKAAGKIPS
     FAPATLSGGE PVYASGVDTG VKGVCSWTLA HCFNTNKTGA YDIEDGPTGH VGVSFDDGPT
     PASPVLYKFL QSKNLAATHF FIGSNIVNNP DIFDQAVKSG GHIAVHTWAH KLMTTLTDMQ
     VLGELGWTIQ IIYDRAGVVP RFWRPPYGDI DNRVRAIAKE VFGLEHAVIW NHDTNDWCLS
     EGGGSDWTPS SDAELDQELN GFYNGPKSPG LIILEHEVTS RSVGAFMRTF PTLISKGWIP
     QSIPDLFSQP WYLNAAGPSD TPTRGFVVGS GDLPNVNNAA VNLTSSSSSA AVARSSSTSI
     VTQTRSSARA SSAVGSSISG QGTATAAAQA AASSKTASGA AMLSSSIFLP VSLMIFASLR
     LF
//