ID T5A5A0_OPHSC Unreviewed; 341 AA.
AC T5A5A0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN ORFNames=OCS_06708 {ECO:0000313|EMBL:EQK97580.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQK97580.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQK97580.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQK97580.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
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; KE658158; EQK97580.1; -; Genomic_DNA.
DR AlphaFoldDB; T5A5A0; -.
DR eggNOG; ENOG502QUGV; Eukaryota.
DR HOGENOM; CLU_814076_0_0_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
DR GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProt.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:UniProt.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
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; PF08030; NAD_binding_6; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374}.
FT DOMAIN 72..184
FT /note="NodB homology"
FT /evidence="ECO:0000259|Pfam:PF01522"
FT DOMAIN 177..260
FT /note="Ferric reductase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF08030"
FT REGION 319..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 37726 MW; 00AF9F84E18CB958 CRC64;
MPRLALLFRL PTRLHRRVRR NRMATLAALA ALALVVVLPV YSAYCVYKPP RFVMEHLRAR
YPDVLFEEPG AGPDKVVALS LDDAPSRYTA DIMAALRESE ARATFFVIGA QVRGREAALR
SLVRAGHELA NHAMHDEPSR ALTDEQLERD LGQVKAMLVA AYEAEGTYGT IPDATRYDTV
VLVAGGNGAS FTFGVALDLL SRLRSDDRRH IVFIWAVKYT SCLDWFRHHL VTLETDGRVS
TMLFVTRESP GPTSSSKLPY AVTNEGELDP EKATALCFVK GWDEKGRDGL QTTRWGESSC
VPTYSVRIHR HKNTCINAAA RRPPSPSAQP PEAARGAVSA R
//
