ID F8N3A1_NEUT8 Unreviewed; 246 AA.
AC F8N3A1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN ORFNames=NEUTE1DRAFT_73964 {ECO:0000313|EMBL:EGO53408.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO53408.1};
RN [1] {ECO:0000313|EMBL:EGO53408.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO53408.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) 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; GL891382; EGO53408.1; -; Genomic_DNA.
DR RefSeq; XP_009857009.1; XM_009858707.1.
DR AlphaFoldDB; F8N3A1; -.
DR GeneID; 20829690; -.
DR KEGG; nte:NEUTE1DRAFT73964; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_73964; -.
DR HOGENOM; CLU_021264_3_0_1; -.
DR OrthoDB; 197504at2759; -.
DR Proteomes; UP000008065; 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 CDD; cd10958; CE4_NodB_like_2; 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: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 Coiled coil {ECO:0000256|SAM:Coils}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..246
FT /note="chitin deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003380833"
FT DOMAIN 51..246
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT COILED 111..140
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 246 AA; 28235 MW; A4B1EFD53DF8B3D3 CRC64;
MATLILLLLI LPSILLLPFY TIYKPPSSLI RYFSQRWTDV LWRLWLPPHR KIVALTIDDA
PSDHTREILA ALKAGGVHAT FFVIGGQVRG REEILREIVR QGHELGNHGM HDEMARELAD
EELERQMKEV EGLIREAYEA EGRVWPVIEG KYYRPGSGFF SERMLSLVRK LGYRLVLGSI
YPHDAQIGYA WLNARHILSM LSPGGIIICH DRRSWTPPML RKVLPEMQRR GYKAVTVSQL
LEEATG
//
