GenomeNet

Database: UniProt
Entry: A0A3D8RU46_9HELO
LinkDB: A0A3D8RU46_9HELO
Original site: A0A3D8RU46_9HELO 
ID   A0A3D8RU46_9HELO        Unreviewed;       249 AA.
AC   A0A3D8RU46;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE            EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN   ORFNames=BP6252_05632 {ECO:0000313|EMBL:RDW77579.1};
OS   Coleophoma cylindrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Coleophoma.
OX   NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW77579.1, ECO:0000313|Proteomes:UP000256645};
RN   [1] {ECO:0000313|EMBL:RDW77579.1, ECO:0000313|Proteomes:UP000256645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP6252 {ECO:0000313|EMBL:RDW77579.1,
RC   ECO:0000313|Proteomes:UP000256645};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
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}.
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:RDW77579.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PDLM01000005; RDW77579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8RU46; -.
DR   STRING; 1849047.A0A3D8RU46; -.
DR   Proteomes; UP000256645; 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:UP000256645};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..249
FT                   /note="chitin deacetylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017826222"
FT   DOMAIN          50..233
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   249 AA;  27685 MW;  B984E25813FF8A90 CRC64;
     MCTMCAIVLC FLLIFFMILA YTVYKPPDFL IDYFQWKYPE VLFHVPLSQK TVALTLDDAP
     STSTAQVLDV LKAYGAKATF FVIGSQVDGV PGRPELLQRM HDEGHEVGNH AWNDYPSIKL
     PLPTLEEQMR NVEALLPPNP PAKDGTIPKY FRPGSGVFNK AMLGVAKALG YRIVLGSIYP
     HDPQIPHPKI NAAHVLSMVQ PGGIIIMHDR RYYSAEQLEL VLKGLAAENW KVESVGGLLR
     AAEEEAKVK
//
DBGET integrated database retrieval system