GenomeNet

Database: UniProt
Entry: A0A371DSY5_9APHY
LinkDB: A0A371DSY5_9APHY
Original site: A0A371DSY5_9APHY 
ID   A0A371DSY5_9APHY        Unreviewed;       374 AA.
AC   A0A371DSY5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE            EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
DE   Flags: Fragment;
GN   ORFNames=OH76DRAFT_1333300 {ECO:0000313|EMBL:RDX55650.1};
OS   Polyporus brumalis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Polyporus.
OX   NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX55650.1, ECO:0000313|Proteomes:UP000256964};
RN   [1] {ECO:0000313|EMBL:RDX55650.1, ECO:0000313|Proteomes:UP000256964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX55650.1,
RC   ECO:0000313|Proteomes:UP000256964};
RX   PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA   Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA   Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA   Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA   Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT   "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT   exposes the biotechnological potential of its oxidative enzymes for
RT   delignifying raw plant biomass.";
RL   Biotechnol. Biofuels 11:201-201(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   -!- 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   ---------------------------------------------------------------------------
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; KZ857382; RDX55650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371DSY5; -.
DR   STRING; 139420.A0A371DSY5; -.
DR   Proteomes; UP000256964; 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:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
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:SF135; CHITIN DEACETYLASE 3; 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   4: Predicted;
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:ARBA00023180};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000313|EMBL:RDX55650.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256964};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          116..304
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          314..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RDX55650.1"
FT   NON_TER         374
FT                   /evidence="ECO:0000313|EMBL:RDX55650.1"
SQ   SEQUENCE   374 AA;  40103 MW;  66557C49993E0F42 CRC64;
     HAAPRALPGR WYHHEDHPAY ALFRRGDTDG VTYPAVGSPE WSAGYPDTDV TKGTPQAWID
     ALNAAVKAGK IPNIPVSTST GGNPTYPQGF DPNGPEVCSA TYKCRNKEDL WDAPDGVFGS
     SFDDGPLPTS MPLYEFLKQN NVITTHFMIG SNILWNADAF TYALETLESD IAVHTWTHPY
     MTTLSNEQVI GELGWTMELI HNSTGGRLPK YWRPPYGDSD ERVRAIAKEV FGLTTVIWNQ
     DTEDWSIGES TGTTRPKVDA SLKEWITGPK SPGLIILEHE LSNNTVGAFM QAFPLIAQNG
     WKFESVARLD GGSVYQNSGD DTDDVTPQAV GVLAAASPSP PAGDSSSAAS SSTTSKPTGT
     GTVTSGSSST VSTG
//
DBGET integrated database retrieval system