CDA_ARTBC
ID CDA_ARTBC Reviewed; 371 AA.
AC D4AM78;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Chitin deacetylase {ECO:0000250|UniProtKB:Q06702};
DE EC=3.5.1.41 {ECO:0000250|UniProtKB:Q06702};
DE Flags: Precursor;
GN Name=CDA {ECO:0000305}; ORFNames=ARB_04768;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000312|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC residues in chitin to form chitosan and acetate.
CC {ECO:0000250|UniProtKB:Q6DWK3}.
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:0000250|UniProtKB:Q6DWK3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; ABSU01000002; EFE35834.1; -; Genomic_DNA.
DR RefSeq; XP_003016479.1; XM_003016433.1.
DR AlphaFoldDB; D4AM78; -.
DR SMR; D4AM78; -.
DR STRING; 663331.D4AM78; -.
DR EnsemblFungi; EFE35834; EFE35834; ARB_04768.
DR GeneID; 9521961; -.
DR KEGG; abe:ARB_04768; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_050708_0_0_1; -.
DR OMA; RDYDFLQ; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; 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 InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; Cobalt;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..371
FT /note="Chitin deacetylase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434493"
FT DOMAIN 168..353
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT REGION 73..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 327
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 175
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 176
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 228
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 232
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 270
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT SITE 296
FT /note="May prevent de-N-acetylated sugar residues from
FT interacting with the active site"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 164..358
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
SQ SEQUENCE 371 AA; 40836 MW; 20DFB597AF6769BA CRC64;
MLCRLFTLFI TAALACCVAA IPLQGQQSNS IIERTPGRWP WHPHRPRPHH PRPHWPFPKP
HWPKPHWPKP HWPKPEPEPT AVPTMAPEPT TVPPTEPSGT YPPETTPTVE PTVVPTDVPT
TFPSMTPTAD PTVAPTGTSV PTGVPTGVPP MPGTIPFGTV INQCTVNGTI ALTFDDGPYD
YTGPLLDIFA KNGAKGTFFV NAMNFGNIMD YADVIKRMYK EGHMLGSHTY SHADLSKLNS
TGIALEMKKL DDILAPIIDG NRPTYMRAPY FAYSDTVSKT MAELKYHMID ANIDTKDYEH
ATPDGVPISV ENFKKGLEAG GTITLCHDVH QTTVELLIQQ LLDEIKKRGL RAVTVGECLG
DPQANWYRPA Q
