CDA3_CRYNB
ID CDA3_CRYNB Reviewed; 410 AA.
AC P0CP77; Q53I51; Q55U29; Q5KIB3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Chitin deacetylase 3 {ECO:0000305};
DE EC=3.5.1.41 {ECO:0000250|UniProtKB:P82476};
DE Flags: Precursor;
GN Name=CDA3 {ECO:0000305}; Synonyms=MP 84 {ECO:0000305};
GN OrderedLocusNames=CNBD2750;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC residues in chitin to form chitosan and acetate (By similarity).
CC Chitosan is required to anchor melanin to the cell wall, for
CC maintenance of cell wall integrity, and for proper cytokinesis (By
CC similarity). Chitosan offers an advantage during infection as it is
CC less readily detected than chitin by host immunosurveillance mechanisms
CC (By similarity). {ECO:0000250|UniProtKB:P82476}.
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:P82476};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000250|UniProtKB:P82476};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; AAEY01000020; EAL21220.1; -; Genomic_DNA.
DR RefSeq; XP_775867.1; XM_770774.1.
DR AlphaFoldDB; P0CP77; -.
DR SMR; P0CP77; -.
DR EnsemblFungi; EAL21220; EAL21220; CNBD2750.
DR GeneID; 4935664; -.
DR KEGG; cnb:CNBD2750; -.
DR VEuPathDB; FungiDB:CNBD2750; -.
DR HOGENOM; CLU_042090_2_0_1; -.
DR Proteomes; UP000001435; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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 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; Cell membrane; Cell wall biogenesis/degradation;
KW Chitin degradation; Chitin-binding; Cleavage on pair of basic residues;
KW Cobalt; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Polysaccharide degradation; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..39
FT /evidence="ECO:0000250"
FT /id="PRO_0000410197"
FT CHAIN 40..385
FT /note="Chitin deacetylase 3"
FT /id="PRO_0000410198"
FT PROPEP 386..410
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451830"
FT DOMAIN 124..314
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 289
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 131
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 132
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 183
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 187
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 225
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT LIPID 385
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 410 AA; 43993 MW; 807AEC6CFB476652 CRC64;
MYGHLSLSTL SLLAVVAAAP FHESWLQPRD SDVSQLFRRG APDPKASDYL SYYPSPGSTP
NVSTIPQAWL DKLATVQLPN VSVATANDGR PTYPNNENDG DSEICSFTDQ CYVEDDLYSP
PGEKVWALSF DDGPTDVSPA LYDYLAQNNI SSSATHFMIG GNIITSPQSV LIAIEAGGHL
AVHTWSHPYM TTLTNEQVVA ELGWTMQALS DLNGGRIPLY WRPPYGDVDN RVRAIAKGVF
GLVTVLWDSD TNDWAISDQP DQYSVASVEA YFDTLVTGNR TQGLLLLEHE LDNNTVEVFE
TEYPKAVANG WSVKNVADAF SMKWYLNSGK GNDDVVTTMS VAGTLTTAKP THTSTSVASA
TATSSASVTD SAGVSIASAA SSQESSSWPI ANRPSLFVIA CGLALAAIMV
