CDA_COLLN
ID CDA_COLLN Reviewed; 248 AA.
AC Q6DWK3;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chitin deacetylase {ECO:0000303|PubMed:8987657};
DE EC=3.5.1.41 {ECO:0000269|PubMed:16878976};
DE AltName: Full=ClCDA {ECO:0000303|PubMed:16878976};
DE Flags: Precursor;
GN Name=CDA {ECO:0000303|PubMed:15555935};
OS Colletotrichum lindemuthianum (Bean anthracnose fungus) (Glomerella
OS lindemuthiana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=290576 {ECO:0000312|EMBL:AAT68493.1};
RN [1] {ECO:0000312|EMBL:AAT68493.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS LEU-7; ALA-57; LYS-69;
RP 125-HIS-VAL-126; ASP-189; GLY-194 AND ARG-219.
RC STRAIN=UPS9;
RX PubMed=15555935; DOI=10.1016/j.pep.2004.08.012;
RA Shrestha B., Blondeau K., Stevens W.F., Hegarat F.L.;
RT "Expression of chitin deacetylase from Colletotrichum lindemuthianum in
RT Pichia pastoris: purification and characterization.";
RL Protein Expr. Purif. 38:196-204(2004).
RN [2] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RC STRAIN=DSM 63144;
RX PubMed=7592838; DOI=10.1074/jbc.270.44.26286;
RA Tsigos I., Bouriotis V.;
RT "Purification and characterization of chitin deacetylase from
RT Colletotrichum lindemuthianum.";
RL J. Biol. Chem. 270:26286-26291(1995).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC STRAIN=ATCC 56676;
RX PubMed=8987657; DOI=10.1271/bbb.60.1598;
RA Tokuyasu K., Ohnishi-Kameyama M., Hayashi K.;
RT "Purification and characterization of extracellular chitin deacetylase from
RT Colletotrichum lindemuthianum.";
RL Biosci. Biotechnol. Biochem. 60:1598-1603(1996).
RN [4] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 56676;
RX PubMed=9373940; DOI=10.1016/s0008-6215(97)00166-3;
RA Tokuyasu K., Ono H., Ohnishi-Kameyama M., Hayashi K., Mori Y.;
RT "Deacetylation of chitin oligosaccharides of dp 2-4 by chitin deacetylase
RT from Colletotrichum lindemuthianum.";
RL Carbohydr. Res. 303:353-358(1997).
RN [5] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 56676;
RX PubMed=10629946; DOI=10.1016/s0008-6215(99)00213-x;
RA Tokuyasu K., Ono H., Hayashi K., Mori Y.;
RT "Reverse hydrolysis reaction of chitin deacetylase and enzymatic synthesis
RT of beta-D-GlcNAc-(1-->4)-GlcN from chitobiose.";
RL Carbohydr. Res. 322:26-31(1999).
RN [6] {ECO:0000305}
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 56676;
RX PubMed=10518926; DOI=10.1016/s0014-5793(99)01113-8;
RA Tokuyasu K., Kaneko S., Hayashi K., Mori Y.;
RT "Production of a recombinant chitin deacetylase in the culture medium of
RT Escherichia coli cells.";
RL FEBS Lett. 458:23-26(1999).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PROTEIN SEQUENCE OF 27-32.
RC STRAIN=ATCC 56676;
RX PubMed=16232493; DOI=10.1016/s1389-1723(99)80088-7;
RA Tokuyasu K., Ohnishi-Kameyama M., Hayashi K., Mori Y.;
RT "Cloning and expression of chitin deacetylase gene from a Deuteromycete,
RT Colletotrichum lindemuthianum.";
RL J. Biosci. Bioeng. 87:418-423(1999).
RN [8] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 56676;
RX PubMed=10913295; DOI=10.1021/bi0005355;
RA Tokuyasu K., Mitsutomi M., Yamaguchi I., Hayashi K., Mori Y.;
RT "Recognition of chitooligosaccharides and their N-acetyl groups by putative
RT subsites of chitin deacetylase from a deuteromycete, Colletotrichum
RT lindemuthianum.";
RL Biochemistry 39:8837-8843(2000).
RN [9] {ECO:0000305}
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 56676;
RX PubMed=10795812; DOI=10.1016/s0008-6215(00)00004-5;
RA Tokuyasu K., Ono H., Mitsutomi M., Hayashi K., Mori Y.;
RT "Synthesis of a chitosan tetramer derivative, beta-D-GlcNAc-(1-->4)-beta-D-
RT GlcNAc-(1-->4)-beta-D-GlcNAc-(1-->4)-D-Glc N through a partial N-
RT acetylation reaction by chitin deacetylase.";
RL Carbohydr. Res. 325:211-215(2000).
RN [10] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 56676;
RX PubMed=12775215; DOI=10.1042/bj20030204;
RA Hekmat O., Tokuyasu K., Withers S.G.;
RT "Subsite structure of the endo-type chitin deacetylase from a
RT deuteromycete, Colletotrichum lindemuthianum: an investigation using
RT steady-state kinetic analysis and MS.";
RL Biochem. J. 374:369-380(2003).
RN [11] {ECO:0000305}
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 56676;
RX PubMed=23572758; DOI=10.1007/s13197-011-0252-0;
RA Suresh P.V., Sachindra N.M., Bhaskar N.;
RT "Solid state fermentation production of chitin deacetylase by
RT Colletotrichum lindemuthianum ATCC 56676 using different substrates.";
RL J. Food Sci. Technol. 48:349-356(2011).
RN [12] {ECO:0000305}
RP BIOTECHNOLOGY.
RX PubMed=22814492; DOI=10.4014/jmb.1112.12026;
RA Kang L., Chen X., Zhai C., Ma L.;
RT "Synthesis and high expression of chitin deacetylase from Colletotrichum
RT lindemuthianum in Pichia pastoris GS115.";
RL J. Microbiol. Biotechnol. 22:1202-1207(2012).
RN [13] {ECO:0007744|PDB:2IW0}
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH ZINC AND ACETATE
RP PRODUCT, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, AND DISULFIDE BONDS.
RC STRAIN=UPS9;
RX PubMed=16878976; DOI=10.1021/bi0606694;
RA Blair D.E., Hekmat O., Schuttelkopf A.W., Shrestha B., Tokuyasu K.,
RA Withers S.G., van Aalten D.M.;
RT "Structure and mechanism of chitin deacetylase from the fungal pathogen
RT Colletotrichum lindemuthianum.";
RL Biochemistry 45:9416-9426(2006).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC polymers in chitin to form chitosan and acetate (PubMed:15555935,
CC PubMed:7592838, PubMed:8987657, PubMed:9373940, PubMed:16232493,
CC PubMed:16878976). May play a role in evasion of the host immune
CC response; plant chitinases liberate chitin molecules from the fungal
CC cell wall which act as elicitors of the plant immune response,
CC deacetylation of the liberated chitin neutralizes elicitor activity
CC (PubMed:8987657, PubMed:10913295). {ECO:0000269|PubMed:15555935,
CC ECO:0000269|PubMed:16232493, ECO:0000269|PubMed:16878976,
CC ECO:0000269|PubMed:7592838, ECO:0000269|PubMed:8987657,
CC ECO:0000269|PubMed:9373940, ECO:0000303|PubMed:10913295,
CC ECO:0000303|PubMed:8987657}.
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:0000269|PubMed:10518926, ECO:0000269|PubMed:10629946,
CC ECO:0000269|PubMed:10795812, ECO:0000269|PubMed:10913295,
CC ECO:0000269|PubMed:12775215, ECO:0000269|PubMed:15555935,
CC ECO:0000269|PubMed:16232493, ECO:0000269|PubMed:16878976,
CC ECO:0000269|PubMed:8987657, ECO:0000269|PubMed:9373940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000269|PubMed:10913295, ECO:0000269|PubMed:15555935,
CC ECO:0000269|PubMed:16232493, ECO:0000269|PubMed:16878976,
CC ECO:0000269|PubMed:8987657, ECO:0000269|PubMed:9373940};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:8987657, ECO:0000303|PubMed:15555935,
CC ECO:0000305|PubMed:16878976};
CC Note=Some evidence supports a zinc cofactor.
CC {ECO:0000269|PubMed:16878976, ECO:0000269|PubMed:8987657};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.4 mM for GlcNAc(2) (at 45 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:8987657};
CC KM=18 mM for GlcNAc(2) (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:12775215, ECO:0000269|PubMed:16878976};
CC KM=11 mM for GlcNAc(3) (at 45 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:8987657};
CC KM=0.66 mM for GlcNAc(3) (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:16878976};
CC KM=4.3 mM for GlcNAc(3) (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:12775215, ECO:0000269|PubMed:16878976};
CC KM=8.9 mM for GlcNAc(4) (at 60 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:15555935};
CC KM=0.6 mM for GlcNAc(4) (at 45 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:8987657};
CC KM=0.125 mM for GlcNAc(4) (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:12775215, ECO:0000269|PubMed:16878976};
CC KM=5.7 mM for GlcNAc(5) (at 60 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:15555935};
CC KM=0.414 mM for GlcNAc(5) (at 45 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:8987657};
CC KM=0.079 mM for GlcNAc(5) (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:12775215};
CC KM=1.5 mM for GlcNAc(6) (at 60 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:15555935};
CC KM=0.048 mM for GlcNAc(6) (at 30 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:12775215};
CC Note=kcat is: 8.52 sec(-1) with GlcNAc(2) as substrate (at 45 degrees
CC Celsius and pH 8.5), 11 sec(-1) with GlcNAc(2) as substrate (at 30
CC degrees Celsius and pH 8.5), 5.94 sec(-1) with GlcNAc(3) as substrate
CC (at 45 degrees Celsius and pH 8.5), 1.53 sec(-1) with GlcNAc(3) as
CC substrate (at 37 degrees Celsius and pH 7), 6 sec(-1) with GlcNAc(3)
CC as substrate (at 30 degrees Celsius and pH 8.5), 96.9 sec(-1) with
CC GlcNAc(4) as substrate (at 45 degrees Celsius and pH 8.5), 7 sec(-1)
CC with GlcNAc(4) as substrate (at 30 degrees Celsius and pH 8.5), 7
CC sec(-1) with GlcNAc(5) as substrate (at 30 degrees Celsius and pH
CC 8.5), 5.4 sec(-1) with GlcNAc(6) as substrate (at 30 degrees Celsius
CC and pH 8.5). {ECO:0000269|PubMed:12775215,
CC ECO:0000269|PubMed:16878976, ECO:0000269|PubMed:8987657};
CC pH dependence:
CC Optimum pH is 8 (PubMed:15555935). Optimum pH is 8.5
CC (PubMed:7592838). Optimum pH is 11-12 (PubMed:8987657).
CC {ECO:0000269|PubMed:15555935, ECO:0000269|PubMed:7592838,
CC ECO:0000269|PubMed:8987657};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius (PubMed:15555935,
CC PubMed:8987657). Optimum temperature is 50 degrees Celsius
CC (PubMed:7592838). {ECO:0000269|PubMed:15555935,
CC ECO:0000269|PubMed:7592838, ECO:0000269|PubMed:8987657};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7592838}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7592838,
CC ECO:0000269|PubMed:8987657}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7592838,
CC ECO:0000269|PubMed:8987657}.
CC -!- BIOTECHNOLOGY: Recombinant chitin deacetylase could be used to produce
CC chitosan oligomers or polymers from chitin, this reaction is currently
CC achieved by thermochemical alkaline deacetylation. Due to its
CC properties, chitosan has many biological and industrial applications
CC such as the production of films or fibers.
CC {ECO:0000303|PubMed:22814492, ECO:0000303|PubMed:23572758}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; AY633657; AAT68493.1; -; Genomic_DNA.
DR PDB; 2IW0; X-ray; 1.81 A; A=1-248.
DR PDBsum; 2IW0; -.
DR AlphaFoldDB; Q6DWK3; -.
DR SMR; Q6DWK3; -.
DR CLAE; CDA4A_COLLI; -.
DR BioCyc; MetaCyc:MON-16910; -.
DR BRENDA; 3.5.1.41; 1572.
DR SABIO-RK; Q6DWK3; -.
DR EvolutionaryTrace; Q6DWK3; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004099; F:chitin deacetylase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Chitin degradation; Chitin-binding; Cobalt; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Polysaccharide degradation; Secreted; Signal; Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:16232493"
FT CHAIN 27..248
FT /note="Chitin deacetylase"
FT /id="PRO_5004273461"
FT DOMAIN 42..232
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:16878976"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:16878976"
FT BINDING 49
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:16878976,
FT ECO:0007744|PDB:2IW0"
FT BINDING 50
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305|PubMed:16878976,
FT ECO:0007744|PDB:2IW0"
FT BINDING 104
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305|PubMed:16878976,
FT ECO:0007744|PDB:2IW0"
FT BINDING 108
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305|PubMed:16878976,
FT ECO:0007744|PDB:2IW0"
FT BINDING 145
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:16878976,
FT ECO:0007744|PDB:2IW0"
FT SITE 171
FT /note="Prevents de-N-acetylated sugar residues from
FT interacting with the active site"
FT /evidence="ECO:0000303|PubMed:16878976"
FT DISULFID 38..237
FT /evidence="ECO:0000269|PubMed:16878976,
FT ECO:0007744|PDB:2IW0"
FT DISULFID 148..152
FT /evidence="ECO:0000269|PubMed:16878976,
FT ECO:0007744|PDB:2IW0"
FT VARIANT 7
FT /note="F -> L (in strain: ATCC 56676)"
FT /evidence="ECO:0000269|PubMed:15555935"
FT VARIANT 57
FT /note="P -> A (in strain: ATCC 56676)"
FT /evidence="ECO:0000269|PubMed:15555935"
FT VARIANT 69
FT /note="R -> K (in strain: ATCC 56676)"
FT /evidence="ECO:0000269|PubMed:15555935"
FT VARIANT 125..126
FT /note="HV -> QL (in strain: ATCC 56676)"
FT /evidence="ECO:0000269|PubMed:15555935"
FT VARIANT 189
FT /note="N -> D (in strain: ATCC 56676)"
FT /evidence="ECO:0000269|PubMed:15555935"
FT VARIANT 194
FT /note="A -> G (in strain: ATCC 56676)"
FT /evidence="ECO:0000269|PubMed:15555935"
FT VARIANT 219
FT /note="K -> R (in strain: ATCC 56676)"
FT /evidence="ECO:0000269|PubMed:15555935"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 116..134
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2IW0"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2IW0"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:2IW0"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2IW0"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2IW0"
SQ SEQUENCE 248 AA; 27041 MW; 1999F03F87AB4DAC CRC64;
MHFSTLFGAA ATAALAGSTN ASPLARRQVP VGTPILQCTQ PGLVALTYDD GPFTFTPQLL
DILKQNDVRA TFFVNGNNWA NIEAGSNPDT IRRMRADGHL VGSHTYAHPD LNTLSSADRI
SQMRHVEEAT RRIDGFAPKY MRAPYLSCDA GCQGDLGGLG YHIIDTNLDT KDYENNKPET
THLSAEKFNN ELSADVGANS YIVLSHDVHE QTVVSLTQKL IDTLKSKGYR AVTVGECLGD
APENWYKA
