CDA_PESTX
ID CDA_PESTX Reviewed; 298 AA.
AC A0A1L3THR9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Chitin deacetylase {ECO:0000303|PubMed:27901067};
DE EC=3.5.1.41 {ECO:0000269|PubMed:27901067};
DE Flags: Precursor;
GN Name=CDA {ECO:0000303|PubMed:27901067};
OS Pestalotiopsis sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=36460 {ECO:0000312|EMBL:APH81274.1};
RN [1] {ECO:0000312|EMBL:APH81274.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=GR1 {ECO:0000312|EMBL:APH81274.1};
RX PubMed=27901067; DOI=10.1038/srep38018;
RA Cord-Landwehr S., Melcher R.L., Kolkenbrock S., Moerschbacher B.M.;
RT "A chitin deacetylase from the endophytic fungus Pestalotiopsis sp.
RT efficiently inactivates the elicitor activity of chitin oligomers in rice
RT cells.";
RL Sci. Rep. 6:38018-38018(2016).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC polymers in chitin to form chitosan and acetate (PubMed:27901067). May
CC play a role in evasion of the host immune response; plant chitinases
CC liberate chitin molecules from the fungal cell wall which act as
CC elicitors of the plant immune response, deacetylation of the liberated
CC chitin neutralizes elicitor activity (PubMed:27901067).
CC {ECO:0000269|PubMed:27901067}.
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:27901067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000305|PubMed:27901067};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- ACTIVITY REGULATION: Inhibited by Fe(2+) and to a lesser extent by
CC Mn(2+). {ECO:0000269|PubMed:27901067}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:27901067};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:27901067};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27901067}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; KY024221; APH81274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L3THR9; -.
DR SMR; A0A1L3THR9; -.
DR BRENDA; 3.5.1.41; 17105.
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: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; IDA:UniProtKB.
DR GO; GO:0042783; P:evasion of host immune response; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Chitin degradation; Chitin-binding; Cobalt; Disulfide bond; Hydrolase;
KW Metal-binding; Polysaccharide degradation; Secreted; Signal; Virulence.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..298
FT /note="Chitin deacetylase"
FT /evidence="ECO:0000255"
FT /id="PRO_5012701795"
FT DOMAIN 39..222
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT DOMAIN 256..298
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 46
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 46
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 47
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 99
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 103
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 140
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT DISULFID 259..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 267..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 272..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 290..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 298 AA; 30941 MW; AE7CFB4112A22D8A CRC64;
MLAPLFAALL AGAATASPIQ ERQSSVPVGT IITACTVPNT FALTFDDGPF AYTSELLDLL
SSNGVKATFF LNGQNWGSIY DYTSVVTRMD AEGHQIGSHT WSHADLATLD AAGITSQMTQ
LETALTSILG KVPTYMRPPY FSTNALALST LGGLGYHVIN ANIDTLDYEH DDDTIGVAFT
NFQNGLASGG TVSLMHDVHA QTVHVLVQEA INAIKAKGLT PVTVGTCLGD ASANWYKSGG
GSGTTPPPAT GGPSPDDTCG GSNGYVCQNS QCCSQWGWCG TTSEYCAAGC QAAYGPCT
