CDA2_YEAST
ID CDA2_YEAST Reviewed; 312 AA.
AC Q06703; D6VYV2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Chitin deacetylase 2 {ECO:0000303|PubMed:9133736};
DE EC=3.5.1.41 {ECO:0000269|PubMed:11812231, ECO:0000305|PubMed:9133736};
DE Flags: Precursor;
GN Name=CDA2 {ECO:0000303|PubMed:9133736}; OrderedLocusNames=YLR308W;
GN ORFNames=L2142.1;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9133736;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<327::aid-yea96>3.0.co;2-t;
RA Mishra C., Semino C.E., McCreath K.J., de la Vega H., Jones B.J.,
RA Specht C.A., Robbins P.W.;
RT "Cloning and expression of two chitin deacetylase genes of Saccharomyces
RT cerevisiae.";
RL Yeast 13:327-336(1997).
RN [5]
RP PROTEIN SEQUENCE OF 45-55, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND GLYCOSYLATION.
RX PubMed=11812231; DOI=10.1006/prep.2001.1547;
RA Martinou A., Koutsioulis D., Bouriotis V.;
RT "Expression, purification, and characterization of a cobalt-activated
RT chitin deacetylase (Cda2p) from Saccharomyces cerevisiae.";
RL Protein Expr. Purif. 24:111-116(2002).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC residues in chitin to form chitosan and acetate (PubMed:9133736,
CC PubMed:11812231). Chitosan is a component of the spore wall
CC (PubMed:9133736). {ECO:0000269|PubMed:11812231,
CC ECO:0000269|PubMed:9133736}.
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:11812231, ECO:0000305|PubMed:9133736};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000305|PubMed:11812231};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:11812231};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for GlcNAc(6) (at 50 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11812231};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:11812231};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:11812231};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11812231}.
CC -!- SUBCELLULAR LOCATION: Prospore {ECO:0000305|PubMed:9133736}.
CC -!- DEVELOPMENTAL STAGE: Induced during sporulation.
CC {ECO:0000269|PubMed:9133736}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11812231}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; U17247; AAB67355.1; -; Genomic_DNA.
DR EMBL; AY557951; AAS56277.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09618.1; -; Genomic_DNA.
DR PIR; S51440; S51440.
DR RefSeq; NP_013411.1; NM_001182196.1.
DR AlphaFoldDB; Q06703; -.
DR SMR; Q06703; -.
DR BioGRID; 31573; 49.
DR DIP; DIP-4678N; -.
DR STRING; 4932.YLR308W; -.
DR PaxDb; Q06703; -.
DR PRIDE; Q06703; -.
DR EnsemblFungi; YLR308W_mRNA; YLR308W; YLR308W.
DR GeneID; 851017; -.
DR KEGG; sce:YLR308W; -.
DR SGD; S000004299; CDA2.
DR VEuPathDB; FungiDB:YLR308W; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR GeneTree; ENSGT00940000176634; -.
DR HOGENOM; CLU_030200_1_0_1; -.
DR InParanoid; Q06703; -.
DR OMA; TCPKLSQ; -.
DR BioCyc; MetaCyc:YLR308W-MON; -.
DR BioCyc; YEAST:YLR308W-MON; -.
DR BRENDA; 3.5.1.41; 984.
DR PRO; PR:Q06703; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06703; protein.
DR GO; GO:0042764; C:ascospore-type prospore; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004099; F:chitin deacetylase activity; IDA:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
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 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; Reference proteome; Signal; Sporulation.
FT SIGNAL 1..44
FT /evidence="ECO:0000269|PubMed:11812231"
FT CHAIN 45..312
FT /note="Chitin deacetylase 2"
FT /id="PRO_0000024827"
FT DOMAIN 118..307
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 273
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 125
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 126
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 172
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
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 213
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..300
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
SQ SEQUENCE 312 AA; 35693 MW; 4033EEFA803F6AF1 CRC64;
MRIQLNTIDL QCIIALSCLG QFVHAEANRE DLKQIDFQFP VLERAATKTP FPDWLSAFTG
LKEWPGLDPP YIPLDFIDFS QIPDYKEYDQ NHCDSVPRDS CSFDCHHCTE HDDVYTCSKL
SQTFDDGPSA STTKLLDRLK HNSTFFNLGV NIVQHPDIYQ RMQKEGHLIG SHTWSHVYLP
NVSNEKIIAQ IEWSIWAMNA TGNHTPKWFR PPYGGIDNRV RAITRQFGLQ AVLWDHDTFD
WSLLLNDSVI TEQEILQNVI NWNKSGTGLI LEHDSTEKTV DLAIKINKLI GDDQSTVSHC
VGGIDYIKEF LS
