CDA1_YEAST
ID CDA1_YEAST Reviewed; 301 AA.
AC Q06702; D6VYV0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Chitin deacetylase 1 {ECO:0000303|PubMed:9133736};
DE EC=3.5.1.41 {ECO:0000305|PubMed:9133736};
DE Flags: Precursor;
GN Name=CDA1 {ECO:0000303|PubMed:9133736}; OrderedLocusNames=YLR307W;
GN ORFNames=L2142.2;
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).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC residues in chitin to form chitosan and acetate (PubMed:9133736).
CC Chitosan is a component of the spore wall (PubMed:9133736).
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:0000305|PubMed:9133736};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000305|PubMed:9133736};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- SUBCELLULAR LOCATION: Prospore {ECO:0000305|PubMed:9133736}.
CC -!- DEVELOPMENTAL STAGE: Induced during sporulation.
CC {ECO:0000269|PubMed:9133736}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; U17247; AAB67356.1; -; Genomic_DNA.
DR EMBL; AY557948; AAS56274.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09616.1; -; Genomic_DNA.
DR PIR; S51439; S51439.
DR RefSeq; NP_013410.1; NM_001182195.1.
DR AlphaFoldDB; Q06702; -.
DR SMR; Q06702; -.
DR BioGRID; 31572; 32.
DR STRING; 4932.YLR307W; -.
DR PaxDb; Q06702; -.
DR PRIDE; Q06702; -.
DR EnsemblFungi; YLR307W_mRNA; YLR307W; YLR307W.
DR GeneID; 851016; -.
DR KEGG; sce:YLR307W; -.
DR SGD; S000004298; CDA1.
DR VEuPathDB; FungiDB:YLR307W; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR GeneTree; ENSGT00940000176634; -.
DR HOGENOM; CLU_030200_1_0_1; -.
DR InParanoid; Q06702; -.
DR OMA; RECQAAI; -.
DR BioCyc; MetaCyc:YLR307W-MON; -.
DR BioCyc; YEAST:YLR307W-MON; -.
DR PRO; PR:Q06702; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06702; protein.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004099; F:chitin deacetylase activity; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Chitin degradation; Chitin-binding; Cobalt; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Polysaccharide degradation; Reference proteome;
KW Signal; Sporulation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..301
FT /note="Chitin deacetylase 1"
FT /id="PRO_0000024826"
FT DOMAIN 108..288
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 263
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 115
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 116
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 162
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 166
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 203
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..290
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
SQ SEQUENCE 301 AA; 34642 MW; 72FEB92E5BF5E252 CRC64;
MKIFNTIQSV LFAAFFLKQG NCLASNGSTA LMGEVDMQTP FPEWLTEFTN LTQWPGIDPP
YIPLDYINLT EVPELDRYYP GQCPKISREQ CSFDCYNCID VDDVTSCFKL SQTFDDGPAP
ATEALLKKLR QRTTFFVLGI NTVNYPDIYE HILERGHLIG THTWSHEFLP SLSNEEIVAQ
IEWSIWAMNA TGKHFPKYFR PPYGAIDNRV RAIVKQFGLT VVLWDLDTFD WKLITNDDFR
TEEEILMDIN TWKGKRKGLI LEHDGARRTV EVAIKINELI GSDQLTIAEC IGDTDYIERY
D
