CDA_EMENI
ID CDA_EMENI Reviewed; 237 AA.
AC Q5AQQ0; A0A1U8QU02; B3VD86; C8VR85;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chitin deacetylase {ECO:0000303|PubMed:28496100};
DE EC=3.5.1.41 {ECO:0000269|PubMed:19760058, ECO:0000269|PubMed:28496100};
DE AltName: Full=AnCDA {ECO:0000303|PubMed:28496100};
DE Flags: Precursor;
GN Name=cda {ECO:0000305}; ORFNames=ANIA_09380 {ECO:0000312|EMBL:CBF87506.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000312|Proteomes:UP000000560};
RN [1] {ECO:0000312|EMBL:ACE79177.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AF93062 {ECO:0000312|EMBL:ACE79177.1};
RX PubMed=19760058; DOI=10.1007/s12010-009-8772-z;
RA Wang Y., Song J.Z., Yang Q., Liu Z.H., Huang X.M., Chen Y.;
RT "Cloning of a heat-stable chitin deacetylase gene from Aspergillus nidulans
RT and its functional expression in Escherichia coli.";
RL Appl. Biochem. Biotechnol. 162:843-854(2010).
RN [2] {ECO:0000312|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000312|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3] {ECO:0000312|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000312|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4] {ECO:0007744|PDB:2Y8U}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 19-237 IN COMPLEX WITH COBALT,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28496100; DOI=10.1038/s41598-017-02043-1;
RA Liu Z., Gay L.M., Tuveng T.R., Agger J.W., Westereng B., Mathiesen G.,
RA Horn S.J., Vaaje-Kolstad G., van Aalten D.M.F., Eijsink V.G.H.;
RT "Structure and function of a broad-specificity chitin deacetylase from
RT Aspergillus nidulans FGSC A4.";
RL Sci. Rep. 7:1746-1746(2017).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC polymers in chitin to form chitosan and acetate.
CC {ECO:0000269|PubMed:19760058, ECO:0000269|PubMed:28496100}.
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:19760058, ECO:0000269|PubMed:28496100};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000269|PubMed:19760058, ECO:0000269|PubMed:28496100};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000303|PubMed:28496100};
CC Note=Evidence supports a metal cofactor but evidence for cobalt is
CC inconsistent. {ECO:0000269|PubMed:19760058,
CC ECO:0000269|PubMed:28496100};
CC -!- ACTIVITY REGULATION: Inhibited by metal chelator
CC ethylenediaminetetraacetic acid (EDTA). {ECO:0000269|PubMed:19760058}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.072 mM for GlcNAc(5) (at 37 degrees Celsius, pH 8 and in
CC presence of Co(2+)) {ECO:0000269|PubMed:28496100};
CC Note=kcat is 7 sec(-1) with GlcNAc(5) as substrate.
CC {ECO:0000269|PubMed:28496100};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:19760058};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:19760058};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; EU734183; ACE79177.1; -; mRNA.
DR EMBL; BN001308; CBF87506.1; -; Genomic_DNA.
DR EMBL; AACD01000172; EAA66447.1; -; Genomic_DNA.
DR RefSeq; XP_682649.1; XM_677557.1.
DR PDB; 2Y8U; X-ray; 1.99 A; A/B=19-237.
DR PDBsum; 2Y8U; -.
DR AlphaFoldDB; Q5AQQ0; -.
DR SMR; Q5AQQ0; -.
DR STRING; 162425.CADANIAP00001167; -.
DR EnsemblFungi; CBF87506; CBF87506; ANIA_09380.
DR EnsemblFungi; EAA66447; EAA66447; AN9380.2.
DR GeneID; 2867795; -.
DR KEGG; ani:AN9380.2; -.
DR VEuPathDB; FungiDB:AN9380; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_021264_11_1_1; -.
DR InParanoid; Q5AQQ0; -.
DR OMA; DLWASDW; -.
DR OrthoDB; 1132954at2759; -.
DR BRENDA; 3.5.1.41; 517.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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: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: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; Glycoprotein; Hydrolase;
KW Metal-binding; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..237
FT /note="Chitin deacetylase"
FT /evidence="ECO:0000255"
FT /id="PRO_5010241342"
FT DOMAIN 40..222
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 47
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 47
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 48
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 97
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 101
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 138
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT SITE 164
FT /note="May prevent de-N-acetylated sugar residues from
FT interacting with the active site"
FT /evidence="ECO:0000303|PubMed:28496100"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:2Y8U"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:2Y8U"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:2Y8U"
SQ SEQUENCE 237 AA; 26014 MW; 16DF188E3D652A3E CRC64;
MFATLALVFT ALASNALTTP LPLVRRVPTG QVITQCTTPN TIALTFDDGP SEYTPQLLDL
LSRYSARATF FVLGDAAAQN PGLLQRMRDE GHQVGAHTYD HVSLPSLGYD GIASQMTRLE
EVIRPALGVA PAYMRPPYLE TNELVLQVMR DLDYRVISAS VDTKDYENQD ADAIINTSFQ
LFLDQLDAGG NIVLAHDIHY WTVASLAERM LQEVNARGLI ATTVGDCLGD GEIAWYH
