CDA8_BOMMO
ID CDA8_BOMMO Reviewed; 381 AA.
AC H9JW43; A0A0F6T2X6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Chitin deacetylase 8 {ECO:0000303|PubMed:30755482};
DE Short=BmCDA8 {ECO:0000303|PubMed:30755482};
DE EC=3.5.1.41 {ECO:0000269|PubMed:30755482};
DE AltName: Full=Chitin deacetylase 17 {ECO:0000312|EMBL:AKD49099.1};
DE Flags: Precursor;
GN Name=CDA8 {ECO:0000303|PubMed:30755482};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000312|Proteomes:UP000005204};
RN [1] {ECO:0000312|EMBL:AK378243}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Midgut {ECO:0000312|EMBL:AK378243};
RX PubMed=23821615; DOI=10.1534/g3.113.006239;
RA Suetsugu Y., Futahashi R., Kanamori H., Kadono-Okuda K., Sasanuma S.,
RA Narukawa J., Ajimura M., Jouraku A., Namiki N., Shimomura M., Sezutsu H.,
RA Osanai-Futahashi M., Suzuki M.G., Daimon T., Shinoda T., Taniai K.,
RA Asaoka K., Niwa R., Kawaoka S., Katsuma S., Tamura T., Noda H.,
RA Kasahara M., Sugano S., Suzuki Y., Fujiwara H., Kataoka H., Arunkumar K.P.,
RA Tomar A., Nagaraju J., Goldsmith M.R., Feng Q., Xia Q., Yamamoto K.,
RA Shimada T., Mita K.;
RT "Large scale full-length cDNA sequencing reveals a unique genomic landscape
RT in a lepidopteran model insect, Bombyx mori.";
RL G3 (Bethesda) 3:1481-1492(2013).
RN [2] {ECO:0000312|Proteomes:UP000005204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000312|Proteomes:UP000005204};
RX PubMed=15591204; DOI=10.1126/science.1102210;
RA Xia Q., Zhou Z., Lu C., Cheng D., Dai F., Li B., Zhao P., Zha X., Cheng T.,
RA Chai C., Pan G., Xu J., Liu C., Lin Y., Qian J., Hou Y., Wu Z., Li G.,
RA Pan M., Li C., Shen Y., Lan X., Yuan L., Li T., Xu H., Yang G., Wan Y.,
RA Zhu Y., Yu M., Shen W., Wu D., Xiang Z., Yu J., Wang J., Li R., Shi J.,
RA Li H., Li G., Su J., Wang X., Li G., Zhang Z., Wu Q., Li J., Zhang Q.,
RA Wei N., Xu J., Sun H., Dong L., Liu D., Zhao S., Zhao X., Meng Q., Lan F.,
RA Huang X., Li Y., Fang L., Li C., Li D., Sun Y., Zhang Z., Yang Z.,
RA Huang Y., Xi Y., Qi Q., He D., Huang H., Zhang X., Wang Z., Li W., Cao Y.,
RA Yu Y., Yu H., Li J., Ye J., Chen H., Zhou Y., Liu B., Wang J., Ye J.,
RA Ji H., Li S., Ni P., Zhang J., Zhang Y., Zheng H., Mao B., Wang W., Ye C.,
RA Li S., Wang J., Wong G.K.-S., Yang H.;
RT "A draft sequence for the genome of the domesticated silkworm (Bombyx
RT mori).";
RL Science 306:1937-1940(2004).
RN [3] {ECO:0000312|EMBL:AKD49099.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-381.
RC TISSUE=Midgut {ECO:0000312|EMBL:AKD49099.1};
RA Zhou Y., Gu Z.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=30987273; DOI=10.3390/ijms20071679;
RA Zhang Z., Yan J., Liu Q., Zhang Y., Gong J., Hou Y.;
RT "Genome-Wide Analysis and Hormone Regulation of Chitin Deacetylases in
RT Silkworm.";
RL Int. J. Mol. Sci. 20:0-0(2019).
RN [5] {ECO:0007744|PDB:5Z34}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 19-381 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE
RP BONDS, GLYCOSYLATION AT ASN-171, AND MUTAGENESIS OF GLN-125 AND SER-241.
RX PubMed=30755482; DOI=10.1074/jbc.ra119.007597;
RA Liu L., Zhou Y., Qu M., Qiu Y., Guo X., Zhang Y., Liu T., Yang J., Yang Q.;
RT "Structural and biochemical insights into the catalytic mechanisms of two
RT insect chitin deacetylases of the carbohydrate esterase 4 family.";
RL J. Biol. Chem. 294:5774-5783(2019).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC (GlcNAc) residues in chitin. Shows activity towards the chitinous
CC oligomers GlcNAc(3), GlcNAc(4), GlcNAc(5) and GlcNAc(6), but not GlcNAc
CC or GlcNAc(2). Requires the substrate to occupy subsites 0, +1, and +2
CC for optimum catalysis. {ECO:0000269|PubMed:30755482}.
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:30755482};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:30755482};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76.7 mM for GlcNAc(3) {ECO:0000269|PubMed:30755482};
CC KM=12.3 mM for GlcNAc(4) {ECO:0000269|PubMed:30755482};
CC KM=15.7 mM for GlcNAc(5) {ECO:0000269|PubMed:30755482};
CC KM=9.2 mM for GlcNAc(6) {ECO:0000269|PubMed:30755482};
CC KM=1.926 mg/ml for ethylene glycol chitin
CC {ECO:0000269|PubMed:30755482};
CC KM=1.599 mg/ml for colloidal chitin {ECO:0000269|PubMed:30755482};
CC Note=kcat is 7.62 min(-1) for GlcNAc(3) (PubMed:30755482). kcat is
CC 5.59 min(-1) for GlcNAc(4) (PubMed:30755482). kcat is 7.52 min(-1)
CC for GlcNAc(5) (PubMed:30755482). kcat is 9.07 min(-1) for GlcNAc(6)
CC (PubMed:30755482). kcat is 0.097 min(-1) for ethylene glycol chitin
CC (PubMed:30755482). kcat is 0.012 min(-1) for colloidal chitin
CC (PubMed:30755482). {ECO:0000269|PubMed:30755482};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the midgut. Has little or no
CC expression in other tissues tested. {ECO:0000269|PubMed:30987273}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the 5th larval instar (feeding)
CC stage with a strong peak of expression in newly-molted larvae, and
CC progressively lower peaks of expression at day 3 and day 7 of the 5th
CC instar. No expression detected during the pupal stage.
CC {ECO:0000269|PubMed:30987273}.
CC -!- INDUCTION: Strongly down-regulated in response to 20-hydroxyecdysone
CC (20E). Up-regulated in response to juvenile hormone analog.
CC {ECO:0000269|PubMed:30987273}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 4 (CE4) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK378243; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BABH01025382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KP744648; AKD49099.1; -; mRNA.
DR RefSeq; XP_004923455.1; XM_004923398.2.
DR PDB; 5Z34; X-ray; 2.40 A; A=19-381.
DR PDBsum; 5Z34; -.
DR AlphaFoldDB; H9JW43; -.
DR SMR; H9JW43; -.
DR GeneID; 101735686; -.
DR KEGG; bmor:101735686; -.
DR eggNOG; ENOG502R90A; Eukaryota.
DR HOGENOM; CLU_022576_0_0_1; -.
DR InParanoid; H9JW43; -.
DR BRENDA; 3.5.1.41; 890.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IC:UniProtKB.
DR GO; GO:0004099; F:chitin deacetylase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..381
FT /note="Chitin deacetylase 8"
FT /evidence="ECO:0000255"
FT /id="PRO_5003621761"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT DISULFID 27..39
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT DISULFID 32..37
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT DISULFID 86..335
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT DISULFID 211..216
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT DISULFID 240..246
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT DISULFID 343..365
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT DISULFID 348..368
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5Z34"
FT MUTAGEN 125
FT /note="Q->A: Moderately impairs specific activity."
FT /evidence="ECO:0000269|PubMed:30755482"
FT MUTAGEN 241
FT /note="S->A: Significantly impairs specific activity."
FT /evidence="ECO:0000269|PubMed:30755482"
SQ SEQUENCE 381 AA; 43310 MW; 1CC4C574AB4E9D85 CRC64;
MKRLSVLCSL LLVAAALGTE LPLATPCDEE ACKLPDCRCS STNIPGGLRA RDTPQFVTVT
FDDGINVINI ETYREVLYGR SNSNRCPAGA TFYVSHEYTN YQLVNELYNR GFEIALHSIS
HRTPQAFWAD ATYQNLVQEI GDQKRQMAHF ASIPASAIKG VRIPFLQMSG NTSFQVMADF
DLLYDCTWPT TALTNPGLWP YTLHHESIQD CIIPPCPTAS IPGPWVLPMI SWRDLNNFPC
SMVDGCFFTP DRTDEEGWFK FILTNFERHY LGNRAPFGFF VHEWFISSNP AIKRAFVRFM
DIINNLNDVF MVNSAEVIDW VKNPVPIDRY RQQQCKFTMP SICRPSFCGP LTGTHNQLSY
YMTICNTCPR NYPWVGNPLG Q
