CDA1_BOMMO
ID CDA1_BOMMO Reviewed; 539 AA.
AC H9J9M0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Chitin deacetylase 1 {ECO:0000303|PubMed:30755482};
DE Short=BmCDA1 {ECO:0000303|PubMed:30755482};
DE EC=3.5.1.41 {ECO:0000269|PubMed:30755482};
DE Flags: Precursor;
GN Name=CDA1 {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|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 [2] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
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 [3] {ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 161-539 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
RP CPAP3-A1, DISULFIDE BONDS, GLYCOSYLATION AT ASN-244 AND ASN-296, AND
RP MUTAGENESIS OF ASP-205.
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 residues in chitin. {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 -!- ACTIVITY REGULATION: Binding to the accessory protein CPAP3-A1 is
CC essential for chitinase activity. {ECO:0000269|PubMed:30755482}.
CC -!- SUBUNIT: Interacts with CPAP3-A1. {ECO:0000269|PubMed:30755482}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in epidermis and head. Moderate
CC expression levels in fat body, Malpighian tubule, testis and midgut.
CC Low expression in silk gland and ovary. {ECO:0000269|PubMed:30987273}.
CC -!- DEVELOPMENTAL STAGE: Shows highest expression during pupal stages, with
CC a peak during pupal day 1. Has relatively low expresson during larval
CC development. {ECO:0000269|PubMed:30987273}.
CC -!- INDUCTION: Up-regulated in response to 20-hydroxyecdysone (20E) and
CC juvenile hormone analog. Also up-regulated in response to the
CC transcription factors BRC-Z2 and POUM2. {ECO:0000269|PubMed:30987273}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in delayed
CC pupation. {ECO:0000269|PubMed:30987273}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 4 (CE4) family.
CC {ECO:0000305}.
CC -!- CAUTION: Has no detectable chitin esterase activity in purified form.
CC Enzymatic activity is detected in the presence of CPAP3-A1, or B.mori
CC molting fluid. However, it is unclear whether this protein functions as
CC a chitin esterase in vivo. {ECO:0000269|PubMed:30755482}.
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DR EMBL; BABH01005057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BABH01005058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004929283.1; XM_004929226.2.
DR PDB; 5ZNS; X-ray; 2.40 A; A=161-539.
DR PDB; 5ZNT; X-ray; 1.98 A; A=161-539.
DR PDBsum; 5ZNS; -.
DR PDBsum; 5ZNT; -.
DR AlphaFoldDB; H9J9M0; -.
DR SMR; H9J9M0; -.
DR STRING; 7091.BGIBMGA006213-TA; -.
DR EnsemblMetazoa; BGIBMGA006213-RA; BGIBMGA006213-TA; BGIBMGA006213.
DR GeneID; 101740647; -.
DR KEGG; bmor:101740647; -.
DR eggNOG; ENOG502QQP5; Eukaryota.
DR HOGENOM; CLU_022576_1_0_1; -.
DR InParanoid; H9J9M0; -.
DR OMA; EMHRKGH; -.
DR OrthoDB; 1060206at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IC:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
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 CDD; cd00112; LDLa; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR SUPFAM; SSF57625; SSF57625; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..539
FT /note="Chitin deacetylase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003621239"
FT DOMAIN 42..104
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 121..157
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNT"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT DISULFID 80..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 122..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 129..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 141..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 168..180
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT DISULFID 173..178
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT DISULFID 230..489
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT DISULFID 354..361
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT DISULFID 391..397
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT DISULFID 497..520
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT DISULFID 503..523
FT /evidence="ECO:0000269|PubMed:30755482,
FT ECO:0007744|PDB:5ZNS, ECO:0007744|PDB:5ZNT"
FT MUTAGEN 205
FT /note="D->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:30755482"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5ZNT"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:5ZNT"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5ZNS"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 277..294
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:5ZNT"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:5ZNS"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 403..418
FT /evidence="ECO:0007829|PDB:5ZNT"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 438..454
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:5ZNT"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:5ZNT"
FT TURN 487..490
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:5ZNT"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:5ZNT"
SQ SEQUENCE 539 AA; 61429 MW; 07BB538D4ABA59B3 CRC64;
MARYARVATL AACLLFACAL ADGHRWRRQA DETAKKDESL EQELCKDKDA GEWFRLVAGE
GDNCRDVIQC TASGIQAIRC PAGLFFDIEK QTCDWKDAVK NCKLKNKERK IKPLLYTEEP
LCQDGFLACG DSTCIERGLF CNGEKDCGDG SDENSCDIDN DPNRAPPCDS SQCVLPDCFC
SEDGTVIPGD LPARDVPQMI TITFDDAINN NNIELYKEIF NGKRKNPNGC DIKATYFVSH
KYTNYSAVQE THRKGHEIAV HSITHNDDER FWSNATVDDW GKEMAGMRVI IEKFSNITDN
SVVGVRAPYL RVGGNNQFTM MEEQAFLYDS TITAPLSNPR LCPYTMYFRM PHRCHGNLQS
CPTRSHAVWE MVMNELDRRE DPSNDEYLPG CAMVDSCSNI LTGDQFYNFL NHNFDRHYEQ
NRAPLGLYFH AAWLKNNPEF LEAFLYWIDE ILQSHNDVYF VTMTQVIQWV QNPRTVTEAK
NFEPWREKCS VEGNPACWVP HSCKLTSKEV PGETINLQTC LRCPVNYPWL NDPTGDGHY
