CDA_AMYRO
ID CDA_AMYRO Reviewed; 421 AA.
AC P50325;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Chitin deacetylase {ECO:0000303|PubMed:8367456};
DE EC=3.5.1.41 {ECO:0000250|UniProtKB:Q6DWK3};
DE AltName: Full=MrCDA {ECO:0000303|PubMed:8367456};
DE Flags: Precursor;
GN Name=CDA {ECO:0000303|PubMed:8367456};
OS Amylomyces rouxii (Filamentous fungus) (Mucor rouxii).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Amylomyces.
OX NCBI_TaxID=29923;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-38.
RC STRAIN=ATCC 24905 / CBS 416.77 / DSM 1191;
RX PubMed=8367456; DOI=10.1073/pnas.90.17.8005;
RA Kafetzopoulos D., Thireos G., Vournakis J.N., Bouriotis V.;
RT "The primary structure of a fungal chitin deacetylase reveals the function
RT for two bacterial gene products.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8005-8008(1993).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC residues in chitin to form chitosan and acetate.
CC {ECO:0000250|UniProtKB:Q6DWK3}.
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:0000250|UniProtKB:Q6DWK3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:J9VND2}. Cell membrane
CC {ECO:0000250|UniProtKB:J9VND2}; Lipid-anchor, GPI-anchor {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; Z19109; CAA79525.1; -; mRNA.
DR PIR; A47713; A47713.
DR AlphaFoldDB; P50325; -.
DR SMR; P50325; -.
DR BRENDA; 3.5.1.41; 3460.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
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; 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 membrane; Cell wall;
KW Cell wall biogenesis/degradation; Chitin degradation; Chitin-binding;
KW Cobalt; Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..390
FT /note="Chitin deacetylase"
FT /id="PRO_0000024832"
FT PROPEP 391..421
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451832"
FT DOMAIN 157..349
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT ACT_SITE 320
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 164
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 165
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 214
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 218
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 255
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT LIPID 390
FT /note="GPI-anchor amidated threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 45972 MW; F51B7F7DA9D3206B CRC64;
MQIKTFALSA AIAQVATLAL ADTSANYWQS FTSQINPKNI SIPSIEQTSS IDPTQECAYY
TPDASLFTFN ASEWPSIWEV ATTNGMNESA EFLSVYNSID WTKAPNISVR TLDANGNLDT
TGYNTATDPD CWWTATTCTS PKISDINDDI SKCPEPETWG LTYDDGPNCS HNAFYDYLQE
QKLKASMFYI GSNVVDWPYG AMRGVVDGHH IASHTWSHPQ MTTKTNQEVL AEFYYTQKAI
KLATGLTPRY WRPPYGDIDD RVRWIASQLG LTAVIWNLDT DDWSAGVTTT VEAVEQSYSD
YIAMGTNGTF ANSGNIVLTH EINTTMSLAV ENLPKIISAY KQVIDVATCY NISHPYFEDY
EWTNVLNGTK SSATASGSAT SASASGGATT AAAHIQASTS GAMSVLPNLA LISAFIATLL
F
