ID M5E9B1_MALS4 Unreviewed; 475 AA.
AC M5E9B1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN ORFNames=MSYG_1712 {ECO:0000313|EMBL:SHO77371.1};
OS Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO77371.1, ECO:0000313|Proteomes:UP000186303};
RN [1] {ECO:0000313|Proteomes:UP000186303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX PubMed=28100699; DOI=10.1093/nar/gkx006;
RA Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA Lehtioe J.;
RT "Proteogenomics produces comprehensive and highly accurate protein-coding
RT gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL Nucleic Acids Res. 45:2629-2643(2017).
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:0000256|ARBA:ARBA00023996};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000256|ARBA:ARBA00023996};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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DR EMBL; LT671823; SHO77371.1; -; Genomic_DNA.
DR RefSeq; XP_018740091.1; XM_018883319.1.
DR STRING; 1230383.M5E9B1; -.
DR GeneID; 30056400; -.
DR KEGG; msym:MSY001_1515; -.
DR VEuPathDB; FungiDB:MSYG_1712; -.
DR HOGENOM; CLU_035539_1_0_1; -.
DR OMA; ILHIERR; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000186303; Chromosome 3.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:UniProt.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10952; CE4_MrCDA_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR10587:SF98; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000186303}.
SQ SEQUENCE 475 AA; 52613 MW; 8EFCCCC726ED937A CRC64;
MLALEYCTFA LLLAGTTTAH IGRGVPLVSE KHVDQHHRFE RLHARDGPPT MSSWAKLKGA
QECKDYSLPS SAKLQKIYPQ GNQIAKIVDG DSEAQSVWKE IQSSGIIPSN VQVKKDTDNH
MGIDDNGYNA GSDPDCWWSA SGCTKPKAKG LSEDLFECPE PHTWGLTFDD GPNCGHNEFY
DFLKDNQLKA TLFYIGANVR DYPLQAQRGL ADGHDICLHT WSHHYMTTLS NEQVFAELYY
TLRIVKDVLG ITTRCWRPPF GDVDDRVRAI ATALGLRTII WDQDTNDWDI KPDGTKSTQQ
IDSNYQKIID LASQNKVDDK GVVVLTHEIN SDTMNEFMKM FPKVKKAYNN VVPLTACMNA
TTPYVEDDIN YPAFNDFISG KVQPKGLPDM DTYQIAVASK VDITKESDQT SPGGFSANSP
QAASASEASD DDTQNTSDSD SKDEPPSSQN ASERLRATPT VVLALAACLS VALWW
//
