ID R9NY48_PSEHS Unreviewed; 738 AA.
AC R9NY48;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN ORFNames=PHSY_001077 {ECO:0000313|EMBL:GAC93512.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC93512.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
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; DF238776; GAC93512.1; -; Genomic_DNA.
DR RefSeq; XP_012187099.1; XM_012331709.1.
DR AlphaFoldDB; R9NY48; -.
DR STRING; 1305764.R9NY48; -.
DR GeneID; 24106378; -.
DR eggNOG; ENOG502QSK3; Eukaryota.
DR HOGENOM; CLU_376034_0_0_1; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
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, ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 428..623
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 675..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 80244 MW; 0D2C8D00E4685EEE CRC64;
MISHAVARAP SDVDYRSELC IGAEPEQGSS SRTRQTSCRI QSTRSMILLL LPWPAPRIGL
MLLTWFLGTK GRLCKRRRTG AGQSCGIGVY VKLSRNRGCG LRQRKRNSLD AELAFLVHHT
RSCIGTTAQL DGCSSLASLA DRHSAPEIRP RQRFSLLLQL ASVKLCLGFA SVLSSGSSSR
PTACRNLPYR YLRAHHPRRL TTSPASLSFG LRLCSRLTFG IIGGMQNRPS LSPASARRFH
FHHHRDSYIT MKLSSTAIVA AVSLASSVAA NIGRGVPDPK NIQNLYKRHR DSGHYHKLIY
KRGSPADSAL KPRATTEPEQ AAITSAKQEC QAYYLPEMAA IQKQFPVPWD NATILPGDTE
AMNVWNAIKN SGTIPTDVKP KGKVNGDFTS FTPTYPHSDP DCWWTYNGCD TPKHPNLAAD
LTQCPEPNTW GLTFDDGPNC THNAFYDFLQ QNKQKATMFY IGSNVLDWPL EAQRGLVDGH
HICVHTWSHQ YMTAFPDEQV FAELYYTAKA IKDVVGVTPT CWRPPFGDID DRVRAIAKGL
GLESVLWTDD TDDWKILPAG TEPTASIDAN YASIIAKETN GPTAGQGNIV LTHEINGHTM
DEFMKQYPKI QAVFKHIVPL TACMNQTNPY PEKITYPNFA QYIAGNINAT GLPQGSQIKA
GDNNYQPSAA ISQTATGTQT GGISGATGAG SSSSTGSSGS SSSTTKANQS NEKSAGTSLV
VGGSLALVGL LSVVVMLV
//
