ID V2XWB6_MONRO Unreviewed; 412 AA.
AC V2XWB6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN ORFNames=Moror_444 {ECO:0000313|EMBL:ESK98067.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK98067.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK98067.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK98067.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK98067.1}.
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DR EMBL; AWSO01000012; ESK98067.1; -; Genomic_DNA.
DR RefSeq; XP_007842629.1; XM_007844438.1.
DR AlphaFoldDB; V2XWB6; -.
DR KEGG; mrr:Moror_444; -.
DR HOGENOM; CLU_035539_0_0_1; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000017559; 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 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 membrane {ECO:0000256|ARBA:ARBA00022475};
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:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..412
FT /note="chitin deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004712316"
FT DOMAIN 132..324
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 344..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 44763 MW; 35C64F8A34FCF705 CRC64;
MFFSSPLLAV ALVSLPNFVS AQDRTSVAQQ AAISDPAEQC RYYNYPPIAG QAVNFPKVWE
TAEILPNDAA ARAKYNEISK SMPNIAPKGN FTQTLATYNV KTDPDCWWSA TECTTAKAPG
VPSDITLVPE PQTLGYGFDD GPNCSHNAFY DYLTSQNQKA TMFFIGSNVL GWPLQAKRAV
EDGHEVCVHT WSHQAMTGLT NEQAFAEIYY TVTTHFLRLI LATLTCDIDD RIRYIVHALG
LRSILWKYDV RDTILGPNGV VDTSAVEGQY EEFIKTAQGG AFRNEGAILL AHETNNMTMS
EAMKYYPQLK TAFKHLVPIG VALNVTQPYV ENGFSQPTFE QYISGTTQTS GPAPSSNSSS
PSGSASRNNT STKPPTGNST TPAGRNGAIS LVSSSIGSIS LPAFLLYVSA IF
//
