ID L8WLG3_THACA Unreviewed; 876 AA.
AC L8WLG3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
GN ORFNames=AG1IA_08790 {ECO:0000313|EMBL:ELU37179.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU37179.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU37179.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(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}.
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:ELU37179.1}.
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DR EMBL; AFRT01002817; ELU37179.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WLG3; -.
DR STRING; 983506.L8WLG3; -.
DR HOGENOM; CLU_328230_0_0_1; -.
DR Proteomes; UP000011668; 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; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR10587:SF138; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 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:UP000011668};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 616..662
FT /note="NodB homology"
FT /evidence="ECO:0000259|Pfam:PF01522"
FT REGION 505..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 95189 MW; D7E0610CCCB4921C CRC64;
MGGCAHGMPI RRRLLMVHIR VQRKKDLCSA VCSADGTRIV SWNSQIEFVE LWDAQLHRSI
TYCKTGGYLY SPRVMLAQKG RRFITEVHYP ERLLNIWDTE YGAHIAGPLR LGKMLDFSPD
GLYVVCQDHN NSTIGCLHVI SVDSTDEVSK VDAPDNRHMV SAKFSWDGLS LVYNTCRTCY
LWNTRDHTIH TIITEPTWTS SLNSRIYSTD GRYLASASDD ETKQSDLMVW SLPIDKPSHV
TIRSDGWAVD SQSRVVFWVP TEIRKKTTEC SGIVIEEDSG DWLCVDYNDM VVGDEWTLGV
MIYIPSTDKI DAAEPGRHNL RVEMWGSDRC MDPRGGGSVF TSPTRDLEKL LSSQRECQQL
SVYPGLITIF DFLKKKSRSS RVAILGLDPR FYPRYLRALT SNLCLFIDLL FRCNAVQSWI
PTRQNLPAHA AASAAKELIH VREYQIYSPI MFAHTAVTLL LSLTAAGSAH GHSTQGYSHA
IRQDPHAIPP LAEITAGMPI EPAVPLSATP TAGSPAVISG APNLPPSKQP LPDMSSYPPG
GQMIPTDSPE VKEWLAEIAA SGVVIPNTTP YKPLPDDAVG QTLCSLNPEA TTAGGADGTC
WWSCSSCTRD TDVVTCPDKL TPKVLNYLAE KNLKASFYVI GANVVNHPEI LQATYLAGHE
LGWTRKVIQA VLGVTPRYFR PPYGDYDRVR AIAKGLGMTP VIWTQGFDTD DWSVNSGGVA
TELMNGYSKM LETLPTLNNG VISLQHDWYQ ATVDLAVGHF LPAALSHNPA PNFQSVIECQ
HQPLGMSYVE TSGSGTPAGP ANNATTTPAP SAPASSTTVA SGPTTGASKP TTTGTPSSTA
SGTSVNSTSA NGAVTTRGAM SRLFAVAIAV VVGVLA
//
