ID LP9E_BOTFB Reviewed; 229 AA. AC A0A384JDH0; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2018, sequence version 1. DT 27-NOV-2024, entry version 21. DE RecName: Full=AA9 family lytic polysaccharide monooxygenase E {ECO:0000303|PubMed:35080440}; DE Short=AA9E {ECO:0000303|PubMed:35080440}; DE EC=1.14.99.56 {ECO:0000305|PubMed:35080440}; DE AltName: Full=Endo-1,4-beta-glucanase AA9E {ECO:0000305}; DE Short=Endoglucanase AA9E {ECO:0000305}; DE AltName: Full=Glycosyl hydrolase 61 family protein AA9E {ECO:0000305}; DE Flags: Precursor; GN Name=AA9E {ECO:0000303|PubMed:35080440}; ORFNames=BCIN_03g05890; OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis OS cinerea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=332648; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10; RX PubMed=23104368; DOI=10.1128/ec.00164-12; RA Staats M., van Kan J.A.L.; RT "Genome update of Botrytis cinerea strains B05.10 and T4."; RL Eukaryot. Cell 11:1413-1414(2012). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10; RX PubMed=26913498; DOI=10.1111/mpp.12384; RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L., RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D., RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.; RT "A gapless genome sequence of the fungus Botrytis cinerea."; RL Mol. Plant Pathol. 18:75-89(2017). RN [4] RP IDENTIFICATION, INDUCTION, AND FUNCTION. RX PubMed=35080440; DOI=10.1128/spectrum.02697-21; RA Srivastava A., Nagar P., Rathore S., Adlakha N.; RT "The Linker Region Promotes Activity and Binding Efficiency of Modular LPMO RT towards Polymeric Substrate."; RL Microbiol. Spectr. 10:e0269721-e0269721(2022). CC -!- FUNCTION: Lytic polysaccharide monooxygenase (LPMO) that depolymerizes CC crystalline and amorphous polysaccharides via the oxidation of scissile CC alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation CC products (Probable). Catalysis by LPMOs requires the reduction of the CC active-site copper from Cu(II) to Cu(I) by a reducing agent and CC H(2)O(2) or O(2) as a cosubstrate (Probable). CC {ECO:0000305|PubMed:35080440}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = 4- CC dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D- CC glucosyl]m + acceptor + H2O.; EC=1.14.99.56; CC Evidence={ECO:0000305|PubMed:35080440}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000305|PubMed:35080440}; CC Note=Binds 1 copper ion per subunit. {ECO:0000305|PubMed:35080440}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:35080440}. CC -!- INDUCTION: Expression is increased 4-fold in cellulose-inducible CC conditions (in Avicel- and wheat bran-containing complex medium). CC {ECO:0000269|PubMed:35080440}. CC -!- BIOTECHNOLOGY: Lignocellulose is the most abundant polymeric composite CC on Earth and is a recalcitrant but promising renewable substrate for CC industrial biotechnology applications. Together with cellobiose CC dehydrogenases (CDHs) an enzymatic system capable of oxidative CC cellulose cleavage is formed, which increases the efficiency of CC cellulases and put LPMOs at focus of biofuel research. CC {ECO:0000305|PubMed:35080440}. CC -!- SIMILARITY: Belongs to the polysaccharide monooxygenase AA9 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP009807; ATZ48364.1; -; Genomic_DNA. DR AlphaFoldDB; A0A384JDH0; -. DR SMR; A0A384JDH0; -. DR EnsemblFungi; Bcin03g05890.1; Bcin03p05890.1; Bcin03g05890. DR VEuPathDB; FungiDB:Bcin03g05890; -. DR OrthoDB; 2722085at2759; -. DR Proteomes; UP000001798; Chromosome bcin03. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR CDD; cd21175; LPMO_AA9; 1. DR Gene3D; 2.70.50.70; -; 1. DR InterPro; IPR049892; AA9. DR InterPro; IPR005103; AA9_LPMO. DR PANTHER; PTHR33353:SF9; ENDOGLUCANASE II; 1. DR PANTHER; PTHR33353; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12560)-RELATED; 1. DR Pfam; PF03443; AA9; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Cellulose degradation; Copper; Disulfide bond; KW Glycoprotein; Metal-binding; Monooxygenase; Oxidoreductase; KW Polysaccharide degradation; Reference proteome; Secreted; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..229 FT /note="AA9 family lytic polysaccharide monooxygenase E" FT /evidence="ECO:0000255" FT /id="PRO_5017037546" FT BINDING 20 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000250|UniProtKB:G2R6N0" FT BINDING 99 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000250|UniProtKB:Q4WP32" FT BINDING 164 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:Q1K8B6" FT BINDING 173 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:Q1K8B6" FT BINDING 175 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000250|UniProtKB:G2R6N0" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 217 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 57..178 FT /evidence="ECO:0000250|UniProtKB:Q7Z9M7" SQ SEQUENCE 229 AA; 23945 MW; DD28E9D3DC16503A CRC64; MRSSDITFVL LSVVATVRSH ATFQELWINS VDQVGSCVRL PPTNSPITDL TSTDLRCNVG GTVGVSGVCS VAAGGNVTVE MHQQPGDRSC ANEAIGGAHY GPVILYMSKV SNAATDTGSG SWFKVDQEGY DQTLNANCGK RSFTIPSTLA PGDYLLRAEV IALHVAGSVG GAQLYMSCFQ LRVTGSGSKN PTGVLFPGAY SATDPGILIN IYQTINNYTI PGPTTVFTG //