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   02-OCT-2024, entry version 20.
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}.
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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:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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
//