ID   LP9A_ASPNC              Reviewed;         412 AA.
AC   A2R5N0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=AA9 family lytic polysaccharide monooxygenase A {ECO:0000250|UniProtKB:Q2US83};
DE            Short=AA9A {ECO:0000250|UniProtKB:Q2US83};
DE            EC=3.2.1.4 {ECO:0000250|UniProtKB:Q2US83};
DE   AltName: Full=Cellulase AA9A {ECO:0000305};
DE   AltName: Full=Endo-beta-1,4-glucanase AA9A {ECO:0000305};
DE            Short=Endoglucanase AA9A {ECO:0000305};
DE   AltName: Full=Glycosyl hydrolase 61 family protein AA9A {ECO:0000305};
DE   Flags: Precursor;
GN   Name=eglD; ORFNames=An15g04900;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes
CC       crystalline and amorphous polysaccharides via the oxidation of scissile
CC       alpha- or beta-(1-4)-glycosidic bonds, yielding C4 oxidation products
CC       (By similarity). 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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q2US83}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000250|UniProtKB:Q2US83};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q4WP32};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q4WP32};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2US83}.
CC   -!- DOMAIN: Has a modular structure: an endo-beta-1,4-glucanase catalytic
CC       module at the N-terminus, a linker rich in serines and threonines, and
CC       a C-terminal carbohydrate-binding module (CBM). The CBM domain is
CC       essential for binding to and subsequent oxidative degradation of
CC       polysaccharide substrate. {ECO:0000250|UniProtKB:Q7S439}.
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:0000250|UniProtKB:Q4WP32}.
CC   -!- SIMILARITY: Belongs to the polysaccharide monooxygenase AA9 family.
CC       {ECO:0000305}.
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DR   EMBL; AM270345; CAK42466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2R5N0; -.
DR   SMR; A2R5N0; -.
DR   CAZy; AA9; Auxiliary Activities 9.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   GlyCosmos; A2R5N0; 3 sites, No reported glycans.
DR   EnsemblFungi; CAK42466; CAK42466; An15g04900.
DR   VEuPathDB; FungiDB:An15g04900; -.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   Proteomes; UP000006706; Chromosome 3R.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR005103; AA9.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   PANTHER; PTHR33353:SF17; ENDO-BETA-1,4-GLUCANASE D; 1.
DR   PANTHER; PTHR33353; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12560)-RELATED; 1.
DR   Pfam; PF03443; AA9; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Copper; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..412
FT                   /note="AA9 family lytic polysaccharide monooxygenase A"
FT                   /id="PRO_5000221057"
FT   DOMAIN          373..409
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   BINDING         21
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
FT   BINDING         103
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
FT   BINDING         172
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:Q1K8B6"
FT   BINDING         183
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..186
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
SQ   SEQUENCE   412 AA;  41981 MW;  B90018CCC26771C3 CRC64;
     MKTTTYSLLA LAAASKLASA HTTVQAVWIN GEDQGLGNSA DGYIRSPPSN SPVTDVTSTD
     MTCNVNGDQA ASKTLSVKAG DVVTFEWHHS DRSDSDDIIA SSHKGPVQVY MAPTAKGSNG
     NNWVKIAEDG YHKSSDEWAT DILIANKGKH NITVPDVPAG NYLFRPEIIA LHEGNREGGA
     QFYMECVQFK VTSDGSSELP SGVSIPGVYT ATDPGILFDI YNSFDSYPIP GPDVWDGSSS
     GSSSGSSSAA AAATTSAAVA ATTPATQAAV EVSSSAAAVV ESTSSAAAAT TEAAAPVVSS
     AAPVQQATSA VTSQAQAPTT FATSSKSSKT ACKNKTKSKS KVAASSTEAV VAPAPTSSVV
     PAVSASASAS AGGVAKMYER CGGINHTGPT TCESGSVCKK WNPYYYQCVA SQ
//