ID   LP9A_ASPCL              Reviewed;         353 AA.
AC   A1C4H2;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
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=ACLA_059790;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276
RC   / 107;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS026990; EAW15312.1; -; Genomic_DNA.
DR   RefSeq; XP_001276738.1; XM_001276737.1.
DR   AlphaFoldDB; A1C4H2; -.
DR   SMR; A1C4H2; -.
DR   STRING; 344612.A1C4H2; -.
DR   GlyCosmos; A1C4H2; 1 site, No reported glycans.
DR   EnsemblFungi; EAW15312; EAW15312; ACLA_059790.
DR   GeneID; 4708945; -.
DR   KEGG; act:ACLA_059790; -.
DR   VEuPathDB; FungiDB:ACLA_059790; -.
DR   eggNOG; ENOG502RXMI; Eukaryota.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   OMA; YIDSPPN; -.
DR   OrthoDB; 2722085at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..353
FT                   /note="AA9 family lytic polysaccharide monooxygenase A"
FT                   /id="PRO_0000394060"
FT   DOMAIN          315..351
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          266..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
FT   BINDING         102
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
FT   BINDING         169
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:Q1K8B6"
FT   BINDING         180
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..183
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
SQ   SEQUENCE   353 AA;  36822 MW;  CA30252C3CAB5C4C CRC64;
     MKSTFGLLAL AAAAKMAHAH ATVQAIWING VDQGAGNSAS GYIRSPPNNS PLVDVTSADM
     TCNVNGKNPV AKTLPVKAGD KITFEWHHTD RSPSDDIIAS SHRGPIMVYM APTAKGAAGN
     GWVKIAEEGY SNGKWAVDNL IANRGKHSIV VPDVPAGDYL FRPEIIALHE GNRLGGAQFY
     MECVQVKVTS NGANALPAGV SIPGAYKATD PGVHFDIYNS FSSYPMPGPA VWNGASAAGS
     APAPTAAPTQ KPVVTAAPTT LATLVKPTTT TAAAPAETDS CDGDDDDYET ETPAPQASAT
     QAPAPQRPAP QTPSGSVKEW YQCGGINYTG AKNCESGLVC KEWNPYYHQC IKA
//