ID   LP9A_ASPTN              Reviewed;         360 AA.
AC   Q0CEU4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=ATEG_07790;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476604; EAU32052.1; -; Genomic_DNA.
DR   RefSeq; XP_001216411.1; XM_001216411.1.
DR   AlphaFoldDB; Q0CEU4; -.
DR   SMR; Q0CEU4; -.
DR   STRING; 341663.Q0CEU4; -.
DR   GlyCosmos; Q0CEU4; 1 site, No reported glycans.
DR   EnsemblFungi; EAU32052; EAU32052; ATEG_07790.
DR   GeneID; 4322940; -.
DR   VEuPathDB; FungiDB:ATEG_07790; -.
DR   eggNOG; ENOG502RXMI; Eukaryota.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   OMA; YIDSPPN; -.
DR   OrthoDB; 2722085at2759; -.
DR   Proteomes; UP000007963; 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..360
FT                   /note="AA9 family lytic polysaccharide monooxygenase A"
FT                   /id="PRO_0000394066"
FT   DOMAIN          322..358
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          254..293
FT                   /note="Disordered"
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        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..183
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
SQ   SEQUENCE   360 AA;  36795 MW;  0BABA36D957D8F7D CRC64;
     MKTSFGLLAL AAAAKLVNAH ATVFAVWIND EDQGLGNTAD GYIRSPPNNS PVTDVTSKDM
     TCNVNGATAA AKTLDVKAGD KITFEWHHNS RDASDDIIAS SHLGPVMVYM APTEKGSAGS
     GWVKIAEDGY SNGKWAVDTL IANRGKHSIT VPDVPAGEYL FRPEIIALHE GNREGGAQLY
     MECVQVKVTS DGSKTLPEGV SIPGTYTATD PGILFDIYNS FDSYPIPGPA VWDGSSSGSS
     SGSSKTTAAA PAATSAASAS STKAPATTAA PVQTESAKPA TSTTQAAAPT TLVTSAKPTA
     TATAGAGDSG SGSCSATAPA TGVVKMYAQC GGMNYSGSTT CESGLTCKQW NPYYHQCVKA
//