ID   LP9A_ASPFN              Reviewed;         367 AA.
AC   B8MXJ7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=AFLA_077840;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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}.
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; EQ963472; EED57089.1; -; Genomic_DNA.
DR   RefSeq; XP_002372701.1; XM_002372660.1.
DR   AlphaFoldDB; B8MXJ7; -.
DR   SMR; B8MXJ7; -.
DR   STRING; 332952.B8MXJ7; -.
DR   GlyCosmos; B8MXJ7; 1 site, No reported glycans.
DR   EnsemblFungi; EED57089; EED57089; AFLA_077840.
DR   VEuPathDB; FungiDB:AFLA_003339; -.
DR   eggNOG; ENOG502RXMI; Eukaryota.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   OMA; YIDSPPN; -.
DR   OrthoDB; 2722085at2759; -.
DR   Proteomes; UP000001875; 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; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..367
FT                   /note="AA9 family lytic polysaccharide monooxygenase A"
FT                   /id="PRO_0000394062"
FT   DOMAIN          329..365
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          37..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         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        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..183
FT                   /evidence="ECO:0000250|UniProtKB:A0A223GEC9"
SQ   SEQUENCE   367 AA;  38033 MW;  0C038474B7C681F3 CRC64;
     MKSSTFGMLA LAAAAKLVSA HATVHAVWIN DVDQGEGNSE SGYIRSPPSN SPITDVTSKD
     MTCNVNNKAT AKTLEVKAGD KITFEWHHDS RSDSDDIIAS SHKGPIMVYM APTEKGTAGN
     GWVKIAEDGY TDGTWAVDTL IKNRGKHSVT VPDVAAGEYL FRPEIIALHE GNRQGGAQFY
     MECVQVKVTS SGSKTLPEGV SIPGAYTATD KGILFDIYNS FDSYPFPGPA VWDGASGSSS
     SPSASASASA PAATSAAPAP SSFTTIAKQP ATSSTEAPST ENTSTTSTIV STTAAASATA
     PATPSSTSAI ASSAASTNSV PQPSSNAGGA VKEWYQCGGL NYKGSTQCEE GLTCKKWNPY
     YYQCISA
//