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Additional file 1: Table S1. Amino-acid identities (%) of AN1602 with other LPMOs. Alignments were performed using ClustalW using the catalytic domains of LPMO9s. Figure S1. Identification of secreted protein from Pichia culture media. Figure S1a. Protein elution profiles of AN1602 expressed in P. pastoris during gel filtration. Figure S1b. Sequence of identified protein using orbitrap mass spectrometry. Matched peptides observed in the spectrum are shown in yellow. Oxidized and alkylated residues are highlighted in green. Figure S1c. Predicted O-glycosylation sites (highlighted in green) in AN1602 from NetOGlyc server.Figure S2a. Protein sequence of AN1602. Figure S2b. Modular organization of AN1602 showing signal peptide (SP), catalytic (AA9), linker and CBM1 domains; numbers represent amino acid residues.Figure S3. MS/MS spectra of oxidized product with m/z 543 that was further fragmented. Masses are labeled based on expected fragmentation from the C4 oxidized product oxidized Glc3. Figure S4. Structure-guided homology model of AN1602 obtained from a structural overlay on the crystal structure of Ls(AA9)A (purple template, PDB code: 5ACF).