ID A0A9Q0AQX4_9PEZI Unreviewed; 390 AA.
AC A0A9Q0AQX4;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE RecName: Full=lytic cellulose monooxygenase (C4-dehydrogenating) {ECO:0000256|ARBA:ARBA00047174};
DE EC=1.14.99.56 {ECO:0000256|ARBA:ARBA00047174};
GN ORFNames=JX265_006325 {ECO:0000313|EMBL:KAI1870155.1};
OS Neoarthrinium moseri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Amphisphaeriales; Apiosporaceae; Neoarthrinium.
OX NCBI_TaxID=1658444 {ECO:0000313|EMBL:KAI1870155.1, ECO:0000313|Proteomes:UP000829685};
RN [1] {ECO:0000313|EMBL:KAI1870155.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TUCIM 5799 {ECO:0000313|EMBL:KAI1870155.1};
RA Vignolle G.A., Hochenegger N., Mach R.L., Mach-Aigner A.R.,
RA Javad Rahimi M., Salim K.A., Chan C.M., Lim L.B.L., Cai F.,
RA Druzhinina I.S., U'Ren J.M., Derntl C.;
RT "Revisited historic fungal species revealed as producer of novel bioactive
RT compounds through whole genome sequencing and comparative genomics.";
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = 4-
CC dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-
CC glucosyl]m + acceptor + H2O.; EC=1.14.99.56;
CC Evidence={ECO:0000256|ARBA:ARBA00045077};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide monooxygenase AA9 family.
CC {ECO:0000256|ARBA:ARBA00044502}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAI1870155.1}.
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DR EMBL; JAFIMR010000014; KAI1870155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q0AQX4; -.
DR OrthoDB; 4849160at2759; -.
DR Proteomes; UP000829685; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; IPR049892; AA9.
DR InterPro; IPR005103; AA9_LPMO.
DR InterPro; IPR000254; CBD.
DR InterPro; IPR035971; CBD_sf.
DR PANTHER; PTHR33353:SF1; 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 {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000829685};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..390
FT /note="lytic cellulose monooxygenase (C4-dehydrogenating)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040357574"
FT DOMAIN 355..390
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 281..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..293
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 39141 MW; F400B9F573BB4E1A CRC64;
MFQKLLGLSL VAAVSAHQNF HQFWVNDVSA GYQVGVRMPP SNSPVTDVTS NDMACNVDGS
TVPSGVETVA ASEGDKITVN WDISGHPGPI THFLFGPVDD ASQATGIGAG WFKIDERDYV
DGKWANEVMG ANGGNYTFTL PTGLQSGEYL LRSEMLALHG AQTVGGAQFY MGCAQLKVTG
TGSGSCTPSI SIPGTYKAED DNIYIPNVYN GFDPTTYTAP GGSVATCGGS GSGSSPSTTA
AASTSASSAA VPASSAASSA PVTVSSAPAA VASSTSKAIA SSTAASAAPT QTADDSEDDS
CDADGDDEDD DSCEAEETSA PATAVPTTFI TRTSASSVAA TSSQAAATSG VASSGKVKLY
GQCGGTGFTG ATECESGSCV VMNDYYSQCV
//
