ID   A0A0H2S4L4_9AGAM        Unreviewed;       594 AA.
AC   A0A0H2S4L4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Aryl-alcohol-oxidase from pleurotus Eryingii {ECO:0000313|EMBL:KLO19185.1};
GN   ORFNames=SCHPADRAFT_992953 {ECO:0000313|EMBL:KLO19185.1};
OS   Schizopora paradoxa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Schizoporaceae; Schizopora.
OX   NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO19185.1, ECO:0000313|Proteomes:UP000053477};
RN   [1] {ECO:0000313|EMBL:KLO19185.1, ECO:0000313|Proteomes:UP000053477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8140 {ECO:0000313|EMBL:KLO19185.1,
RC   ECO:0000313|Proteomes:UP000053477};
RG   DOE Joint Genome Institute;
RA   Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA   Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT   "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT   wood degrader in East Asia.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; KQ085888; KLO19185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2S4L4; -.
DR   STRING; 27342.A0A0H2S4L4; -.
DR   InParanoid; A0A0H2S4L4; -.
DR   OrthoDB; 3215324at2759; -.
DR   Proteomes; UP000053477; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053477};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..594
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005202190"
FT   DOMAIN          111..134
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          301..315
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        529
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        573
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         113
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         260
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   594 AA;  63098 MW;  68F968C7CC35E8D0 CRC64;
     MPRRSIVLVL AALAKAVSSA LFTDVGQLSK TEYDFVIVGA GAAGNVLASR LTESKEFSVL
     VIEAGVTDQG VLGIEVPFLA PTNQPMTAVT WNFTTTPQTS LAGRVLNYPR GRVLGGSSSI
     NFLTYTRGSN EEYDRWAELT GDSGWAWDNV AQFYFKSSRL VPPVDGHSTA GDFNPADHGN
     GPIEVSLPGM PTEIDNRVIN TSKQSGSEFP FNIDLQSGNA VGVGLAQSTI GGGARSSSST
     AYLTPVLNRT NLDVLIQTTV TRLISSGSSE NPIFRTVEVA ANASSKRSTV SAKKEVILSA
     GSIGTPQILM LSGIGDQTAL KKLGIKTLLN LPDVGQNLQD HPIMSNYFLV NSNNTFDDVL
     RNTSILDADL AQWTNNRTGL FGNAPGNAVA FLRLPNNAAI FKQFKDPSAG PQSAHFEFIF
     ADGFAATVQP QPATGHFLTI NSAVVSPISK GSVTLNSTNP FEFPIINPNF FSSPFDQAVM
     LQAVKTARSF VAASPWAGFV QSRFGPVGDA ETDDEIIAAS KQSIVTIFHP VCTARMSPKD
     ASWGVVDPQL LVKGATGLRI VDASIFPIIP AAHTVGPTYI VAERAAQLIK DAWS
//