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Database: UniProt
Entry: A0A0H2RJ10_9AGAM
LinkDB: A0A0H2RJ10_9AGAM
Original site: A0A0H2RJ10_9AGAM 
ID   A0A0H2RJ10_9AGAM        Unreviewed;       656 AA.
AC   A0A0H2RJ10;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:KLO11965.1};
GN   ORFNames=SCHPADRAFT_830236 {ECO:0000313|EMBL:KLO11965.1};
OS   Schizopora paradoxa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Schizoporaceae; Schizopora.
OX   NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO11965.1, ECO:0000313|Proteomes:UP000053477};
RN   [1] {ECO:0000313|EMBL:KLO11965.1, ECO:0000313|Proteomes:UP000053477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8140 {ECO:0000313|EMBL:KLO11965.1,
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; KQ085988; KLO11965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2RJ10; -.
DR   STRING; 27342.A0A0H2RJ10; -.
DR   InParanoid; A0A0H2RJ10; -.
DR   OrthoDB; 2418107at2759; -.
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; 2.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053477}.
FT   DOMAIN          90..113
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          278..292
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          636..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         565..566
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   656 AA;  72925 MW;  322894A77D1F4C91 CRC64;
     MVAPKEVDVI VCGGGPAGCV VAGRLAYADP NLQVMLVEGG NNNRDDPWVY RPGIYVKNMQ
     RDGVNDKATF YTDTMASSYL RGRKSIVPCA NILGGGSSIN FQMYTRASAS DWDDFKSEGW
     TAKDLLPLMK RLENYQKPCN NDTHGYDGPI AISNGGQITQ LAWDFVRAAD AVGVPFNEDF
     RFLNVCIDLE TSHGTEIWAK YVNRVTGRRS DAATAYVHSV MDVQSNLHLR TNSRVSRVIF
     EGTKAVGVAF VHSRNRAHKG ELRETIVRAR KCVVLSSGTL GTPQILERSG VGNSELLKKL
     DIKVVSDLPG VGEQYQDHYT TLSIFRVSNE STTSDDFMRG DKETQDKLFA QWENVPEKAL
     LSSNLIDAGF KIRPTEEELK EMGPEFNKLW DTYFKDKPDK PVMFGSIVSG AYADHSLLPP
     GKYMTMFQYL EYPASRGKIH IQSANPYVEP FFDSGFMNNK ADFAPIRWSY KKTREVARRM
     DAFRGELTSH HPHFHPGSPA ACRDIDIRTA KQLLPNSFTV GIHMGTWHRP SEPYDASKVH
     EDIVYTEEDD KAIDDWIADH VETTWHSLGT CAMKPREEGG VVDQRLNVFG TTNLKCADLS
     ICPDNLGTNT YSSALLVGEK AASLLCEDLG LKVRTPHAPV PHAPIPTGRP ATISAK
//
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