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}.
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; 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
//