ID A0A2H3BGM8_9AGAR Unreviewed; 618 AA.
AC A0A2H3BGM8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:PBK68830.1};
GN ORFNames=ARMSODRAFT_957914 {ECO:0000313|EMBL:PBK68830.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK68830.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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}.
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DR EMBL; KZ293431; PBK68830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3BGM8; -.
DR STRING; 1076256.A0A2H3BGM8; -.
DR OrthoDB; 2241281at2759; -.
DR Proteomes; UP000218334; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000218334};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..618
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013930909"
FT DOMAIN 38..346
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 469..605
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 552
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 595
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 126..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 618 AA; 66645 MW; 3C694BD4AA0D944B CRC64;
MFTKLVLSAV FLGLTHAALV DLNATQSDGV KILKKQTFEY IVVGGGTAGL TVARRLAESS
SKTSVLVLEA GGSGVGKDIV TIPKNSFAFV GTEIDWGFTI APQEHAADAE INLSSGKILG
GDSSINGLVW TRASKAEYDA FETLGSPGWN WDTLYAHMQK AEQLEYPSAS LIDEYGYVVD
ASSVGTSGPV SLSFPAYLPL QHRTLIEASV ELGHTFNTDA YGGENAGVYY SLSSQNTVPV
RETSEFAYLT PWETHKQLTV LTYATVSKIN LDKSAKATGV QVIFPDGSKY TASLKSGGEV
ILSAGVVRTP QLLELSGIGD SSILTPLGID VKVDLPGVGA NYEDHTLTLL TYQLKDGLLS
FDALSYNETL LEEQTELYSL GQGWLTFAQA VVNFEPIDVV LTADEIEEAK QILSTKPEST
PQDQFDIIKE QILNGTTQVE YLLFNSFSAG ETKEANTSYI SMAITHTHPL SRGSIHINST
SIDDYPIINP NMLEAEWDNW FLAKATAYGR KIFETQAFQE IVVSEEVFPG SNVSTDDEWL
TYVQENLNSG YHSVGSASLL PKESNGVVDA NLRVYGTKNL RVADLSVLPL LISAHTQPAA
YAVGELAATL ITTGSTNC
//
