ID A0A165FDC9_EXIGL Unreviewed; 607 AA.
AC A0A165FDC9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:KZV88807.1};
GN ORFNames=EXIGLDRAFT_772323 {ECO:0000313|EMBL:KZV88807.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88807.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV88807.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88807.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV426089; KZV88807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165FDC9; -.
DR STRING; 1314781.A0A165FDC9; -.
DR InParanoid; A0A165FDC9; -.
DR OrthoDB; 1348067at2759; -.
DR Proteomes; UP000077266; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 277..291
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 544
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 587
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 607 AA; 64851 MW; 049FAEE0E9E3CAA8 CRC64;
MFKLVTKGRQ LRQPEGLTVG SRLSEDPRIS VLVLEAGQDA EDFQEVIVPG LILTGQSVGG
ILDWKYQTVP QPNFNGRQIT LSAGKALGGS SVTSALIFTR GQKEQYDAWG SLNNDPSWGF
SALLPFFKKS EHVFQPDAYQ RELGAKLDLP FRGAKGAAAV GYGNFEYAQS ALWRSAAEKL
GLPAGTDETD GETRAVSVST ASIDPRNNTR CDATCAYYTP VSRRPNFTVM TNVTVTRILW
KSTKVPGDAV AGGVEYVDQS GVVHNISVTR EVIVAAGAIG SPKILELSGV GNPAILKSAG
VKPVVTLPAV GENLSDDMQV WVNSVAVNVE ITADVLAANP TFAAEQLDLW SHNRTGLLSR
APCSLTLTAP SDLFSHEALA PLLKAARANI SHYASQFSNG ISAVARGIVA QHTAALSLWE
RNAERPVELF FQPGYLGPTP AAQRPGGANT NFSSITTLFY TPLSRGRVHI ASSDPSVPPT
LDPAYWSHPL DSAAHVKGVQ FARKMLKTAP LSSINGGEFE PGEDKQSDED VEAWMRTIIQ
SDFHAVGTAV MLPKELGGVV DTKLKVYGTR NVRVVDASIF PLPLSAHTLA SVYAVAEKAA
DMIKKSG
//
