ID A0A166DEQ2_9AGAM Unreviewed; 646 AA.
AC A0A166DEQ2;
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=Aryl-alcohol oxidase {ECO:0000313|EMBL:KZT38444.1};
GN ORFNames=SISSUDRAFT_1119629 {ECO:0000313|EMBL:KZT38444.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT38444.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT38444.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT38444.1,
RC ECO:0000313|Proteomes:UP000076798};
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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KV428063; KZT38444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166DEQ2; -.
DR STRING; 1314776.A0A166DEQ2; -.
DR Proteomes; UP000076798; 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.
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:UP000076798};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..646
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007872129"
FT DOMAIN 158..181
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT ACT_SITE 580
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 625
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 579..580
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 646 AA; 69639 MW; 8EFD32C9048720C4 CRC64;
MAFGAILFLT SMLKNAVTAV ALLATNTLLR EELQELQNLD SYSPDLDHKC LKAESIHKDA
LELCVYAIII TDPTKIATDY DFVIVGGGTA GNVVANRLSE NSNWKILVVE AGINNAGIED
VSVPFLGPDA SPNKPWTWNY TTVPQKALNG RSLAYQRGKL LGGSSSINFM IYTRGSSDYW
DAIAKWSGDP GWSWISMLPY FKKLETITPP ADHHNTFGQF NPLVHGFSGP LSVSLSGFAS
ELSSRVINTT FVDHADFKFN LDVNSGDQLG VGWLQASIND TVRASSAVAY LAPQFISRPN
LHVLIQQQVT KVLFSTSHGT PAAIGVTFSA GPGAPTFTVK PSKEVILCGG AIGSVQLLML
SGIGPPAQLN AFNIPLVVNS TQVGQNLIDH PAVFNHFSVN APQSLDQLRE NATALEVAEE
EYADEGEGPL VDTVSDTIGF FRVPSNNSVF QQFPDSSVGP KSAHYEFLWS DIWASFLPTA
IAPPTGDFVT LTQVLVAPAS RGSIVLNSPS AFEFPLIDPG FLTSDYDVTL HLLAFKSAKQ
FMSEKSWKGF NLGLAPDSAN TNTDAEIIEY IRNNAVTLWH PTGTNRMQGV GANEDGVVTN
ELLVKGVDKL RVVDASVFPF IVPGHTEATV YALAERSADI IKAAWA
//
