ID A0A0D0BD21_9AGAR Unreviewed; 598 AA.
AC A0A0D0BD21;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=GYMLUDRAFT_224388 {ECO:0000313|EMBL:KIK61550.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK61550.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK61550.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK61550.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KN834770; KIK61550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BD21; -.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OrthoDB; 3215324at2759; -.
DR Proteomes; UP000053593; 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; PS00624; GMC_OXRED_2; 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:UP000053593};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..598
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002207257"
FT DOMAIN 302..316
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 530
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 574
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 260
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 598 AA; 64364 MW; 3BFA8F414C26DE27 CRC64;
MALILLTFFL LLHQHAAIAT LFENIQDVPP TDYDFVILGG GTAGCVVANR LSENENFNVL
VLEAGRPNMG IPTVDIPLFE YTIPSRYEWN STTIPQPALN NRSVNFPHAL ILGGSSSHNG
MYYNRGPKDD WDRYARLTGD EGWSWNSIQP FIAKNERWTP PADGHNTTGQ FNPSIHSTTG
INPVSLAGFP LPIDPLGLQA AQELGGIFAF NLDYNSGNPL GISWGQYTIN NGTRSSAAAS
YLAPEFMNRR NLHVLVNARV SRVLQTSSRS HVPQVLGAEF AQDLNGPFYR VNASKEVILS
TGAINTPQVL LNSGIGNSTF LSSIGIAPLV DLPSVGQNLS VHASAKNAWI VNASAQTEDI
IFQNQSLQNE LIEQWMQTKQ GPLVGAPVGL TMYFRFNDTV LAALGEDPSS GSTAPHASIG
MQPANFPIVP ATGKFLTMST GVLTPTSRGF ITINSTSPNV FAPPIIDAKT LSARFDVLAM
REVIRTALSF VSAPAWDGYV VSPADNLAVA MESDEALDEY IRTIGGPNEH VVGTASMTSH
EAGYGVVNPD LLVKGVTGLR IVDLSVLPLV TAGHTMAPAY IVGERASFLI KKKWEGHD
//
