ID A0A067MWK0_9AGAM Unreviewed; 602 AA.
AC A0A067MWK0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=BOTBODRAFT_27541 {ECO:0000313|EMBL:KDQ20128.1};
OS Botryobasidium botryosum FD-172 SS1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Botryobasidiaceae; Botryobasidium.
OX NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ20128.1, ECO:0000313|Proteomes:UP000027195};
RN [1] {ECO:0000313|Proteomes:UP000027195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL198018; KDQ20128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067MWK0; -.
DR STRING; 930990.A0A067MWK0; -.
DR HOGENOM; CLU_002865_6_0_1; -.
DR InParanoid; A0A067MWK0; -.
DR OrthoDB; 1704824at2759; -.
DR Proteomes; UP000027195; 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; 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:UP000027195}.
FT DOMAIN 94..117
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 285..299
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 539
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 582
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 538..539
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 602 AA; 66325 MW; 8D145637BA360EBB CRC64;
MEKTFLTASI KTIAAQEFDY VIAEGETAGL VLAARLSEDP GVTVCVLEAG GDNLDEPEIL
IPHRLNFGNP NIVWEFQTVP QPHVNNKVAT WSRGKGLGGS SALNLWLYQR PPAFDIDAIG
RLGNPGWNWD RFLEYAKKSE TFRLPTVKEA KEYNFHTNPE YHGNNGPLRA GFFSRTTECS
LLFQKTLNNL GIKTQKDHMG GKLCGTWVDP ATVDKETGSR SYAANAYYAP NASRENLKVL
TGALVHKLLF STKPNEDVQA TGVAFIYDGK PFEVKARKEV IVSAGALKSP QILELSGIGD
PKVLKPLGID VHVDLPGVGA NMQEHNMILM TFELTESDRW ATRDAVHFNP ELAAEQLALY
RTSGEGIYSV SRGVIAFTPL KTLNAKAAED MIASVEAKIQ AQDDPALREQ WALQLDAMKD
DNVPDCEFTG NLFCVPTEHP PDIKKKYFSV AGIHNHTFSR GTIHINSNDP ADQAVIDPRS
LEQDEDMVML VEILKFMRTL PQTEPFKSMV AGELSPGDRC VTDEDLRAYI KRHLGTAWHT
AGTCSMLPRS QGGVVDSRLK VYGTTNVRVI DLSVIPLHIM AHTQATVYAL AEQAADIIKG
II
//
