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Database: UniProt
Entry: A0A167VMF6_9AGAM
LinkDB: A0A167VMF6_9AGAM
Original site: A0A167VMF6_9AGAM 
ID   A0A167VMF6_9AGAM        Unreviewed;       529 AA.
AC   A0A167VMF6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KZP05170.1};
GN   ORFNames=FIBSPDRAFT_877808 {ECO:0000313|EMBL:KZP05170.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP05170.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP05170.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP05170.1,
RC   ECO:0000313|Proteomes:UP000076532};
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; KV417857; KZP05170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167VMF6; -.
DR   STRING; 436010.A0A167VMF6; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000076532; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
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:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000076532}.
FT   DOMAIN          258..272
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         85
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   529 AA;  58767 MW;  DEDCE913C5CD4FB2 CRC64;
     MPSRLEYDFI VVGGGTAGCV LANRLTEDPN IQVLVIEGGP DDRKHPAVLQ LKDWLSLLGG
     PLDYQYMTTE QPRGNSHIMH SRAKVLGGCS SHNTLICFRP FPQDLDDWVK EGCTGWDNRT
     IQPYGDRLLN HIAPVHLKDQ NPIMADWITA CNETTGVERI EDFDAWAKNR HLGSQVWSEG
     VGWLSVAYTP EDGKRSSASV AYMHHIMDGQ RPNLHVMLET WVDRIVFKGD RAVGVECVSK
     EGARSTAYAR HEVMLCAGAV DTPRLLLLSG VGPKEQLLDL GIPVVHDLPG VGENLQDHPE
     SIIMWETDEL PKNTVMESDA ALFIKRDKEC PDPRPDLMFH VYSVPFADNT ERMGYPRPPH
     AICMTPNIPR PRSRGRLFLT SADPTVKPAL DFRYFTDAED YDAKCLVDGM KIAREIAKTA
     PFSNWLKKEI APGPSVTSDE DLNEYARRAS HTVYHPAGTC KMGAFSDPMA VVDPLLRVRG
     LKGLRVVDAS VFPLMVTANP MVTVLMIGER ASDLVKADFY RNTAALASL
//
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