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Database: UniProt
Entry: F8QAY3_SERL3
LinkDB: F8QAY3_SERL3
Original site: F8QAY3_SERL3 
ID   F8QAY3_SERL3            Unreviewed;       763 AA.
AC   F8QAY3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=SERLA73DRAFT_171373 {ECO:0000313|EMBL:EGN94369.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; GL945488; EGN94369.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8QAY3; -.
DR   STRING; 936435.F8QAY3; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_011025_0_0_1; -.
DR   InParanoid; F8QAY3; -.
DR   OMA; IGYLQCA; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000008063; 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   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR005018; DOMON_domain.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SMART; SM00664; DoH; 1.
DR   SUPFAM; SSF49344; CBD9-like; 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|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..763
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003377245"
FT   DOMAIN          312..335
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          480..494
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   763 AA;  80943 MW;  DA4E2A8A021FAE75 CRC64;
     MVLSFLLLSV LSISGSVLAQ SSSGYTDSGN GFVFQGYTDP VYDVTYGLVF PPLVTTGTNS
     TEFIGEIVAP IGAQWIGLSL GGAMLDSLLL VAWPNINSVV FSSRYTTAYT GPIITSLPST
     TVNSTHWKWV FRCQNCTSWQ GGSINLGGSS ALAWAYSNVA VNDPSDPQSS FQEHTDFGFF
     GENFAAAHSS NYNNYLNGDP GTTSSVPTST STVVSSTTTL TSPTTTATPY DYIVVGAGPG
     GIIAADRLSE AGKKVLLLER GGPSTGETGG TYDAVWAEGT NLTKFDIPGL FESMFTDSNP
     WYWCKDITVF AGCLLGGGTS INGALYWLPQ DSDFSTSVGW PSSWGNHQPY TNKMAARLPS
     TDHPSTDGLR YLEQSATVTA QLLNGQGYRN ITINDDPNSK DHSYGNSAFD FINGKRGGPV
     ATYLQTALAR SNFVYKDHTL VSNVVRNGSQ ITGVQTNDSS LGPNGVVPLT PNGRVILSAG
     SYGSPRILFQ SGIGPADMIA LVEGSPTAAA NLPPSSQYID LPVGYNVSDN PSINFVFTHP
     SIDAYDNWAD VWTDPRPADA VQYLKDQSGV FAGASPKLNF WRSYTGTDDK QRWMQGTVRP
     GASAVNTTYA YNDSQIFTIT TYLSQGVTSR GRIGINAALT GLPLVNPWFT DPVDKSTLIT
     ALNDIVSNIN TVPGLTLITP DNQTTITDYV NSYDPGSLDS NHWVGSNSIG SVVDSNTKVF
     STNNLFVVDA SIIPSLPTGN PHGTLMSAAE QAAAKILALA GGP
//
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