ID F8QAY2_SERL3 Unreviewed; 751 AA.
AC F8QAY2;
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_77778 {ECO:0000313|EMBL:EGN94368.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL945488; EGN94368.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QAY2; -.
DR STRING; 936435.F8QAY2; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_011025_0_0_1; -.
DR InParanoid; F8QAY2; -.
DR OMA; FYEAWTT; -.
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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47190:SF1; -; 1.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 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 Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 300..323
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 468..482
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 751 AA; 80498 MW; B446D187E92BE206 CRC64;
MHVVLAQSSS SYTDSGNGFV FQGYTDPVYN VTYGFVLPPL VTTGTNSTEF IGEIVAPLDA
QWIGLSLGGA MLNSLLLVAW PNANSVVFSS RYATQYALPT AYTGPIITSL PSTTVNSTHW
KWVFRCWEGG SFDLGGASTL AWAYSDVVVA DPSDAQSSFQ EHTDFGFFGE DFAVAHNRNY
GSYLNGSPGT TGILPTSTYS ATSSTTALPG STVIATPYDY IIVGAGPGGI IAADRLSEAG
KKVLLLERGG PSTGETGGTY NAPWAEGTNL TKFDIPGLYE SMFSDPNPWY WCKDITVYAG
CLLGGGTSIN GALYWLPQDS DFSVSVGWPI SWVNHQPYTS KIAARLPSTD HPSTDGLRYL
EQSYTVTSQL INGQGYRNVT INNYPNSKDH VYGYSAFDFI AGKRGGPVAT YLQTALSRPN
FVYRDYTLVS SVVRNRSQIT GVQTNDSSLG PNGVVPLTHK GRVILSAGSY GSPRILFQSG
IGPSDMIALV EGNPTTAANL PPSSQYIDLP VGYNVSDNPS VNFVFTHPDI DAYDNWANVW
SDPRPADAAQ YLRDQSGVLA GITSKLNFWR SYTDTDGKQR WMQGTVRPGA SVINTTYAYN
VSQTFTITTY LSQGVTSRGR IGINAALTGI PLVNPWFTDP VDKSTIITAL NDLISTVNTV
PGLTLITPDN QTTITDYVNN YDPALLNSNH WVGSDSIGSV VDSNTKVFKT DNLFIIDASI
IPSLPTGNPH GTLMSAAEQA VAKILALAGG P
//
