ID F7W577_SORMK Unreviewed; 654 AA.
AC F7W577;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=WGS project CABT00000000 data, contig 2.30 {ECO:0000313|EMBL:CCC12665.1};
GN ORFNames=SMAC_05626 {ECO:0000313|EMBL:CCC12665.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC12665.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC12665.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC12665.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCC12665.1}.
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DR EMBL; CABT02000030; CCC12665.1; -; Genomic_DNA.
DR RefSeq; XP_003348530.1; XM_003348482.1.
DR AlphaFoldDB; F7W577; -.
DR STRING; 771870.F7W577; -.
DR GeneID; 10805995; -.
DR KEGG; smp:SMAC_05626; -.
DR VEuPathDB; FungiDB:SMAC_05626; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_4_1_1; -.
DR InParanoid; F7W577; -.
DR OMA; DIRMNCH; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000001881; 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 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:SF100; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G00630)-RELATED; 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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..654
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003370938"
FT DOMAIN 358..372
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 654 AA; 70652 MW; 3622AC049326CFDF CRC64;
MILRRLLGLA FAAVPLASAV ELTGYEYIVV GSGAGGGPLA ARLAMAGHKT LLIEAGDDQG
NNINVTVPAY NARSSEDEKM SWDFYVRHYP DDKQQARDWK TSYRLPDGSI YTGLFPPEGA
EMLGTLYPRA GVLGGCTAHN ALIAVYPHQS DFQYLADLTG DQGWSPSNMR KHFVSMEDKN
YVNGLYSGHG RDGWLSTEVT PLTIPLKDPQ LLSLTLGGAF ALGNITQSPI NLATVLAGDL
NANTIARDKK PAYYETPLSS KNGARSGSRD FVVAVRDARK PDGSKKYPLD VRLNCHVTRI
TFNTSSSSSE PIATGVEFLD GAHLYRASPL SANRANNVRP NGTPGSAHAS REVIISGGAY
NSPQILKLSG IGPRTELEKF GIPVLVDLPG VGGNLQDHYE IGVNVKVPKD WTALKGCTFQ
LYGNTSDPCL DRWLNPVLGD RGTYASSGLA VAMLYKSSVT TDDSYDVFTF GGPVNFAGYY
PGYSVDITAE HDWWTWAILK AHPRNRAGTV SLRSSNPLDT PVINYNYFDF GSGDYQADLT
AMREAIGLAR DALKRQVVRT QEVRPGADIQ SDGEIEQFIK DGAWGHHASS TCPIGADGDP
MAVLDSKFRV RGVKGLRVVD ASVYPRIPGT FTAVSTYLAA EKAAVDILEG LKKN
//
