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Database: UniProt
Entry: S7RQ95_GLOTA
LinkDB: S7RQ95_GLOTA
Original site: S7RQ95_GLOTA 
ID   S7RQ95_GLOTA            Unreviewed;       428 AA.
AC   S7RQ95;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:EPQ55064.1};
GN   ORFNames=GLOTRDRAFT_42078 {ECO:0000313|EMBL:EPQ55064.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ55064.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ55064.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ55064.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KB469302; EPQ55064.1; -; Genomic_DNA.
DR   RefSeq; XP_007866119.1; XM_007867928.1.
DR   AlphaFoldDB; S7RQ95; -.
DR   STRING; 670483.S7RQ95; -.
DR   GeneID; 19306106; -.
DR   KEGG; gtr:GLOTRDRAFT_42078; -.
DR   eggNOG; KOG2820; Eukaryota.
DR   HOGENOM; CLU_007884_0_1_1; -.
DR   OMA; FYMFPPN; -.
DR   OrthoDB; 1952715at2759; -.
DR   Proteomes; UP000030669; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   PANTHER; PTHR10961:SF45; L-PIPECOLATE OXIDASE; 1.
DR   PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030669}.
FT   DOMAIN          7..380
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   428 AA;  46304 MW;  2CAA737D1CAD1F28 CRC64;
     MVDKTSDILI LGAGCFGAST AYHLLKRGFT SVTVVDRSTV LPAPDGASTD FNRIVRSSYS
     EPFYARFARE AIAAWKDQSE WGDTYHESGV LVLGTGESSY CDSAYDNDVT MGARITNFSD
     ADGLRSAFPP SIKTSFSETS SGYLNSDGGW ANATKGTSLM VSKVLALGGR ILRGKTAKRL
     LQGNGRTSGV EFNDGTTIRA DLVIVATGSW TASSFPEVQL GDKFIATGQS VATIQLTAEE
     ALKYNDCPVV LDFKSGFYVF PPNDDYILKM AIHAGGYANF EPTPQSTTPI STPRTIGSHG
     VDGLRIPKAM AKALREHLRA VYPELADKPF SGTRLCWYND TPDEDWVIGY YPGDQGLMFA
     TGGSGHAFKF LPVIGSLVAD AVTDDLDPSL KQRFAFDRKC RAHDLSRSLT VLPLQESELR
     TAEDLVPQ
//
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