ID A0A165F508_9APHY Unreviewed; 414 AA.
AC A0A165F508;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZT08405.1};
GN ORFNames=LAESUDRAFT_676470 {ECO:0000313|EMBL:KZT08405.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT08405.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT08405.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT08405.1,
RC ECO:0000313|Proteomes:UP000076871};
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 -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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; KV427615; KZT08405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165F508; -.
DR STRING; 1314785.A0A165F508; -.
DR InParanoid; A0A165F508; -.
DR OrthoDB; 1699331at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF309; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14510)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 7..332
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 414 AA; 45111 MW; 950E45AE12E9E410 CRC64;
MESKLPTKVI IAGAGIAGPV LAMFLKTKGY DPVVYERVDK IEDVGLSLCL QPNGLKVLSL
IPGFLESIIG KQLSHLVQIS YYPSSSPSEV PLADLDAPSH LPDLTGGFGM LGVRRPVFNR
TIVEAAERQG VKIVWGHQLV ALRQGEDEVQ VTFANGATDT ASFVVGCDGL HSNTRICLFG
EEKVNYTGLC QTGGVSPTPE SHKGRASMTN IYSDGAHMVS YPISNTETSW AITLREPEAR
ETWRAMDEEK QREFKQSTFS QWPFGAGELV RSADRIIKYG LYDRPELKSW HQGRVVLLGD
AAHPTSPHLG QGANQAFEDI YHLVRLLTKH NPSAAPPATA LLSTIFTEYE SLRIARTSML
VQGARQQGES RVVSGAEACK MRDGAIKKAL GNGEGLLQGM LMVYRGPFDG ESEI
//
