ID A0A166N274_EXIGL Unreviewed; 475 AA.
AC A0A166N274;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZV78672.1};
GN ORFNames=EXIGLDRAFT_689734 {ECO:0000313|EMBL:KZV78672.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV78672.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV78672.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV78672.1,
RC ECO:0000313|Proteomes:UP000077266};
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}.
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DR EMBL; KV426796; KZV78672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166N274; -.
DR STRING; 1314781.A0A166N274; -.
DR InParanoid; A0A166N274; -.
DR OrthoDB; 1947085at2759; -.
DR Proteomes; UP000077266; 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; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000077266}.
FT DOMAIN 9..178
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 318..349
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 475 AA; 51703 MW; 5AFF4D302BB14543 CRC64;
MAAPSPIRIS IVGGGISGLC LASVLAKYDE DHKLNVVIYE STASFGEVGA GVTVWGRTFQ
VIRALGLQDD LNAIDMSKGV DSSEWAFRYR RSDAGPVGRE FARRPFPNGS SFHRAQFLSI
FAAKVEQSPN IRVECNKRLV SANTQGAGQP LTLTFKDGTT ATCDVLIGAD GVRSPVRVAM
MDCAARDLGD DMFRSQGPAV WSGECIYRSL VPMSQLCETY KQLGGQGDPA IQSGPVLYCG
QDKAFALYPI QGGKVINVGL GITQPGKAGT LFPDERWVSD VEPGFLEKEF EDWEIEVRAI
VNCMKTASRW AIHVVPGLNS FAYGRIAIQG DAAHAMTPYN GSGVNQAIEV RFSPRYIVIR
DTSPNPYSLQ DAYVLGRMLT HPKTTMETVQ SALKAYDSVR RERAQGVQEL SLQLGRLATF
TEELQLQPGA DPIAVTAARL EAAGKWVGEG DLEDDVRKAE ENYSKFIAKA REEVC
//
