ID A0A1B7MYS0_9AGAM Unreviewed; 446 AA.
AC A0A1B7MYS0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OAX37758.1};
GN ORFNames=K503DRAFT_742254 {ECO:0000313|EMBL:OAX37758.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX37758.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX37758.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX37758.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KV448333; OAX37758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7MYS0; -.
DR STRING; 1314800.A0A1B7MYS0; -.
DR InParanoid; A0A1B7MYS0; -.
DR OrthoDB; 1947085at2759; -.
DR Proteomes; UP000092154; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092154};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..177
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 314..381
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 446 AA; 48936 MW; 3D6F39C054F270CE CRC64;
MSFSSGAPKF RVAICGAGIG GLVLAVTIGQ FAGCDVEVDI YEAHDTITTA GVGMIISRRT
VEVIKALCMH EEISHASTKP SSSTRGSKFR KSDIPEGGFE WFSRIVRQGN PIHRQHLVDI
LKQHLPSSCT VHFNKRLTTY EKLSAGSLVL HFADESSENT DVLIGADGIR SSVRKTLFET
IDKDLVDPSK IRHYIDPSWT GTLVYRAIIP AQKLLEMDPN NVSLGELVMF CGKGKNIISY
PVSQGTLINV AAFASDEQKA GTPFEGRWVS DVSQEEVEEA FQDFEPAVKS LLKCFNNPSR
WALHVVNELP LSVRDRVALI GDACHAMTPH LGAGAGQAME DAFVLGRLLA HPLTTLDNVP
AALRAYQDIR LPAAQLVARN SKHTGWMYRF NMPGYYDGTD QGNERGELEI LQEMIISHIE
VCGQGSAVAE WQQAEKKLQE NVGLCT
//
