ID A0A165QTG6_9APHY Unreviewed; 1063 AA.
AC A0A165QTG6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KZT69908.1};
GN ORFNames=DAEQUDRAFT_668534 {ECO:0000313|EMBL:KZT69908.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT69908.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT69908.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT69908.1,
RC ECO:0000313|Proteomes:UP000076727};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR000209-1};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; KV429054; KZT69908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QTG6; -.
DR STRING; 1314783.A0A165QTG6; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0070330; F:aromatase activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
DR CDD; cd06206; bifunctional_CYPOR; 1.
DR CDD; cd11068; CYP120A1; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR023206; Bifunctional_P450_P450_red.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF127; BIFUNCTIONAL CYTOCHROME P450_NADPH--P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Heme {ECO:0000256|PIRSR:PIRSR000209-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000209-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000209-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 498..638
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 679..906
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 453..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000209-1"
SQ SEQUENCE 1063 AA; 117365 MW; F42715BD6121D6FD CRC64;
MTTPIPCPPS LPFFGHVTKI EKEVPLRSFI LLAKQYGEIY ELLQFSRSLL VVSTYELLND
ICDDKRFVKN PGGALEQVRN GVGDGLFTAK PGEENWELAH RILMPAFGTA AVREMFDDMH
DIATQLILKW ERFGPNVAVN PAEDFTRLTF DTIALCSMSY RLNSFYRETN PPFVEAMVDF
LVESGLRAFR PTLVTNVMGY NAKYEQDIKT MADLANEIIA DRRANPTEKN DLLNRMLEGK
DPKTGKTLSD ENIKNNLLTF LIAGHETTSS TLSFLTYFIL KKPEVLRKLR AEVDAVLGDE
QPQIGDLNKL PYLTACLRET LRMGPAAPMR GAQAWEDTTI GGGRYAVKKG QNISILIWQA
LRDPKVWGED AEEFNPERML DGKFEALPPN AWQPFGFGMR ACIGRAFAWQ EMMLTAALIV
QRFDVTMDDP SYELVIKQTL TIKPRDFRIR VAPRRDKGAP VPRPATFTPR ASAFRGAAGS
TSTTGSASAG GGAARQPVYV LYGSNTGTSE TFAQRVVNGA AARGFRAGMG TLDSYAGKLP
ADGPVVIITA SFEGEPADNA AHFVDWLSNL KGEELANVRF AVFGCGNRDW VNTYQRIPTL
IDARLEERGA QRLVARGAGD ASGGDFFETF DEWEAGLWET LSKEYGSAAM EDVQAGLAGG
LEMKMVDEGT YRASVLRQPD AALGTVVENT LLTAPDAPAK RHIEFELPEG MSYRAGDYLA
VLPSNPPRDV HRVIARFGLS PEQEVVLSSS GPTPLPVNRP ISVQILLSGY VELSQPATSR
DLRLLQAAEN APTEVLRALS DDYAEKVLNA RLSVLDILEN HPSLKLPFPT YLQMLPAMRI
RQYSISSSPL WHPTHVTLTV SVVDAPSRAG RRDTFLGVAS TFLAGLRAGD KVQLAVRVSS
GAFHPPADPT EPMVLFAAGS GLAPMRGFLQ ERAMQKKAGR EVGRSLLFFG CRRPGEDYLY
GETDLREWQA LGIVDVRPAF SRATEESKGC RYVQDRAWLD REEVRAAYNA QAKFYTCGSR
KVAQGIKEVL TKIIKEAQGI DDSTADEVFK RAIRGRYATD IFE
//
