ID A0A165NC16_9AGAM Unreviewed; 1061 AA.
AC A0A165NC16;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Fatty acid hydroxylase {ECO:0000313|EMBL:KZT19446.1};
GN ORFNames=NEOLEDRAFT_1183328 {ECO:0000313|EMBL:KZT19446.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT19446.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT19446.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT19446.1,
RC ECO:0000313|Proteomes:UP000076761};
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; KV425640; KZT19446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165NC16; -.
DR STRING; 1314782.A0A165NC16; -.
DR InParanoid; A0A165NC16; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000076761; 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:UP000076761};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 496..637
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 673..903
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
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 1061 AA; 117461 MW; 5DC9562A38D0C824 CRC64;
MSVPIPQPPT IPFLGNVLAI DKELPIGSFG LLAKQYGEIY QLNLLGRIVY FVNSCELVRE
LSNDKKFQKS VPGSLNEVRS LAGDGLFTAL ADEPNWAIAH RLLMPAFGTA NIRNMWDDMK
DICSQLILKW SRFGPDYVIS PTDEYTRLTL DTIALCSMNY RFNSFYSETL PPFCEAMTDF
LKECNARANR PAIVQALMTS ATAKWEADKK LMVDVASQIV KHRRHHPIEK KDLLNTMLYG
KDPKTGQGLS DDAITKNLIT FLIAGHETTS GILSFTTYYL LKNPECLIRL RKEVDDVTQG
KSITLEHLAK MPYLNAVLRE SIRLNPTAAV RAVVALEDVA LAGKYAIKKG QAFAINNHAA
QRDHKVWGDD ADEFKPERML DGKFEAMPPE SWQPFGYGMR ACIGRPFAWQ EAQLVIASII
QTFDLCFNDP DYTLEVKQAL TLKPKDFYIR ASLRSNAVHL LSTPSSSLLA PKAAGKDYAP
VNAPVEQDDG TPKPRMYVLY GSNTGTSESF AQRIASDASS RGFKASIGTL DQATGRILTD
GPVIIITASF EGQPADNAAQ AVQWLEQGTS DTEFKDLKYA IFGCGNRDWV RTYQRVPKLV
DEILEKKGGT RLLPRGEGDA SGSTFFEDFD AWEADLWMVL TKEYNTVSTK VEETLTVKTT
KSGTTRASEL RQPDAKLGTV TQNRVLTKPS ASGVKRHIEF ALPEGMSFRA GDYLAILPVN
PGELVKRAIA HFGLSPEEEV TISSSSPSTL PLNKPINILS LLSGYVELSQ PASTKDLQVL
TSLTDSAATK SKLEALLGDY KASVLNKRVS VLDVLESHKD IKISLSTFLR LLPPMRIRQY
SISSSPLANP QNVTLTVSIV EGAPVPGHRD VPFLGVASNY LARLQPGERV QLMVKPSGTQ
FHPPSDLSTP ILMFCAGSGL APMRGFIQER AKQKESGREV GPMHLFFGCR SPEEDYLYAE
DDIAEWVKAG VVDVRPAFSR ASEKSEGCKY VQDRIWHDRE DVMKAYNAGA RFYVCGSRKV
ATGVQKVCID ILKAAVNLSD EEAQRIWERV EQERGASDIF E
//
