ID F8MFE9_NEUT8 Unreviewed; 1108 AA.
AC F8MFE9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE Includes:
DE RecName: Full=Cytochrome P450 {ECO:0000256|PIRNR:PIRNR000209};
DE EC=1.14.14.1 {ECO:0000256|PIRNR:PIRNR000209};
DE Includes:
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000209};
GN ORFNames=NEUTE1DRAFT_145879 {ECO:0000313|EMBL:EGO60003.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO60003.1};
RN [1] {ECO:0000313|EMBL:EGO60003.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO60003.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018, ECO:0000256|PIRNR:PIRNR000209}.
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DR EMBL; GL891303; EGO60003.1; -; Genomic_DNA.
DR RefSeq; XP_009850185.1; XM_009851883.1.
DR AlphaFoldDB; F8MFE9; -.
DR GeneID; 20826633; -.
DR KEGG; nte:NEUTE1DRAFT145879; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_145879; -.
DR HOGENOM; CLU_001570_7_0_1; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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 Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000209};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000209};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000209};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000209};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW Iron {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000209,
KW ECO:0000256|PIRSR:PIRSR000209-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|PIRNR:PIRNR000209};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000209};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000209};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000209}.
FT DOMAIN 504..645
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 684..916
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 481..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 412
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 1108 AA; 123711 MW; 17F82DEB5F723B03 CRC64;
MSSDETPQTV PIPGPPGLPL VGNSFDIDTE FPLGSMLNFA DQYGEIFRLN FPGRNTVFVT
SQALVHELCD EKRFQKTVNS ALHEIRHGIH DGLFTARNDE PNWGIAHRIL MPAFGPMAIQ
NMFPEMHEIA SQLALKWARH GPNQSIKVTD DFTRLTLDTI ALCSMDYRFN SYYHDDMHPF
IDAMASFLVE SGNRSRRPAL PAFMYSKVDR KFYDDIRVLR ETAEGVLKSR KEHPSERKDL
LTAMLDGVDP KTGGKLSDDS IIDNLITFLI AGHETTSGLL SFAFVQLLKN PETYRKAQKE
VDDVCGKGPI KLEHMNKLHY IAAVLRETLR LCPTIPVIGV ESKEDTVIGG KYEVSKGQPF
ALLFAKSHVD PAVYGDTAND FVPERMLDEN FERLNKEFPD CWKPFGNGMR ACIGRPFAWQ
EALLVMAVCL QNFNFMPEDP NYTLQYKQTL TTKPKGFYMR AMLRDGMSAL DLERRLKGEL
VAPRPTAQGP VSGQPKKSGE GKPISIYYGS NTGTCETFAQ RLASDAEAHG FTATIIDSLD
AANQNLPKDR PVVFITASYE GQPPDNAALF VGWLESLTGN ELEGVQYAVF GCGHRDWAQT
FHRIPKLVDN TVSERGGDRI CSLGLADAGK GEMFTEFEQW EDEVFWPAME EKYEVSKKED
DNEALLQSGL TVNFSKPRSS TLRQDVQEAV VVDAKTISAP GAPPKRHIEV QLSSDSGAYR
SGDYLAVLPI NPKETVNRVM RRFQLAWDTN ITIEASRQTT ILPTGVPVPV HDVLGAYVEL
SQPATKKNIL ALAEAADNAE TKATLRQLAG PEYTEKITSR RVSILDLLEQ FPSIPLPFSS
FLSLLPPMRV RQYSISSSPL WNPSHVTLTY SLLESPSLSN PEKKHVGVAT SYLASLEAGD
KLNVSIRPSH KAFHLPVDAD KTPLIMIAAG SGLAPFRGFV QERAAQIAAG RSLAPAMLFY
GCRHPEQDDL YRDEFDKWES IGAVSVRRAF SRYPESQETK GCKYVGDRLW EDREEVTGLW
DRGAKVYVCG SREVGESVKK VVVRIALERQ KMIVEAREKG ELDALPEGIL EGLKLKGLTV
EDVEVSEERA LKWFEGIRNE RYATDVFD
//
