ID Q0TZQ9_PHANO Unreviewed; 953 AA.
AC Q0TZQ9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_15063 {ECO:0000313|EMBL:EAT77606.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT77606.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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 -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; CH445359; EAT77606.2; -; Genomic_DNA.
DR RefSeq; XP_001805226.1; XM_001805174.1.
DR AlphaFoldDB; Q0TZQ9; -.
DR STRING; 321614.Q0TZQ9; -.
DR EnsemblFungi; SNOT_15063; SNOT_15063; SNOG_15063.
DR GeneID; 5982154; -.
DR KEGG; pno:SNOG_15063; -.
DR VEuPathDB; FungiDB:JI435_150630; -.
DR eggNOG; KOG0157; Eukaryota.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_7_0_1; -.
DR InParanoid; Q0TZQ9; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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; 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 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 Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 383..524
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 561..790
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 953 AA; 106572 MW; DCF65BCFA8DCADD7 CRC64;
MFSEMHDIAS QLVMKWGRHG PEHKIHVVDD FTRLTLDTIA LCAMDYRFNS YYYQKMHPFV
DAMSDFLKVS GDRARRDPIS QMFYRAETAK YWEDIELLRK TSMEVIKNRR ENPTEKKDLL
NGMLNGVDPK TGEKMSDESI MDNMITFLIA GHETTSGLLS FTFYYLLKNP AAYEKAQQEV
DSVIGKGPIT VDHLSKVPFL NAVLRESLRL SPTAPSIGLT AKQDTVLGGK YPVKAGAPIL
TLFPLIHRDP LAYGEDAEEF RPERMLDEEF DRRNKEYPNC WKPFGNGMRA CIGRPFAWQE
ALLVLAILLQ NFNFSMDDAS YKLQIKQTLT IKPKDFYMRA HLRNGVSATS LERALQSATL
QEPPPANGGQ AVRKQKANKG KPIAIYYGSN TGTCEALANR LASDAANHGF RADVVDTLDA
ARENLPTDKP VVMVTASYEG QPADNAAHFV NWIGTLKDKE LEKVSYAVFG CGHRDWAKTF
HKVPKYLNTT LEERGATKLV EMGTTDAASG DIFTDFETWE DQVLWPALRE KYGSSEVEGE
GSMEATLDVD ISTPRSTILR QDVREARVEE VQVLSANGVA EKRHIEISLP SDMSYSAGDY
LAILPLNPKE NIRRATKYFG LSWDSMLTIQ SAGPTTLPTD TPISAVDVFG AYVELAQPAS
KRNILTLVDA TRDEDTKTQL LRLADSAFTE EITAKRVSVL DLLERFPSVQ LPLGVFLKMQ
PPMRVRQYSI SSSPLWNPNN VTLTYAVVNQ PALSGQGRYV GVATNHLSKL APGDKLHVSV
RASHQAFHLP KDGKSIPIIC IAAGTGLAPF RGFIQERAAQ LAAGRTLAPA LLFYGCHSPD
SDLLYSDLLK KWEQLGAVSL RFAFSRQPEA SEGCKYVQDR MYHDRADIIE LFNQGAKLFV
CGSREVGDGA EEMLIKIAKE KFQGEEGREA DDKKAREWFE DLRNERFATD VFA
//
