ID G2XPQ2_BOTF4 Unreviewed; 946 AA.
AC G2XPQ2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Similar to NADPH--cytochrome P450 reductase {ECO:0000313|EMBL:CCD33596.1};
GN ORFNames=BofuT4_P072750.1 {ECO:0000313|EMBL:CCD33596.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD33596.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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|ARBA:ARBA00036596};
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; FQ790249; CCD33596.1; -; Genomic_DNA.
DR AlphaFoldDB; G2XPQ2; -.
DR STRING; 999810.G2XPQ2; -.
DR eggNOG; KOG0157; Eukaryota.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_7_0_1; -.
DR InParanoid; G2XPQ2; -.
DR Proteomes; UP000008177; Unplaced contigs.
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:0004497; F:monooxygenase activity; IEA:InterPro.
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; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
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:UP000008177};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 383..524
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 554..784
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 946 AA; 105170 MW; 3DDCCC72EB45DDFF CRC64;
MHDIASQLVM KWARFGSREK IDVTDGFTRL TLDSIALCAM GTRFNSFYHE EMHPFVDAMT
GFLLESGARA QRPAIASYFM RSAQAKYDAD INLLQSTAKE LLAERRANPN DKKDLLNAMI
NGRDPKTGKG LPDSNILNNM ITFLIAGHET TSGMLSFLFY YLLKNPSAYQ AVQREVDEVV
GKGPITIDHM SKLPYIEACL RETLRLTPTA PAFTVFPLPD STESPIIIGG KYEVKPGQPI
LALIPAVHRD PTVYGDDVAS FKPERMLDEQ FKNLPPNAWK PFGNGMRGCI GRPFAWQESI
LIVAMLLQNL NFRMDDPSYN LVIKQTLTIK PNGFFMHASL RDGIDPIHLE KMLHVDVSKE
RLSESDQKLT KVLSNPGKPK QPMSIFYGSN SGTCEALARS LAREASGRGY EAQVDPLDAA
VDKIPKDQPV ILISSSYEGQ PPDNASHFVE WLENLQGSDR LKGVKYAVYG CGNHDWVSTF
HRIPKLLDNQ FEKHGATRIG DTGLGDVADG DIFEAFDEWQ DNHLWTKLTS SADHGEIGLE
IEIDSTSRSS RLRQDVRESI VLSNKVLTAP GEPEKRHISL KIPTGMSYRA GDYMAVLPIN
NSKNIRRVLK QYGLPWDAML NIKASPNTTL PTGHPISVWD VLGAYVELSQ VATRKNVAKI
ASSTPEPEVR EKIEYLAKEG FDTEILLKRR SPLDILEEYP SAALSLGDFL AMLPPMRIRQ
YSISSSPLED PSVATLTWSV LDTVSKAGES KRHLGVASNY LSSVEEGDRV HVSVKPSRGA
FHPPTDLENT PVIYICAGTG LAPFRGFVQE RALQIAAGRK LAPAYLFIGC GYPDKDALFS
DELKKWEADG AVKLYYAFSK APELSKGCRH VQDRLWEERE ELKKAFDSGA KLYVCGSSMV
GEGVSVMTKK IYAEAADLLG KTKTDEEVEI WFQGIKNDRY ASDVFT
//
