ID W9NMQ6_FUSOX Unreviewed; 960 AA.
AC W9NMQ6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOVG_16777 {ECO:0000313|EMBL:EXA32011.1};
OS Fusarium oxysporum f. sp. pisi HDV247.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1080344 {ECO:0000313|EMBL:EXA32011.1};
RN [1] {ECO:0000313|EMBL:EXA32011.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HDV247 {ECO:0000313|EMBL:EXA32011.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum HDV247.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXA32011.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HDV247 {ECO:0000313|EMBL:EXA32011.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum HDV247.";
RL Submitted (MAY-2012) 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|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; JH651003; EXA32011.1; -; Genomic_DNA.
DR AlphaFoldDB; W9NMQ6; -.
DR HOGENOM; CLU_001570_7_0_1; -.
DR Proteomes; UP000030751; Unassembled WGS sequence.
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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 392..535
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 570..801
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 960 AA; 107692 MW; 6C444A622184CA66 CRC64;
MPAFGPLSIQ HMFDEMHDIA SQLALKWARY GPNSPIMATD DFTRLTLDTL ALCSMGYRFN
SYYSPVLHPF IEAMGEFLTE AGEKPRRLPL PGIVYRDRDR KYQQDIEIMR NTAREVLDAR
KADGNTRKDL LAAMLEGVDT KTGKKMTDES IMDNLITFLI AGHETTSGLL SFAFYQLLTH
PDAYQLAQNE VDRVVGKGPI QVEHLSKLPY LNGVLRETLR LNATIPLFTV EAFEDTLLGN
KYPVKAGETI INLLAKSQLD PTVFGDDADK FRPERMFDEN FARMNKEFPN SWKPFGNGMR
ACIGRPFAWQ ESLLVMVMLL QNFNFVLDPN YHLGFKQTLT IKPKDMYMRA ILRDNLTPTT
LERRLAGLPV LAKGEANGTN GESADAEDGI PITILYGSNS GTCESLAQRV ATDAAQHGFR
VTKIDCLDMA NGNLPVDQPV VIITASYEGQ PPDNAGHFVA WVEKTAQEDK PFKDVSYAVF
GCGHKDWVLT FHRIPKLVDR TLAKHGATRL VDMGLADVSQ NMVFSDFETW EDNILWPALE
KRYKPDCKTM LTDKRLSVKS CSFRTLSLRQ DVREATVVST KTLTSNIDVK SKKKHIEIQL
PEGTGYTAGD YLAVLPINPH EIVRRALRRF RLPMDAHLEI SSSTPAALPT DTSVSAMDVL
SSYVELSQPA TKRNLLIIAE AASNVETKAA LTSLSQERYV EEISNKRVSV LEILERYPSV
ELSIGDFLQM LPSIRIRQYS ISSSPLWNQA HATITFSVLK GPAFSGHGTY NGVATSYLDS
LAEGDTLQVA IRSSPAAFSL PSNPECSPII CVAAGSGLAP FRGFIQQRAI IYDSGRTLAP
ALLFFGCRAP DQDDLYRDEF DSWQRLGAVQ VRRAYSRHRE GCRYVQDRIW QDKEDFIELW
NKGAMVYVCG SRAMADSVKE VMIKVKTEIE KRSGGDIGLD EARKWFDEQR NVRYVMDVFD
//
