ID A0A0J9WC46_FUSO4 Unreviewed; 1074 AA.
AC A0A0J9WC46;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=FOXG_17221 {ECO:0000313|EMBL:KNB20106.1};
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428 {ECO:0000313|EMBL:KNB20106.1, ECO:0000313|Proteomes:UP000009097};
RN [1] {ECO:0000313|EMBL:KNB20106.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4287 {ECO:0000313|EMBL:KNB20106.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNB20106.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 {ECO:0000313|EMBL:KNB20106.1};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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 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 -!- 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; DS231740; KNB20106.1; -; Genomic_DNA.
DR RefSeq; XP_018258151.1; XM_018397239.1.
DR AlphaFoldDB; A0A0J9WC46; -.
DR GeneID; 28958012; -.
DR KEGG; fox:FOXG_17221; -.
DR VEuPathDB; FungiDB:FOXG_17221; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000009097; 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 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; 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 PIRSF; PIRSF000209; Bifunctional_P450_P450R; 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 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 Heme {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW Iron {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
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 Reference proteome {ECO:0000313|Proteomes:UP000009097};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000209}.
FT DOMAIN 508..649
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 688..918
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 414
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 1074 AA; 120037 MW; 153AAF16E2331AA5 CRC64;
MALSCDESTP IPEPRGLPFL GNVTEFRSED SLQDLDRLHD TYGEIYRLRF PKVGSCVIVG
SQKLVNELCD EKRFRKAIQA ELAEIRLAAG DGLFTAREGE VSWDIAHRVL MPVFGPTAIR
SMFDEMYDVV SQMTLKWARY GPTSPISASE DFTRLALDTI ALCSMGYRFN SFYKDTTHPF
VQSMSDSLVE LGNRSLRPSW ARIFYRSSER KLAKDINFMR TTSEDLIKAR KADPNADQRK
DLLAAMMNGV DPRTGSRMDD ESIINNLLTF LIAGHETTSG TLSFAFYSML KNPDAYLKAQ
QEVDSIMGRD PITVDKLFQL KYVPAVLRET LRQCSPIPGI TLEAREDTLL DGKYHIRKGE
AVAAIFSKSH LDPLVYGADA KEFKPERMMD ENFDRLQQEF PNCWKPFGNG VRACIGRAFA
WQEMLLATSM LLQNFDFYLD DPLYKLKIAE TLTIKPKDFL MGASLRHNMT PLDLESHLRG
TNNKQGIPAA HSQSPPSTIK ASIAATPISI YYGSNSGTCE ILARRLASNA SSHGFSVMVI
DTLDTARNRL PQDHPVVIFV ASYEGQPPDN AAHFVNWIQS MTGNEVQKVH YVVFGVGNSE
WRQTFHRIPK LIDDELGKRG GERLVTLGLT NVAEKDPFLD FEIWESKELW PALEKKYPDV
TGGTPEALVG SMGLSVDISV SRASALRKSV KEAIVTGVRD LAAPGLPRKR HIEMKLPSGC
SYEVGDYLEV LPMNPRDAVT RALRRFKLPW DAVLTIAGSE ITSLPIGIPV SAWDVLSSYV
ELAFLSTRKD TLVLASYAQS EKVRTEIELL ASDVKFKSEI EDKRVSILDL LERFPSVELP
IATYLGMLQP IRTRQYSISS SPLKDPSHAT LTYSVLETPS LSGQGLYMGV ASNFLASLKP
DDRLQVSIRR SNIAFHLPLA PDTTPIICVA AGAGLAPFRG FIQQRSIQMK ADRILAPALL
IFGCRRRDDD LYREEFDAWE GEGAVVVKRA YSRDAKLTAG CKYVQDRVIE QQEYIRKLWN
QGGNVYVCGS RQVGDAVEGA LGSILSGVQG GDREDGKRFL DNFRNKRFVM DIFS
//
