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Bifunctional cytochrome P450/NADPH--P450 reductase (Cytochrome P450foxy) (Fatty acid omega-hydroxylase) (P450foxy) [Includes: Cytochrome P450 505 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]

 C505_FUSOX              Reviewed;        1066 AA.
Q9Y8G7;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
18-JUL-2018, entry version 106.
RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000305};
AltName: Full=Cytochrome P450foxy {ECO:0000303|PubMed:11985584};
AltName: Full=Fatty acid omega-hydroxylase;
AltName: Full=P450foxy {ECO:0000303|PubMed:11985584};
Includes:
RecName: Full=Cytochrome P450 505;
EC=1.14.14.1 {ECO:0000269|PubMed:11985584, ECO:0000269|PubMed:8830036};
Includes:
RecName: Full=NADPH--cytochrome P450 reductase;
EC=1.6.2.4 {ECO:0000269|PubMed:11985584, ECO:0000269|PubMed:8830036};
Name=CYP505 {ECO:0000303|PubMed:11985584};
Fusarium oxysporum (Fusarium vascular wilt).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
Fusarium; Fusarium oxysporum species complex.
NCBI_TaxID=5507;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-99; 353-359;
362-380; 518-538; 616-626 AND 1005-1009, AND SUBCELLULAR LOCATION.
STRAIN=MT-811;
PubMed=10995755; DOI=10.1074/jbc.M005617200;
Kitazume T., Takaya N., Nakayama N., Shoun H.;
"Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a
membrane-bound eukaryotic counterpart of Bacillus megaterium
cytochrome P450BM3.";
J. Biol. Chem. 275:39734-39740(2000).
[2]
FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, SUBSTRATE
SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=MT-811;
PubMed=8830036; DOI=10.1093/oxfordjournals.jbchem.a021260;
Nakayama N., Takemae A., Shoun H.;
"Cytochrome P450foxy, a catalytically self-sufficient fatty acid
hydroxylase of the fungus Fusarium oxysporum.";
J. Biochem. 119:435-440(1996).
[3]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
PubMed=11985584; DOI=10.1046/j.1432-1033.2002.02855.x;
Kitazume T., Tanaka A., Takaya N., Nakamura A., Matsuyama S.,
Suzuki T., Shoun H.;
"Kinetic analysis of hydroxylation of saturated fatty acids by
recombinant P450foxy produced by an Escherichia coli expression
system.";
Eur. J. Biochem. 269:2075-2082(2002).
-!- FUNCTION: Functions as a fatty acid monooxygenase (PubMed:8830036,
PubMed:11985584). Catalyzes hydroxylation of fatty acids at omega-
1, omega-2 and omega-3 positions (PubMed:11985584). Shows activity
toward fatty acids with a chain length of 9-18 carbons with
optimum chain lengths of 12-14 carbons (lauric, tridecylic and
myristic acids) (PubMed:8830036, PubMed:11985584). Can also use
shorter saturated fatty acids with a chain length of 9 or 10
carbons as substrates (PubMed:11985584). Also displays a NADPH-
dependent reductase activity in the C-terminal domain, which
allows electron transfer from NADPH to the heme iron of the
cytochrome P450 N-terminal domain (PubMed:8830036,
PubMed:11985584). {ECO:0000269|PubMed:11985584,
ECO:0000269|PubMed:8830036}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000269|PubMed:11985584, ECO:0000269|PubMed:8830036}.
-!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
reduced hemoprotein. {ECO:0000269|PubMed:11985584,
ECO:0000269|PubMed:8830036}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:11985584};
Note=Binds 1 FAD. {ECO:0000250};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:11985584};
Note=Binds 1 FMN. {ECO:0000250};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:11985584};
-!- ENZYME REGULATION: Stimulated NADPH--cytochrome reductase activity
in the presence of substrate. Inhibited by fatty acid substrates
longer than 13 carbons and the degree of inhibition increases with
increasing chain length. {ECO:0000269|PubMed:11985584}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.16 mM for NADH {ECO:0000269|PubMed:8830036};
KM=0.15 mM for laurate {ECO:0000269|PubMed:8830036};
KM=3200 uM for nonanoic acid {ECO:0000269|PubMed:11985584};
KM=260 uM for decanoic acid {ECO:0000269|PubMed:11985584};
KM=160 uM for undecanoic acid {ECO:0000269|PubMed:11985584};
KM=30 uM for laurate/dodecanoic acid
{ECO:0000269|PubMed:11985584};
KM=36 uM for tridecanoic acid {ECO:0000269|PubMed:11985584};
KM=19 uM for tetradecanoic acid {ECO:0000269|PubMed:11985584};
KM=8 uM for pentadecanoic acid {ECO:0000269|PubMed:11985584};
KM=10 uM for hexadecanoic acid {ECO:0000269|PubMed:11985584};
KM=74 uM for NADH {ECO:0000269|PubMed:11985584};
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:8830036};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10995755,
ECO:0000269|PubMed:8830036}; Peripheral membrane protein
{ECO:0000269|PubMed:10995755, ECO:0000269|PubMed:8830036}.
-!- SIMILARITY: In the N-terminal section; belongs to the cytochrome
P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB030037; BAA82526.1; -; Genomic_DNA.
ProteinModelPortal; Q9Y8G7; -.
SMR; Q9Y8G7; -.
PRIDE; Q9Y8G7; -.
eggNOG; KOG0157; Eukaryota.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
BRENDA; 1.11.2.4; 2351.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-EC.
Gene3D; 1.10.630.10; -; 1.
Gene3D; 1.20.990.10; -; 1.
Gene3D; 3.40.50.360; -; 1.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR023206; Bifunctional_P450_P450_red.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR039261; FNR_nucleotide_bd.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
Pfam; PF00067; p450; 1.
PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
Direct protein sequencing; Electron transport; FAD; Flavoprotein; FMN;
Heme; Iron; Membrane; Metal-binding; Monooxygenase;
Multifunctional enzyme; NADP; Oxidoreductase; Transport.
CHAIN 1 1066 Bifunctional cytochrome P450/NADPH--P450
reductase.
/FTId=PRO_0000052210.
DOMAIN 500 641 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 676 904 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 506 511 FMN. {ECO:0000250|UniProtKB:P14779}.
NP_BIND 554 557 FMN. {ECO:0000250|UniProtKB:P14779}.
REGION 1 480 Cytochrome P450.
REGION 481 1066 NADPH-P-450 reductase.
METAL 407 407 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P14779}.
BINDING 588 588 FMN. {ECO:0000250|UniProtKB:P14779}.
BINDING 596 596 FMN. {ECO:0000250|UniProtKB:P14779}.
SITE 270 270 Important for catalytic activity.
{ECO:0000250|UniProtKB:P14779}.
SEQUENCE 1066 AA; 117926 MW; 6B8123698C223DBA CRC64;
MAESVPIPEP PGYPLIGNLG EFTSNPLSDL NRLADTYGPI FRLRLGAKAP IFVSSNSLIN
EVCDEKRFKK TLKSVLSQVR EGVHDGLFTA FEDEPNWGKA HRILVPAFGP LSIRGMFPEM
HDIATQLCMK FARHGPRTPI DTSDNFTRLA LDTLALCAMD FRFYSYYKEE LHPFIEAMGD
FLTESGNRNR RPPFAPNFLY RAANEKFYGD IALMKSVADE VVAARKASPS DRKDLLAAML
NGVDPQTGEK LSDENITNQL ITFLIAGHET TSGTLSFAMY QLLKNPEAYS KVQKEVDEVV
GRGPVLVEHL TKLPYISAVL RETLRLNSPI TAFGLEAIDD TFLGGKYLVK KGEIVTALLS
RGHVDPVVYG NDADKFIPER MLDDEFARLN KEYPNCWKPF GNGKRACIGR PFAWQESLLA
MVVLFQNFNF TMTDPNYALE IKQTLTIKPD HFYINATLRH GMTPTELEHV LAGNGATSSS
THNIKAAANL DAKAGSGKPM AIFYGSNSGT CEALANRLAS DAPSHGFSAT TVGPLDQAKQ
NLPEDRPVVI VTASYEGQPP SNAAHFIKWM EDLDGNDMEK VSYAVFACGH HDWVETFHRI
PKLVDSTLEK RGGTRLVPMG SADAATSDMF SDFEAWEDIV LWPGLKEKYK ISDEESGGQK
GLLVEVSTPR KTSLRQDVEE ALVVAEKTLT KSGPAKKHIE IQLPSAMTYK AGDYLAILPL
NPKSTVARVF RRFSLAWDSF LKIQSEGPTT LPTNVAISAF DVFSAYVELS QPATKRNILA
LAEATEDKDT IQELERLAGD AYQAEISPKR VSVLDLLEKF PAVALPISSY LAMLPPMRVR
QYSISSSPFA DPSKLTLTYS LLDAPSLSGQ GRHVGVATNF LSHLTAGDKL HVSVRASSEA
FHLPSDAEKT PIICVAAGTG LAPLRGFIQE RAAMLAAGRT LAPALLFFGC RNPEIDDLYA
EEFERWEKMG AVDVRRAYSR ATDKSEGCKY VQDRVYHDRA DVFKVWDQGA KVFICGSREI
GKAVEDVCVR LAIEKAQQNG RDVTEEMARA WFERSRNERF ATDVFD


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