C505_FUSOX
ID C505_FUSOX Reviewed; 1066 AA.
AC Q9Y8G7;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000305};
DE AltName: Full=Cytochrome P450foxy {ECO:0000303|PubMed:11985584};
DE AltName: Full=Fatty acid omega-hydroxylase;
DE AltName: Full=P450foxy {ECO:0000303|PubMed:11985584};
DE Includes:
DE RecName: Full=Cytochrome P450 505;
DE EC=1.14.14.1 {ECO:0000269|PubMed:11985584, ECO:0000269|PubMed:8830036};
DE Includes:
DE RecName: Full=NADPH--cytochrome P450 reductase;
DE EC=1.6.2.4 {ECO:0000269|PubMed:11985584, ECO:0000269|PubMed:8830036};
GN Name=CYP505 {ECO:0000303|PubMed:11985584};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-99; 353-359;
RP 362-380; 518-538; 616-626 AND 1005-1009, AND SUBCELLULAR LOCATION.
RC STRAIN=MT-811;
RX PubMed=10995755; DOI=10.1074/jbc.m005617200;
RA Kitazume T., Takaya N., Nakayama N., Shoun H.;
RT "Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a
RT membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome
RT P450BM3.";
RL J. Biol. Chem. 275:39734-39740(2000).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=MT-811;
RX PubMed=8830036; DOI=10.1093/oxfordjournals.jbchem.a021260;
RA Nakayama N., Takemae A., Shoun H.;
RT "Cytochrome P450foxy, a catalytically self-sufficient fatty acid
RT hydroxylase of the fungus Fusarium oxysporum.";
RL J. Biochem. 119:435-440(1996).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=11985584; DOI=10.1046/j.1432-1033.2002.02855.x;
RA Kitazume T., Tanaka A., Takaya N., Nakamura A., Matsuyama S., Suzuki T.,
RA Shoun H.;
RT "Kinetic analysis of hydroxylation of saturated fatty acids by recombinant
RT P450foxy produced by an Escherichia coli expression system.";
RL Eur. J. Biochem. 269:2075-2082(2002).
CC -!- FUNCTION: Functions as a fatty acid monooxygenase (PubMed:8830036,
CC PubMed:11985584). Catalyzes hydroxylation of fatty acids at omega-1,
CC omega-2 and omega-3 positions (PubMed:11985584). Shows activity toward
CC fatty acids with a chain length of 9-18 carbons with optimum chain
CC lengths of 12-14 carbons (lauric, tridecylic and myristic acids)
CC (PubMed:8830036, PubMed:11985584). Can also use shorter saturated fatty
CC acids with a chain length of 9 or 10 carbons as substrates
CC (PubMed:11985584). Also displays a NADPH-dependent reductase activity
CC in the C-terminal domain, which allows electron transfer from NADPH to
CC the heme iron of the cytochrome P450 N-terminal domain (PubMed:8830036,
CC PubMed:11985584). {ECO:0000269|PubMed:11985584,
CC ECO:0000269|PubMed:8830036}.
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:0000269|PubMed:11985584, ECO:0000269|PubMed:8830036};
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; Evidence={ECO:0000269|PubMed:11985584,
CC ECO:0000269|PubMed:8830036};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11985584};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11985584};
CC Note=Binds 1 FMN. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:11985584};
CC -!- ACTIVITY REGULATION: Stimulated NADPH--cytochrome reductase activity in
CC the presence of substrate. Inhibited by fatty acid substrates longer
CC than 13 carbons and the degree of inhibition increases with increasing
CC chain length. {ECO:0000269|PubMed:11985584}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for NADH {ECO:0000269|PubMed:8830036};
CC KM=0.15 mM for laurate {ECO:0000269|PubMed:8830036};
CC KM=3200 uM for nonanoic acid {ECO:0000269|PubMed:11985584};
CC KM=260 uM for decanoic acid {ECO:0000269|PubMed:11985584};
CC KM=160 uM for undecanoic acid {ECO:0000269|PubMed:11985584};
CC KM=30 uM for laurate/dodecanoic acid {ECO:0000269|PubMed:11985584};
CC KM=36 uM for tridecanoic acid {ECO:0000269|PubMed:11985584};
CC KM=19 uM for tetradecanoic acid {ECO:0000269|PubMed:11985584};
CC KM=8 uM for pentadecanoic acid {ECO:0000269|PubMed:11985584};
CC KM=10 uM for hexadecanoic acid {ECO:0000269|PubMed:11985584};
CC KM=74 uM for NADH {ECO:0000269|PubMed:11985584};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:8830036};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10995755,
CC ECO:0000269|PubMed:8830036}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10995755, ECO:0000269|PubMed:8830036}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000305}.
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DR EMBL; AB030037; BAA82526.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y8G7; -.
DR SMR; Q9Y8G7; -.
DR VEuPathDB; FungiDB:FOC1_g10006735; -.
DR VEuPathDB; FungiDB:FOC4_g10006868; -.
DR VEuPathDB; FungiDB:FOIG_06751; -.
DR VEuPathDB; FungiDB:FOMG_03037; -.
DR VEuPathDB; FungiDB:FOXG_04152; -.
DR VEuPathDB; FungiDB:FOZG_02961; -.
DR VEuPathDB; FungiDB:HZS61_014270; -.
DR BRENDA; 1.11.2.4; 2351.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
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; ISS:UniProtKB.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.630.10; -; 1.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 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; 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 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; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; FMN;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme;
KW NADP; Oxidoreductase; Transport.
FT CHAIN 1..1066
FT /note="Bifunctional cytochrome P450/NADPH--P450 reductase"
FT /id="PRO_0000052210"
FT DOMAIN 500..641
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 676..904
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..480
FT /note="Cytochrome P450"
FT REGION 481..1066
FT /note="NADPH-P-450 reductase"
FT BINDING 407
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:0000250|UniProtKB:P14779"
FT BINDING 506..511
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P14779"
FT BINDING 554..557
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P14779"
FT BINDING 588
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P14779"
FT BINDING 596
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P14779"
FT SITE 270
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P14779"
SQ 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
