Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional cytochrome P450/NADPH--P450 reductase

Gene

CYP505

Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Catalytic activityi

RH + [reduced NADPH--hemoprotein reductase] + O2 = ROH + [oxidized NADPH--hemoprotein reductase] + H2O.2 Publications
NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.2 Publications

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=0.16 mM for NADH1 Publication
  2. KM=0.15 mM for laurate1 Publication
  3. KM=3200 µM for nonanoic acid1 Publication
  4. KM=260 µM for decanoic acid1 Publication
  5. KM=160 µM for undecanoic acid1 Publication
  6. KM=30 µM for laurate/dodecanoic acid1 Publication
  7. KM=36 µM for tridecanoic acid1 Publication
  8. KM=19 µM for tetradecanoic acid1 Publication
  9. KM=8 µM for pentadecanoic acid1 Publication
  10. KM=10 µM for hexadecanoic acid1 Publication
  11. KM=74 µM for NADH1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei182 – 1821Fatty acidBy similarity
    Binding sitei265 – 2651Fatty acidBy similarity
    Sitei270 – 2701Important for catalytic activityBy similarity
    Metal bindingi407 – 4071Iron (heme axial ligand)By similarity
    Binding sitei445 – 4451Fatty acidBy similarity
    Binding sitei588 – 5881FMNBy similarity
    Binding sitei596 – 5961FMNBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi506 – 5116FMNBy similarity
    Nucleotide bindingi554 – 5574FMNBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BRENDAi1.11.2.4. 2351.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional cytochrome P450/NADPH--P450 reductaseCurated
    Alternative name(s):
    Cytochrome P450foxy1 Publication
    Fatty acid omega-hydroxylase
    P450foxy1 Publication
    Including the following 2 domains:
    Cytochrome P450 505 (EC:1.14.14.12 Publications)
    NADPH--cytochrome P450 reductase (EC:1.6.2.42 Publications)
    Gene namesi
    Name:CYP5051 Publication
    OrganismiFusarium oxysporum (Fusarium vascular wilt)
    Taxonomic identifieri5507 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10661066Bifunctional cytochrome P450/NADPH--P450 reductasePRO_0000052210Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5507.FOXG_04152P0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y8G7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini500 – 641142Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini676 – 904229FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 480480Cytochrome P450Add
    BLAST
    Regioni22 – 309Fatty acid bindingBy similarity
    Regioni76 – 8813Fatty acid bindingBy similarityAdd
    BLAST
    Regioni330 – 3323Fatty acid bindingBy similarity
    Regioni481 – 1066586NADPH-P-450 reductaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the cytochrome P450 family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG0157. Eukaryota.
    KOG1158. Eukaryota.
    COG0369. LUCA.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProiIPR023206. Bifunctional_P450_P450_red.
    IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    IPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR008254. Flavodoxin/NO_synth.
    IPR029039. Flavoprotein-like_dom.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF00067. p450. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000209. Bifunctional_P450_P450R. 1 hit.
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    SSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y8G7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAESVPIPEP PGYPLIGNLG EFTSNPLSDL NRLADTYGPI FRLRLGAKAP
    60 70 80 90 100
    IFVSSNSLIN EVCDEKRFKK TLKSVLSQVR EGVHDGLFTA FEDEPNWGKA
    110 120 130 140 150
    HRILVPAFGP LSIRGMFPEM HDIATQLCMK FARHGPRTPI DTSDNFTRLA
    160 170 180 190 200
    LDTLALCAMD FRFYSYYKEE LHPFIEAMGD FLTESGNRNR RPPFAPNFLY
    210 220 230 240 250
    RAANEKFYGD IALMKSVADE VVAARKASPS DRKDLLAAML NGVDPQTGEK
    260 270 280 290 300
    LSDENITNQL ITFLIAGHET TSGTLSFAMY QLLKNPEAYS KVQKEVDEVV
    310 320 330 340 350
    GRGPVLVEHL TKLPYISAVL RETLRLNSPI TAFGLEAIDD TFLGGKYLVK
    360 370 380 390 400
    KGEIVTALLS RGHVDPVVYG NDADKFIPER MLDDEFARLN KEYPNCWKPF
    410 420 430 440 450
    GNGKRACIGR PFAWQESLLA MVVLFQNFNF TMTDPNYALE IKQTLTIKPD
    460 470 480 490 500
    HFYINATLRH GMTPTELEHV LAGNGATSSS THNIKAAANL DAKAGSGKPM
    510 520 530 540 550
    AIFYGSNSGT CEALANRLAS DAPSHGFSAT TVGPLDQAKQ NLPEDRPVVI
    560 570 580 590 600
    VTASYEGQPP SNAAHFIKWM EDLDGNDMEK VSYAVFACGH HDWVETFHRI
    610 620 630 640 650
    PKLVDSTLEK RGGTRLVPMG SADAATSDMF SDFEAWEDIV LWPGLKEKYK
    660 670 680 690 700
    ISDEESGGQK GLLVEVSTPR KTSLRQDVEE ALVVAEKTLT KSGPAKKHIE
    710 720 730 740 750
    IQLPSAMTYK AGDYLAILPL NPKSTVARVF RRFSLAWDSF LKIQSEGPTT
    760 770 780 790 800
    LPTNVAISAF DVFSAYVELS QPATKRNILA LAEATEDKDT IQELERLAGD
    810 820 830 840 850
    AYQAEISPKR VSVLDLLEKF PAVALPISSY LAMLPPMRVR QYSISSSPFA
    860 870 880 890 900
    DPSKLTLTYS LLDAPSLSGQ GRHVGVATNF LSHLTAGDKL HVSVRASSEA
    910 920 930 940 950
    FHLPSDAEKT PIICVAAGTG LAPLRGFIQE RAAMLAAGRT LAPALLFFGC
    960 970 980 990 1000
    RNPEIDDLYA EEFERWEKMG AVDVRRAYSR ATDKSEGCKY VQDRVYHDRA
    1010 1020 1030 1040 1050
    DVFKVWDQGA KVFICGSREI GKAVEDVCVR LAIEKAQQNG RDVTEEMARA
    1060
    WFERSRNERF ATDVFD
    Length:1,066
    Mass (Da):117,926
    Last modified:November 1, 1999 - v1
    Checksum:i6B8123698C223DBA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB030037 Genomic DNA. Translation: BAA82526.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB030037 Genomic DNA. Translation: BAA82526.1.

    3D structure databases

    ProteinModelPortaliQ9Y8G7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5507.FOXG_04152P0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiKOG0157. Eukaryota.
    KOG1158. Eukaryota.
    COG0369. LUCA.

    Enzyme and pathway databases

    BRENDAi1.11.2.4. 2351.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProiIPR023206. Bifunctional_P450_P450_red.
    IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    IPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR008254. Flavodoxin/NO_synth.
    IPR029039. Flavoprotein-like_dom.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF00067. p450. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000209. Bifunctional_P450_P450R. 1 hit.
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    SSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3."
      Kitazume T., Takaya N., Nakayama N., Shoun H.
      J. Biol. Chem. 275:39734-39740(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-99; 353-359; 362-380; 518-538; 616-626 AND 1005-1009, SUBCELLULAR LOCATION.
      Strain: MT-811.
    2. "Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the fungus Fusarium oxysporum."
      Nakayama N., Takemae A., Shoun H.
      J. Biochem. 119:435-440(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: MT-811.
    3. "Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system."
      Kitazume T., Tanaka A., Takaya N., Nakamura A., Matsuyama S., Suzuki T., Shoun H.
      Eur. J. Biochem. 269:2075-2082(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.

    Entry informationi

    Entry nameiC505_FUSOX
    AccessioniPrimary (citable) accession number: Q9Y8G7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: November 1, 1999
    Last modified: May 11, 2016
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.