Bifunctional P-450:NADPH-P450 reductase - Fusarium oxysporum (Panama disease fungus)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Bifunctional P-450:NADPH-P450 reductase

Alternative name(s):
Cytochrome P450foxy
Fatty acid omega-hydroxylase

Including the following 2 domains:

Cytochrome P450 505
EC=1.14.14.1
NADPH--cytochrome P450 reductase
EC=1.6.2.4

Gene names

Name:

CYP505

Organism

Fusarium oxysporum (Panama disease fungus)

Taxonomic identifier

5507 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › mitosporic Nectriaceae › Fusarium › Fusarium oxysporum species complex

Protein attributes

Sequence length	1066 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as a fatty acid monooxygenase. Shows highest activity toward fatty acids with a chain length of 12-14 carbons. The reductase domain is required for electron transfer from NADP to cytochrome P450. Ref.2
Catalytic activity	RH + reduced flavoprotein + O₂ = ROH + oxidized flavoprotein + H₂O. NADPH + n oxidized hemoprotein = NADP⁺ + n reduced hemoprotein.
Cofactor	Binds 1 FAD By similarity. Binds 1 FMN By similarity. Heme group By similarity.
Subcellular location	Membrane; Peripheral membrane protein Ref.1 Ref.2.
Sequence similarities	In the N-terminal section; belongs to the cytochrome P450 family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Membrane
Ligand	FAD FMN Flavoprotein Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1066

1066

Bifunctional P-450:NADPH-P450 reductase

PRO_0000052210

Regions

Domain

500 – 641

142

Flavodoxin-like

Domain

676 – 904

229

FAD-binding FR-type

Region

1 – 480

480

Cytochrome P450

Region

481 – 1066

586

NADPH-P-450 reductase

Sites

Metal binding

407

1

Iron (heme axial ligand) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y8G7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 6B8123698C223DBA
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FASTA

1,066

117,926

        10         20         30         40         50         60 
MAESVPIPEP PGYPLIGNLG EFTSNPLSDL NRLADTYGPI FRLRLGAKAP IFVSSNSLIN 

        70         80         90        100        110        120 
EVCDEKRFKK TLKSVLSQVR EGVHDGLFTA FEDEPNWGKA HRILVPAFGP LSIRGMFPEM 

       130        140        150        160        170        180 
HDIATQLCMK FARHGPRTPI DTSDNFTRLA LDTLALCAMD FRFYSYYKEE LHPFIEAMGD 

       190        200        210        220        230        240 
FLTESGNRNR RPPFAPNFLY RAANEKFYGD IALMKSVADE VVAARKASPS DRKDLLAAML 

       250        260        270        280        290        300 
NGVDPQTGEK LSDENITNQL ITFLIAGHET TSGTLSFAMY QLLKNPEAYS KVQKEVDEVV 

       310        320        330        340        350        360 
GRGPVLVEHL TKLPYISAVL RETLRLNSPI TAFGLEAIDD TFLGGKYLVK KGEIVTALLS 

       370        380        390        400        410        420 
RGHVDPVVYG NDADKFIPER MLDDEFARLN KEYPNCWKPF GNGKRACIGR PFAWQESLLA 

       430        440        450        460        470        480 
MVVLFQNFNF TMTDPNYALE IKQTLTIKPD HFYINATLRH GMTPTELEHV LAGNGATSSS 

       490        500        510        520        530        540 
THNIKAAANL DAKAGSGKPM AIFYGSNSGT CEALANRLAS DAPSHGFSAT TVGPLDQAKQ 

       550        560        570        580        590        600 
NLPEDRPVVI VTASYEGQPP SNAAHFIKWM EDLDGNDMEK VSYAVFACGH HDWVETFHRI 

       610        620        630        640        650        660 
PKLVDSTLEK RGGTRLVPMG SADAATSDMF SDFEAWEDIV LWPGLKEKYK ISDEESGGQK 

       670        680        690        700        710        720 
GLLVEVSTPR KTSLRQDVEE ALVVAEKTLT KSGPAKKHIE IQLPSAMTYK AGDYLAILPL 

       730        740        750        760        770        780 
NPKSTVARVF RRFSLAWDSF LKIQSEGPTT LPTNVAISAF DVFSAYVELS QPATKRNILA 

       790        800        810        820        830        840 
LAEATEDKDT IQELERLAGD AYQAEISPKR VSVLDLLEKF PAVALPISSY LAMLPPMRVR 

       850        860        870        880        890        900 
QYSISSSPFA DPSKLTLTYS LLDAPSLSGQ GRHVGVATNF LSHLTAGDKL HVSVRASSEA 

       910        920        930        940        950        960 
FHLPSDAEKT PIICVAAGTG LAPLRGFIQE RAAMLAAGRT LAPALLFFGC RNPEIDDLYA 

       970        980        990       1000       1010       1020 
EEFERWEKMG AVDVRRAYSR ATDKSEGCKY VQDRVYHDRA DVFKVWDQGA KVFICGSREI 

      1030       1040       1050       1060 
GKAVEDVCVR LAIEKAQQNG RDVTEEMARA WFERSRNERF ATDVFD

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References

[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.
Strain: MT-811.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB030037 Genomic DNA. Translation: BAA82526.1.
3D structure databases
ProteinModelPortal	Q9Y8G7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.630.10. 1 hit. 1.20.990.10. 1 hit.
InterPro	IPR023206. 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. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. PF00067. p450. 1 hit. [Graphical view]
PIRSF	PIRSF000209. Bifunctional_P450_P450R. 1 hit.
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C505_FUSOX

Accession

Primary (citable) accession number: Q9Y8G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families