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Reviewed, UniProtKB/Swiss-Prot Q9HDG2 (NCPR_PHACH)

Last modified November 4, 2008. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADPH--cytochrome P450 reductase
      Short name=CPR
      Short name=P450R
    EC=1.6.2.4
Gene names
Name: CPR
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesCorticialesCorticiaceaePhanerochaete

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.

Catalytic activity

NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein.

Cofactor

FAD By similarity.

FMN By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane proteinBy similarity.

Sequence similarities

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Ontologies

Keywords

   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   LigandFAD
FMN
Flavoprotein
NADP
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNADPH-hemoprotein reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 736736NADPH--cytochrome P450 reductase
PRO_0000167607

Regions

Transmembrane8 – 2417 Potential
Domain66 – 216151Flavodoxin-like
Domain269 – 546278FAD-binding FR-type
Nucleotide binding162 – 19332FMN By similarity
Nucleotide binding310 – 32112FAD By similarity
Nucleotide binding452 – 46312FAD By similarity
Nucleotide binding572 – 59019NADP By similarity
Nucleotide binding682 – 69817NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HDG2-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: AC45F12C96198AB1

FASTA73681,628
        10         20         30         40         50         60 
MAVSSSSDVI VLSVGIILAA LYLFREQIFS AAKPKTVQVP SSKAAAGGNG NPRDFIAKMK 

        70         80         90        100        110        120 
EGKKRIVIFY GSQTGTAEEY AIRLAKEAKS KFGLASLVCD PEEYDFENLD QVPEDCCVFF 

       130        140        150        160        170        180 
VMATYGEGEP TDNAVQLCQN LSDESFEFSN GEHKLPGLKY VIFGLGNKTY EHYNLISRNV 

       190        200        210        220        230        240 
DRDLQKMGAI RIGERGEGDD DKSMEEDYLE WKDGMWEAFA KAMNVEEGQG GDSPDFVVTE 

       250        260        270        280        290        300 
VFDHPEEKVY LGELSARALT RTKGIHDAKN PYPAPIIAAK ELFAPGSDRN CVHIELSTES 

       310        320        330        340        350        360 
SGITYQHGDH VGVWPSNADK EVDRLLYALG LHEKKDTVIN IESLDPALAK VPFPVPTTYA 

       370        380        390        400        410        420 
TVLRHYIDIS ALAGRQILGV LAKFAPNPEA EAVLKDLNSN KEHYQNIVAN GCMKLGEVLQ 

       430        440        450        460        470        480 
YAAGNDLHAD PTASNTTAWK IPFDIIVSSI PRLQPRYYSI SSSPKLYPNA IHATVVVLKY 

       490        500        510        520        530        540 
KSEKAPRVEE RWIYGVGSNF LLNLKYASHH DKAATLVSDD SPSEPSIVSH YPTYSIEGPR 

       550        560        570        580        590        600 
GAYKQGDVVK VPIHVRRSTF RLPTNPKSPV IMIGPGTGVA PFRGFVQERV AMARRTIEKH 

       610        620        630        640        650        660 
GPEGLADWGP IRLYYGCRRS DQDFLYKDEW PEYAKELHGK FIMRCAFSRE PPYKPDGSKI 

       670        680        690        700        710        720 
YVQDLIWEDA EQIADAILNG KGYVYICGDA KSMSKSVEET LCRILGEAKG GSAEVEGAAE 

       730 
LKLLKERNRL LLDVWS 

« Hide

References

[1]"Cytochrome P450 oxidoreductase gene and its differentially terminated cDNAs from the white rot fungus Phanerochaete chrysosporium."
Yadav J.S., Loper J.C.
Curr. Genet. 37:65-73(2000) [PubMed: 10672447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.
[2]"Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism."
Warrilow A.G.S., Lamb D.C., Kelly D.E., Kelly S.L.
Biochem. Biophys. Res. Commun. 299:189-195(2002) [PubMed: 12437968] [Abstract]
Cited for: KINETIC MECHANISM.

Cross-references

Sequence databases

AF193060 Genomic DNA. Translation: AAG31349.1.
AF193061 mRNA. Translation: AAG31350.1.
AF193062 mRNA. Translation: AAG31351.1.

3D structure databases

HSSPHSSP built from PDB template 1AMO based on UniProtKB P00388.
ModBaseSearch...

Family and domain databases

InterProIPR003097. FAD-binding_1.
IPR001094. Flavdoxin_like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. FPN_cyt_redctse.
IPR015702. NADPH_Cyt_Red.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PANTHERPTHR19384:SF17. NADPH_Cyt_Red. 1 hit.
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Entry information

Entry nameNCPR_PHACH
AccessionPrimary (citable) accession number: Q9HDG2
Secondary accession number(s): Q9HG14
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2001
Last modified: November 4, 2008
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents