Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q4WM67 (NCPR_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH--cytochrome P450 reductase
Short name=CPR
Short name=P450R
EC=1.6.2.4
Gene names
Name:cprA
ORF Names:AFUA_6G10990
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Involved in ergosterol biosynthesis By similarity.

Catalytic activity

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein. Ref.2

Cofactor

FAD By similarity.

FMN By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Cell membrane; Single-pass membrane protein By similarity. Microsome Ref.2.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 695695NADPH--cytochrome P450 reductase
PRO_0000404329

Regions

Transmembrane9 – 3123Helical; Potential
Domain66 – 221156Flavodoxin-like
Domain277 – 538262FAD-binding FR-type
Nucleotide binding72 – 765FMN By similarity
Nucleotide binding166 – 19732FMN By similarity
Nucleotide binding317 – 32812FAD By similarity
Nucleotide binding447 – 45812FAD By similarity
Nucleotide binding547 – 56519NADP By similarity
Nucleotide binding642 – 65817NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WM67 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: AB6C6208F70E9112

FASTA69576,783
        10         20         30         40         50         60 
MAQLDTLDIV VLVVLLVGSV AYFTKGSYWA VPKDPYAAAN SAMNGAAKTG KTRDIIQKME 

        70         80         90        100        110        120 
ETGKNCVIFY GSQTGTAEDY ASRLAKEGSQ RFGLKTMVAD LEDYDYENLD KFPEDKIAFF 

       130        140        150        160        170        180 
VLATYGEGEP TDNAVEFYQF ITGEDVAFES GASAEEKPLS SLKYVAFGLG NNTYEHYNAM 

       190        200        210        220        230        240 
VRHVDAALTK LGAQRIGTAG EGDDGAGTME EDFLAWKEPM WAALSESMNL QEREAVYEPV 

       250        260        270        280        290        300 
FSVIEDESLS PEDDSVYLGE PTQGHLSGSP KGPYSAHNPY IAPIVESREL FTAKDRNCLH 

       310        320        330        340        350        360 
MEIGIAGSNL TYQTGDHIAI WPTNAGVEVD RFLEVFGIEK KRHTVINIKG LDVTAKVPIP 

       370        380        390        400        410        420 
TPTTYDAAVR FYMEICAPVS RQFVSSLVPF APDEESKAEI VRLGNDKDYF HEKISNQCFN 

       430        440        450        460        470        480 
IAQALQNITS KPFSAVPFSL LIEGLNRLQP RYYSISSSSL VQKDKISITA VVESVRLPGA 

       490        500        510        520        530        540 
SHIVKGVTTN YLLALKQKQN GDPSPDPHGL TYAITGPRNK YDGIHVPVHV RHSNFKLPSD 

       550        560        570        580        590        600 
PSKPIIMVGP GTGVAPFRGF IQERAALAES GKDVGPTILF FGCRNRNEDF LYKEEWKVYQ 

       610        620        630        640        650        660 
EKLGDKLKII TAFSRETAKK VYVQHRLQEH ADLVSDLLKQ KATFYVCGDA ANMAREVNLV 

       670        680        690 
LGQIIAKSRG LPAEKGEEMV KHMRSSGSYQ EDVWS

« Hide

References

« Hide 'large scale' references
[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]"Increased cytochrome P-450 activity in Aspergillus fumigatus after xenobiotic exposure."
Baillie G.S., Hitchcock C.A., Burnet F.R.
J. Med. Vet. Mycol. 34:341-347(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAHF01000006 Genomic DNA. Translation: EAL88947.1.
RefSeqXP_750985.1. XM_745892.1.

3D structure databases

ProteinModelPortalQ4WM67.
ModBaseSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00001977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00001977; CADAFUAP00001977; CADAFUAG00001977.
GeneID3508290.
KEGGafm:AFUA_6G10990.

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000282027.
KOK00327.
OMAKPLQHRA.
OrthoDBEOG47SWP5.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000208. P450R. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCPR_ASPFU
AccessionPrimary (citable) accession number: Q4WM67
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: July 5, 2005
Last modified: May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents