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Q5BFT5 (NCPR_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:AN0595
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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 By 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 695695NADPH--cytochrome P450 reductase
PRO_0000404332

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
Q5BFT5 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: D3C5316080312354

FASTA69576,698
        10         20         30         40         50         60 
MAQLDTLDVV VLAVLLAGSI AYFTKGTFWA VAKDPYASSG PAMNGVAKAG KSRNIIEKMD 

        70         80         90        100        110        120 
ETGKNCVIFY GSQTGTAEDY ASRLAKEGSQ RFGLKTMVAD IEEYDYENLD QFPEDKVAFF 

       130        140        150        160        170        180 
VLATYGEGEP TDNAVEFYQF ITGDDVSFEG GGSAEDKPLS SLKYVAFGLG NNTYEHYNAM 

       190        200        210        220        230        240 
VRQVDAALTK LGAQRIGSAG EGDDGAGTME EDFLAWKEPM WAALSEAMNL QEREASYEPV 

       250        260        270        280        290        300 
FCVTEDESLT PEDNSVYLGE PTKGHLEGQP NGPYSAHNPY IAPIVESREL FTVKDRNCLH 

       310        320        330        340        350        360 
MEISIAGTNL TYQTGDHIAI WPTNAGAEVD RFLNVFGLEE KRHSVINIKG IDVTAKVPIP 

       370        380        390        400        410        420 
TPTTYDAAVR YYMEVCAPVS RQFVSTLAAF APDEETKTEI VRLGSDKDYF HEKITNQCFN 

       430        440        450        460        470        480 
IAQALQSITS KPFSNVPFSL LIEGLNKIQP RYYSISSSSL VQKDKISITA VVESTRLPGA 

       490        500        510        520        530        540 
THIVKGVTTN YLLALKQKQN GDPSPDPHGQ TYAINGPRNK YDGIHVPVHV RHSNFKLPSD 

       550        560        570        580        590        600 
PSRPIIMIGP GTGVAPFRGF IQERAALAAR GEKVGPTVLF FGCRKRDEDF LYKDEWKVFQ 

       610        620        630        640        650        660 
DQLGDSLKII TAFSRESEKK VYVQHRLKEH AELVSDLLKQ KATFYVCGDA ANMAREVNLV 

       670        680        690 
LGQIIAAQRG LPAEKGEEMV KHMRSSGSYQ EDVWS

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000007 Genomic DNA. Translation: EAA66694.1.
BN001308 Genomic DNA. Translation: CBF89160.1.
RefSeqXP_658199.1. XM_653107.1.

3D structure databases

ProteinModelPortalQ5BFT5.
ModBaseSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00002079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00002079; CADANIAP00002079; CADANIAG00002079.
GeneID2876366.
KEGGani:AN0595.2.

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000282027.
KOK00327.
OMARDENDAS.
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_EMENI
AccessionPrimary (citable) accession number: Q5BFT5
Secondary accession number(s): C8VSB1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: April 26, 2005
Last modified: April 3, 2013
This is version 56 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