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P50126 (NCPR_CANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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

Names and origin

Protein namesRecommended name:
NADPH--cytochrome P450 reductase

Short name=CPR
Short name=P450R
EC=1.6.2.4
Gene names
Name:NCP1
OrganismCandida maltosa (Yeast)
Taxonomic identifier5479 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
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.

FMN.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein.

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 – 680680NADPH--cytochrome P450 reductase
PRO_0000167605

Regions

Transmembrane8 – 2417Helical; Potential
Domain60 – 204145Flavodoxin-like
Domain264 – 509246FAD-binding FR-type
Nucleotide binding149 – 18032FMN By similarity
Nucleotide binding304 – 31512FAD By similarity
Nucleotide binding435 – 44612FAD By similarity
Nucleotide binding532 – 55019NADP By similarity
Nucleotide binding628 – 64417NADP By similarity

Experimental info

Sequence conflict301Q → E in BAA04997. Ref.2
Sequence conflict170 – 1712LL → VF in BAA04997. Ref.2
Sequence conflict5651F → P in BAA04997. Ref.2
Sequence conflict5791Q → K in BAA04997. Ref.2
Sequence conflict6191V → L in BAA04997. Ref.2
Sequence conflict6641E → D in BAA04997. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P50126 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E396F81E169705C9

FASTA68077,131
        10         20         30         40         50         60 
MALDKLDLYV IIVLAVAVAA YFAKNQFLDQ PQDTGFLSND TAGGNSRDIL ETLKKNNKNT 

        70         80         90        100        110        120 
LLLFGSQTGT AEDYANKLSR EIHSRFGLKT MVADFADYDW DNFGDIPNDI LVFFIVATYG 

       130        140        150        160        170        180 
EGEPTDNADE FHTWLTDEAD TLSTLRYTVF GLGNSTYEFY NAIGRKFDRL LEEKGGERFA 

       190        200        210        220        230        240 
DYGEGDDGTG TLDEDFLTWK DNVFDTLKND LNFEERELKY EPNVKLTERD DLTVDDSEVS 

       250        260        270        280        290        300 
LGEPNKKYIQ SEEIDLTKGP FDHTHPYLAK ISKTRELFAS KERNCVHVEF DVSESNLKYT 

       310        320        330        340        350        360 
TGDHLAVWPS NSDENIAKFI KCFGLDDKIN TVFELKALDS TYQIPFPNPI TYGAVVRHHL 

       370        380        390        400        410        420 
EISGPVSRQF FLAIAGFAPD EETKKTFTRI GNDKQEFANK ITRKKLNVAD ALLFASNGRP 

       430        440        450        460        470        480 
WSDVPFEFII ENVPHLQPRY YSISSSSLSE KQTINITAVV EVEEEADGRA VTGVVTNLLK 

       490        500        510        520        530        540 
NIEIEQNKTG EKPVVHYDLS GPRNKFNKFK LPVHVRRSNF KLPKNTTTPV ILIGPGTGVA 

       550        560        570        580        590        600 
PLRGFVRERV QQVKNGVNVG KTVLFYGCRN EHDDFLYKQE WSEYASVLGE NFEMFTAFSR 

       610        620        630        640        650        660 
QDPSKKVYVQ DKIAENSKVV NDLLNEGAII YVCGDASRMA RDVQSTIAKI VAKHREIQED 

       670        680 
KAVELVKSWK VQNRYQEDVW 

« Hide

References

[1]"Candida maltosa NADPH-cytochrome P450 reductase: cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum."
Kaergel E., Honeck H., Vogel F., Boehmer A., Schunk W.-H.
Yeast 12:333-348(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: EH15.
[2]"Evidence that the expression of the gene for NADPH-cytochrome P-450 reductase is n-alkane-inducible in Candida maltosa."
Ohkuma M., Masuda Y., Park S.M., Ohtomo R., Ohta A., Takagi M.
Biosci. Biotechnol. Biochem. 59:1328-1330(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76226 mRNA. Translation: CAA53812.1.
D25327 Genomic DNA. Translation: BAA04997.1.
PIRS63698.
S63895.

3D structure databases

ProteinModelPortalP50126.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
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.
SUPFAMSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCPR_CANMA
AccessionPrimary (citable) accession number: P50126
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 90 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